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Conserved domains on  [gi|2500175490|ref|WP_281192831|]
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phosphotransferase [Erysipelothrix rhusiopathiae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
60-287 5.51e-114

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


:

Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 338.73  E-value: 5.51e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490  60 DNAIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQFYYLEDKYNVKIVVNDDYYRY 139
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDKYGVKLIYNPDYAEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 140 NNTSTLMLVLDQLKNTYICSSDNYFVENVFNPYEYKTTYPVqVHTTHESGEYYADFTDEGLITQIGIGSGTYNCMVGHVF 219
Cdd:COG4750    81 NNISSLYLVRDKLGNTYICSSDNYLTENPFEKYEYKSYYSA-VYKEGETDEWCVKTNRDGRITKIEIGGKDGWIMLGHSY 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500175490 220 FDQAFSHDFGELLKQEYPKEETKSKLWEKVYVEHMDQFTMYAEVYSKDIIKEFDSLEELQAFDASYLE 287
Cdd:COG4750   160 WDKEDSKKFKEILEEEYEDPETRDLYWEDIYMDHIDELDMYARKYPAGDIYEFDSLDELREFDPSYLE 227
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
311-506 1.17e-38

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


:

Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 139.23  E-value: 1.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 311 IVPVKDGLTNLSLKFEYDGKAYIYRHPGVGTDEYINRKSEFFAQQKAKKLGFDDSYIYMDPEKGWKLSYFIDQARKL--D 388
Cdd:cd05151     3 IEPLKGGLTNKNYLVEVAGKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEVIYFDPETGVKITEFIEGATLLtnD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 389 YHQWDEVKQALEMIKDIHDQQLsgefefniwnkscdfigklsqqdkdvfsdfdelfkliesvkkysdKDNVPlrlCHCDF 468
Cdd:cd05151    83 FSDPENLERIAALLRKLHSSPL---------------------------------------------EDLVL---CHNDL 114
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2500175490 469 YDPNILFSGNDLYLIDWEYAGVDDPGVDIGTFIACSDY 506
Cdd:cd05151   115 VPGNFLLDDDRLYLIDWEYAGMNDPLFDLAALFSENNL 152
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
405-565 3.39e-27

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


:

Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 107.56  E-value: 3.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 405 IHDQQLSGEFefniwnkscDFIGKLSQQDKDVFSDFDELFKLIESVKKYSDKDNVPLRLCHCDFYDPNILFSGND-LYLI 483
Cdd:COG0510     2 LHASPALLRF---------DLFARLERYLALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGrLYLI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 484 DWEYAGVDDPGVDIGTFIACSDYTYEEAMQVLELYNKTPMDASMQRHFIAYIAIASYYWFVWAIF---QESNGAAvGEYL 560
Cdd:COG0510    73 DWEYAGLGDPAFDLAALLVEYGLSPEQAEELLEAYGFGRPTEELLRRLRAYRALADLLWALWALVraaQEANGDL-LKYL 151

                  ....*
gi 2500175490 561 TIWYN 565
Cdd:COG0510   152 LRRLE 156
 
Name Accession Description Interval E-value
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
60-287 5.51e-114

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 338.73  E-value: 5.51e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490  60 DNAIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQFYYLEDKYNVKIVVNDDYYRY 139
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDKYGVKLIYNPDYAEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 140 NNTSTLMLVLDQLKNTYICSSDNYFVENVFNPYEYKTTYPVqVHTTHESGEYYADFTDEGLITQIGIGSGTYNCMVGHVF 219
Cdd:COG4750    81 NNISSLYLVRDKLGNTYICSSDNYLTENPFEKYEYKSYYSA-VYKEGETDEWCVKTNRDGRITKIEIGGKDGWIMLGHSY 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500175490 220 FDQAFSHDFGELLKQEYPKEETKSKLWEKVYVEHMDQFTMYAEVYSKDIIKEFDSLEELQAFDASYLE 287
Cdd:COG4750   160 WDKEDSKKFKEILEEEYEDPETRDLYWEDIYMDHIDELDMYARKYPAGDIYEFDSLDELREFDPSYLE 227
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
62-282 2.18e-49

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 170.88  E-value: 2.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQF-YYLEDKYNVKIVVNDDYYRYN 140
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIeELLKKYPNIKFVYNPDYAETN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 141 NTSTLMLVLDQLK-NTYICSSDNYFVENVFNPYEYKTTYPVQV--HTTHESGEYYADFTDEGL----ITQIGIGSGTYNC 213
Cdd:cd02523    81 NIYSLYLARDFLDeDFLLLEGDVVFDPSILERLLSSPADNAILvdKKTKEWEDEYVKDLDDAGvllgIISKAKNLEEIQG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 214 -MVGHVFFDQAFSHDFGELLKqEYPKEETKSKLWEKVYVEHMDQFTMYAEVYSKDIIKEFDSLEELQAFD 282
Cdd:cd02523   161 eYVGISKFSPEDADRLAEALE-ELIEAGRVNLYYEDALQRLISEEGVKVKDISDGFWYEIDDLEDLERAE 229
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
311-506 1.17e-38

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 139.23  E-value: 1.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 311 IVPVKDGLTNLSLKFEYDGKAYIYRHPGVGTDEYINRKSEFFAQQKAKKLGFDDSYIYMDPEKGWKLSYFIDQARKL--D 388
Cdd:cd05151     3 IEPLKGGLTNKNYLVEVAGKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEVIYFDPETGVKITEFIEGATLLtnD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 389 YHQWDEVKQALEMIKDIHDQQLsgefefniwnkscdfigklsqqdkdvfsdfdelfkliesvkkysdKDNVPlrlCHCDF 468
Cdd:cd05151    83 FSDPENLERIAALLRKLHSSPL---------------------------------------------EDLVL---CHNDL 114
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2500175490 469 YDPNILFSGNDLYLIDWEYAGVDDPGVDIGTFIACSDY 506
Cdd:cd05151   115 VPGNFLLDDDRLYLIDWEYAGMNDPLFDLAALFSENNL 152
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
405-565 3.39e-27

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 107.56  E-value: 3.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 405 IHDQQLSGEFefniwnkscDFIGKLSQQDKDVFSDFDELFKLIESVKKYSDKDNVPLRLCHCDFYDPNILFSGND-LYLI 483
Cdd:COG0510     2 LHASPALLRF---------DLFARLERYLALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGrLYLI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 484 DWEYAGVDDPGVDIGTFIACSDYTYEEAMQVLELYNKTPMDASMQRHFIAYIAIASYYWFVWAIF---QESNGAAvGEYL 560
Cdd:COG0510    73 DWEYAGLGDPAFDLAALLVEYGLSPEQAEELLEAYGFGRPTEELLRRLRAYRALADLLWALWALVraaQEANGDL-LKYL 151

                  ....*
gi 2500175490 561 TIWYN 565
Cdd:COG0510   152 LRRLE 156
GntI_guanitoxin NF041256
guanitoxin biosynthesis pre-guanitoxin N-oxide kinase GntI;
312-549 9.91e-19

guanitoxin biosynthesis pre-guanitoxin N-oxide kinase GntI;


Pssm-ID: 469156 [Multi-domain]  Cd Length: 279  Bit Score: 86.45  E-value: 9.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 312 VPVKD-GLTNLSLKFEYDGKAYIYRHPGVGTDEY-INRKSEFFAQQKAKKLGFDDSYIYMDPEKGWKLSYFID--QARKL 387
Cdd:NF041256   18 VEIQDsGLTNRNYRVENGGEKFVVRISGGNSNLLgINRHAELIALKAVAAMGIGPEVLAFDPPEGHLVTRFIEgrHFSLE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 388 DYHQWDEVKQALEMIKDIHdQQLSGEFEFNIWNKSCDFIGKLSQQDKDVFSDFDELFKLIESVKK----YSDKdnvPLRL 463
Cdd:NF041256   98 DLTQPENIDRIAQLLKQVH-SGPPIPGRFSPYRDIEDYIQTAFARGIDLPPPLERIEGLLRNIERkrgaFPDR---FEGL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 464 CHCDFYDPNILFSGNDLYLIDWEYAGVDDPGVDIGTFIACSDYTYEEAMQVLELYNKTpMDASMQRHFIAYIAIASYYWF 543
Cdd:NF041256  174 CHNDLFANNFIDDGGSIRLLDWEYAGMGDILFDLANFSMNQSLDREGDKILLESYFGK-VSQALLAALNLMKFVVIFWEA 252

                  ....*.
gi 2500175490 544 VWAIFQ 549
Cdd:NF041256  253 MWGVLQ 258
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
330-522 6.90e-15

Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. This alignment covers the protein kinase portion of the protein. The divergence of this family makes it very difficult to create a model that specifically predicts choline/ethanolamine kinases only. However if [add Pfam ID here for Choline_kinase_C] is also present then it is definitely a member of this family.


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 73.85  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 330 KAYIYRHPGVGTDEYINRKSEF--FAQQKAKKLG------FDDSYIYMdpekgwklsyFIdQARKLDYHQ---WDEVKQA 398
Cdd:pfam01633   3 RKVLLRIYGPGTELLINREDEIvnFALLSERGLGpklygfFPNGRIEE----------FI-PSRTLSTEDlrdPEISKLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 399 LEMIKDIHDQQLSGEFEFNIWN---------KSCDFIGKLSQQDKDVFSDFDELFKLIESVKKYSDKDNVPLRLCHCDFY 469
Cdd:pfam01633  72 AKRLAELHSLEMPGKKSPSLWKtmrkwlsllKNLGAPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQ 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2500175490 470 DPNILF--SGNDLYLIDWEYAGVDDPGVDIGTFIA--CSDYTYEEAMQVLElYNKTP 522
Cdd:pfam01633 152 SGNILLlnETKRLVLIDFEYASYNYRGFDIANHFCewAGDYHDPTPFFKCD-YSLYP 207
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
433-547 1.34e-10

Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline kinase, ethanolamine kinase, and similar proteins. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270923 [Multi-domain]  Cd Length: 229  Bit Score: 61.52  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 433 DKDVFSDFDELFKLIESVKKYSDKDNVPLRLCHCDFYDPNILFSGND--LYLIDWEYAGVDDPGVDIGTFIACS--DYTY 508
Cdd:cd14021    84 TTDELRNPSVLTSIAKLLAKFHKIKTPPVVFCHNDLQENNILLTNDQdgLRLIDFEYSGFNYRGYDIANFFNESmiDYDH 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500175490 509 EEAMQVLELYNKTPmDASMQRHFIA-YI--------------------------AIAS-YYWFVWAI 547
Cdd:cd14021   164 PEPPYFKIYKENYI-SEEEKRLFVSvYLseyleknvlpsldklveqflqeveifTLGShLYWGLWSI 229
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
62-138 5.10e-10

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 58.36  E-value: 5.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500175490  62 AIIMAAGMSSRFAplsyeRPKGLLNVRGEVLIERQIRQLHERGiTDITIVLGYmkEQFYYLEDKYNVKIVVNDDYYR 138
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALAGLGVPVVPDPDPGQ 69
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
305-560 7.37e-09

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 57.44  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 305 VSDITGivpvkdGLTNLSLKFEYDGK-----AYIYRHPGVGTDEYINRKSEFFAQQKAKKLGFddsyiymdpekGWKL-- 377
Cdd:PLN02421   19 VERISG------GITNLLLKVSVKEEngnevSVTVRLFGPNTDYVIDRERELQAIKYLSAAGF-----------GAKLlg 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 378 -------SYFIDqARKLDYHQWDEVKQALEMIKDI---HDQQLSGEFEFNIWNKSCDFIGKLS--------QQDKDVFSD 439
Cdd:PLN02421   82 vfgngmiQSFIN-ARTLTPSDMRKPKVAAEIAKELrrlHQVEIPGSKEPQLWNDIFKFYEKAStvkfedpeKQKKYETIS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 440 FDELFKLIESVKKYSDKDNVPLRLCHCDFYDPNILFSGND--LYLIDWEYAGVDDPGVDIGTFI---ACSDYTY------ 508
Cdd:PLN02421  161 FEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLMLNEDEgkLYFIDFEYGSYSYRGYDIGNHFneyAGFDCDYslypsk 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500175490 509 EEAMQVLELYNKtPMDASMQRH------FI---AYIAIASYYWFVWAIFQESNGAAVGEYL 560
Cdd:PLN02421  241 EEQYHFFRHYLR-PDDPEEVSDaeleelFVetnFYALASHLYWAIWAIVQAKMSPIDFDYL 300
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
317-518 1.19e-08

thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (thiK), and additional proteobacterial homologs taken to be orthologs with equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274268 [Multi-domain]  Cd Length: 256  Bit Score: 56.25  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 317 GLTNLSLKFEYDGKAYIYRHPG-VGTDEYINRKSEFFAQQKAKKLGFDDSYIYMDPekGWKLSYFIDQ--ARKLDYHQWD 393
Cdd:TIGR02721   7 GLTNRSWRIEHPGISFVWRPQSpVCKALGVDRQREYQILQALSALGLAPKPILVNE--HWLLVEWLEGevITLDQFVALD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 394 EVKQALEMIKDIHDQQLSG-EFEFNI-----WNkSCDfigklsqqDKDVFSDFDELFKLIESVKKYSDkdnVPLRLCHCD 467
Cdd:TIGR02721  85 LLLELAALLHQLHSQPRFGyPLSLKAriahyWL-QID--------PARRTPEWLRLYKQFRSAPEPAP---LPLAPLHMD 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2500175490 468 FYDPNILFSGNDLYLIDWEYAGVDDPGVDIGTFIACSDytyEEAMQ-VLELY 518
Cdd:TIGR02721 153 VHAYNLVVTPQGLKLIDWEYASDGDIALELAAIIRAND---EEQQQdFVQRY 201
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
61-143 1.14e-06

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 49.26  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490  61 NAIIMAAGMSSRFAplsyeRPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMK-EQFYYLEDKYNVKIVVNDDYYRY 139
Cdd:TIGR03310   1 DAIILAAGLSSRMG-----QNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEAdELVALLANHSNITLVHNPQYAEG 75

                  ....
gi 2500175490 140 NNTS 143
Cdd:TIGR03310  76 QSSS 79
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
460-518 4.74e-06

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 48.57  E-value: 4.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500175490 460 PLRLCHCDFYDPNILFSGND---LYLIDWEYAGVDDPGVDIGTFIAC---SDYTYEEAMQVLELY 518
Cdd:COG3173   191 PPVLVHGDLRPGNLLVDPDDgrlTAVIDWELATLGDPAADLAYLLLYwrlPDDLLGPRAAFLAAY 255
lant_syn_V_LxmK NF038156
class V lanthionine synthetase subunit LxmK;
459-501 1.61e-05

class V lanthionine synthetase subunit LxmK;


Pssm-ID: 468390 [Multi-domain]  Cd Length: 347  Bit Score: 47.15  E-value: 1.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2500175490 459 VPLRLCHCDFYDPNILFSGNDLYLIDWEYAGVDDPGVDIGTFI 501
Cdd:NF038156  189 APRVPVHGDLRLDQFLVADGRLYLTDWEEFRLGDPARDVGAFA 231
 
Name Accession Description Interval E-value
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
60-287 5.51e-114

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 338.73  E-value: 5.51e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490  60 DNAIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQFYYLEDKYNVKIVVNDDYYRY 139
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDKYGVKLIYNPDYAEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 140 NNTSTLMLVLDQLKNTYICSSDNYFVENVFNPYEYKTTYPVqVHTTHESGEYYADFTDEGLITQIGIGSGTYNCMVGHVF 219
Cdd:COG4750    81 NNISSLYLVRDKLGNTYICSSDNYLTENPFEKYEYKSYYSA-VYKEGETDEWCVKTNRDGRITKIEIGGKDGWIMLGHSY 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500175490 220 FDQAFSHDFGELLKQEYPKEETKSKLWEKVYVEHMDQFTMYAEVYSKDIIKEFDSLEELQAFDASYLE 287
Cdd:COG4750   160 WDKEDSKKFKEILEEEYEDPETRDLYWEDIYMDHIDELDMYARKYPAGDIYEFDSLDELREFDPSYLE 227
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
62-282 2.18e-49

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 170.88  E-value: 2.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQF-YYLEDKYNVKIVVNDDYYRYN 140
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIeELLKKYPNIKFVYNPDYAETN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 141 NTSTLMLVLDQLK-NTYICSSDNYFVENVFNPYEYKTTYPVQV--HTTHESGEYYADFTDEGL----ITQIGIGSGTYNC 213
Cdd:cd02523    81 NIYSLYLARDFLDeDFLLLEGDVVFDPSILERLLSSPADNAILvdKKTKEWEDEYVKDLDDAGvllgIISKAKNLEEIQG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 214 -MVGHVFFDQAFSHDFGELLKqEYPKEETKSKLWEKVYVEHMDQFTMYAEVYSKDIIKEFDSLEELQAFD 282
Cdd:cd02523   161 eYVGISKFSPEDADRLAEALE-ELIEAGRVNLYYEDALQRLISEEGVKVKDISDGFWYEIDDLEDLERAE 229
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
311-506 1.17e-38

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 139.23  E-value: 1.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 311 IVPVKDGLTNLSLKFEYDGKAYIYRHPGVGTDEYINRKSEFFAQQKAKKLGFDDSYIYMDPEKGWKLSYFIDQARKL--D 388
Cdd:cd05151     3 IEPLKGGLTNKNYLVEVAGKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEVIYFDPETGVKITEFIEGATLLtnD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 389 YHQWDEVKQALEMIKDIHDQQLsgefefniwnkscdfigklsqqdkdvfsdfdelfkliesvkkysdKDNVPlrlCHCDF 468
Cdd:cd05151    83 FSDPENLERIAALLRKLHSSPL---------------------------------------------EDLVL---CHNDL 114
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2500175490 469 YDPNILFSGNDLYLIDWEYAGVDDPGVDIGTFIACSDY 506
Cdd:cd05151   115 VPGNFLLDDDRLYLIDWEYAGMNDPLFDLAALFSENNL 152
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
62-279 6.20e-29

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 114.95  E-value: 6.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQF--YYLEDKYNVKIVVNDDYYRY 139
Cdd:COG1213     2 AVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIeeALARPGPDVTFVYNPDYDET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 140 NNTSTLMLVLDQLKN-TYICSSDNYFVENVF---NPYEYKTTYPVQVHTTHESGE---YYADftDEGLITQIG--IGSGT 210
Cdd:COG1213    82 NNIYSLWLAREALDEdFLLLNGDVVFDPAILkrlLASDGDIVLLVDRKWEKPLDEevkVRVD--EDGRIVEIGkkLPPEE 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500175490 211 YNC-MVGHVFFDQAFSHDFGELLKQEYPKEETKSKlWEKVYVEHMDQftmYAEVYSKDIIK----EFDSLEELQ 279
Cdd:COG1213   160 ADGeYIGIFKFSAEGAAALREALEALIDEGGPNLY-YEDALQELIDE---GGPVKAVDIGGlpwvEIDTPEDLE 229
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
405-565 3.39e-27

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 107.56  E-value: 3.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 405 IHDQQLSGEFefniwnkscDFIGKLSQQDKDVFSDFDELFKLIESVKKYSDKDNVPLRLCHCDFYDPNILFSGND-LYLI 483
Cdd:COG0510     2 LHASPALLRF---------DLFARLERYLALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGrLYLI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 484 DWEYAGVDDPGVDIGTFIACSDYTYEEAMQVLELYNKTPMDASMQRHFIAYIAIASYYWFVWAIF---QESNGAAvGEYL 560
Cdd:COG0510    73 DWEYAGLGDPAFDLAALLVEYGLSPEQAEELLEAYGFGRPTEELLRRLRAYRALADLLWALWALVraaQEANGDL-LKYL 151

                  ....*
gi 2500175490 561 TIWYN 565
Cdd:COG0510   152 LRRLE 156
GntI_guanitoxin NF041256
guanitoxin biosynthesis pre-guanitoxin N-oxide kinase GntI;
312-549 9.91e-19

guanitoxin biosynthesis pre-guanitoxin N-oxide kinase GntI;


Pssm-ID: 469156 [Multi-domain]  Cd Length: 279  Bit Score: 86.45  E-value: 9.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 312 VPVKD-GLTNLSLKFEYDGKAYIYRHPGVGTDEY-INRKSEFFAQQKAKKLGFDDSYIYMDPEKGWKLSYFID--QARKL 387
Cdd:NF041256   18 VEIQDsGLTNRNYRVENGGEKFVVRISGGNSNLLgINRHAELIALKAVAAMGIGPEVLAFDPPEGHLVTRFIEgrHFSLE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 388 DYHQWDEVKQALEMIKDIHdQQLSGEFEFNIWNKSCDFIGKLSQQDKDVFSDFDELFKLIESVKK----YSDKdnvPLRL 463
Cdd:NF041256   98 DLTQPENIDRIAQLLKQVH-SGPPIPGRFSPYRDIEDYIQTAFARGIDLPPPLERIEGLLRNIERkrgaFPDR---FEGL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 464 CHCDFYDPNILFSGNDLYLIDWEYAGVDDPGVDIGTFIACSDYTYEEAMQVLELYNKTpMDASMQRHFIAYIAIASYYWF 543
Cdd:NF041256  174 CHNDLFANNFIDDGGSIRLLDWEYAGMGDILFDLANFSMNQSLDREGDKILLESYFGK-VSQALLAALNLMKFVVIFWEA 252

                  ....*.
gi 2500175490 544 VWAIFQ 549
Cdd:NF041256  253 MWGVLQ 258
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
62-130 5.18e-16

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 77.24  E-value: 5.18e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQFY-YLED--KYNVKI 130
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEeYFGDgsKFGVNI 72
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
62-130 7.79e-16

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 77.12  E-value: 7.79e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQFY-YLED--KYNVKI 130
Cdd:COG1208     2 AVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEeYFGDgsRFGVRI 73
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
330-522 6.90e-15

Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. This alignment covers the protein kinase portion of the protein. The divergence of this family makes it very difficult to create a model that specifically predicts choline/ethanolamine kinases only. However if [add Pfam ID here for Choline_kinase_C] is also present then it is definitely a member of this family.


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 73.85  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 330 KAYIYRHPGVGTDEYINRKSEF--FAQQKAKKLG------FDDSYIYMdpekgwklsyFIdQARKLDYHQ---WDEVKQA 398
Cdd:pfam01633   3 RKVLLRIYGPGTELLINREDEIvnFALLSERGLGpklygfFPNGRIEE----------FI-PSRTLSTEDlrdPEISKLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 399 LEMIKDIHDQQLSGEFEFNIWN---------KSCDFIGKLSQQDKDVFSDFDELFKLIESVKKYSDKDNVPLRLCHCDFY 469
Cdd:pfam01633  72 AKRLAELHSLEMPGKKSPSLWKtmrkwlsllKNLGAPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQ 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2500175490 470 DPNILF--SGNDLYLIDWEYAGVDDPGVDIGTFIA--CSDYTYEEAMQVLElYNKTP 522
Cdd:pfam01633 152 SGNILLlnETKRLVLIDFEYASYNYRGFDIANHFCewAGDYHDPTPFFKCD-YSLYP 207
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
62-136 1.33e-12

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 66.72  E-value: 1.33e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500175490  62 AIIMAAGMSSRFaplsyERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQFYYLEDKYNVKIVVNDDY 136
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDW 75
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
311-549 9.01e-12

Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate, and displays negligible activity towards N-methylated derivatives of Etn. The Drosophila ETNK is implicated in development and neuronal function. Mammals contain two ETNK proteins, ETNK1 and ETNK2. ETNK1 selectively increases Etn uptake and phosphorylation, as well as PtdEtn synthesis. ETNK2 is found primarily in the liver and reproductive tissues. It plays a critical role in regulating placental hemostasis to support late embryonic development. It may also have a role in testicular maturation. ETNK is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270706 [Multi-domain]  Cd Length: 307  Bit Score: 66.45  E-value: 9.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 311 IVPVKDGLTNLSLKFEYDGKAY-------IYrhpGVGTDEYINRKSEFFAQQKAKKLG--------FDDSYIYmdpekgw 375
Cdd:cd05157     3 VKRITGGITNALYKVTYPSGDTpktvlvrIY---GPGTELLIDRDRELRILQLLSRAGigpklygrFENGRVE------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 376 klsYFIDqARKLDYHQ-WDEVKQAL---EMiKDIHDQQLSGEFEF----NIWNKSCDFIGKLSQQDKDV--------FSD 439
Cdd:cd05157    73 ---EFLP-GRTLTPEDlRDPKISRLiarRL-AELHSIVPLGEIEGkkkpILWTTIRKWLDLAPEVFEDEknkekkleKVD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 440 FDELFKLIESVKKY-SDKDNVPLRLCHCDFYDPNILF--SGNDLYLIDWEYAGVDDPGVDIGTFIA--CSDYTYEEamqv 514
Cdd:cd05157   148 LERLRKELEWLEKWlESLEKSPIVFCHNDLLYGNILYneDDDSVTFIDFEYAGPNPRAFDIANHFCewAGFYCVLD---- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500175490 515 lelYNKTPmDASMQRHFI-AYI----------------------------AIASYYWFVWAIFQ 549
Cdd:cd05157   224 ---YSRYP-TKEEQRNFLrAYLesldglpggeevseeeveklynevnlfrLASHLFWGLWALIQ 283
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
62-131 3.27e-11

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 63.36  E-value: 3.27e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQFY-YLED--KYNVKIV 131
Cdd:cd04189     3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKeALGDgsRFGVRIT 75
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
433-547 1.34e-10

Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline kinase, ethanolamine kinase, and similar proteins. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270923 [Multi-domain]  Cd Length: 229  Bit Score: 61.52  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 433 DKDVFSDFDELFKLIESVKKYSDKDNVPLRLCHCDFYDPNILFSGND--LYLIDWEYAGVDDPGVDIGTFIACS--DYTY 508
Cdd:cd14021    84 TTDELRNPSVLTSIAKLLAKFHKIKTPPVVFCHNDLQENNILLTNDQdgLRLIDFEYSGFNYRGYDIANFFNESmiDYDH 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500175490 509 EEAMQVLELYNKTPmDASMQRHFIA-YI--------------------------AIAS-YYWFVWAI 547
Cdd:cd14021   164 PEPPYFKIYKENYI-SEEEKRLFVSvYLseyleknvlpsldklveqflqeveifTLGShLYWGLWSI 229
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
62-138 5.10e-10

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 58.36  E-value: 5.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500175490  62 AIIMAAGMSSRFAplsyeRPKGLLNVRGEVLIERQIRQLHERGiTDITIVLGYmkEQFYYLEDKYNVKIVVNDDYYR 138
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALAGLGVPVVPDPDPGQ 69
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
62-136 1.71e-09

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 57.57  E-value: 1.71e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500175490  62 AIIMAAGMSSRFAplsyeRPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQFYYLEDKYNVKIVVNDDY 136
Cdd:cd04182     3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDW 72
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
61-134 4.14e-09

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 57.20  E-value: 4.14e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500175490  61 NAIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQFY-YLEDK-YNVKIVVND 134
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEaHLGDSrFGLRITISD 76
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
305-560 7.37e-09

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 57.44  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 305 VSDITGivpvkdGLTNLSLKFEYDGK-----AYIYRHPGVGTDEYINRKSEFFAQQKAKKLGFddsyiymdpekGWKL-- 377
Cdd:PLN02421   19 VERISG------GITNLLLKVSVKEEngnevSVTVRLFGPNTDYVIDRERELQAIKYLSAAGF-----------GAKLlg 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 378 -------SYFIDqARKLDYHQWDEVKQALEMIKDI---HDQQLSGEFEFNIWNKSCDFIGKLS--------QQDKDVFSD 439
Cdd:PLN02421   82 vfgngmiQSFIN-ARTLTPSDMRKPKVAAEIAKELrrlHQVEIPGSKEPQLWNDIFKFYEKAStvkfedpeKQKKYETIS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 440 FDELFKLIESVKKYSDKDNVPLRLCHCDFYDPNILFSGND--LYLIDWEYAGVDDPGVDIGTFI---ACSDYTY------ 508
Cdd:PLN02421  161 FEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLMLNEDEgkLYFIDFEYGSYSYRGYDIGNHFneyAGFDCDYslypsk 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500175490 509 EEAMQVLELYNKtPMDASMQRH------FI---AYIAIASYYWFVWAIFQESNGAAVGEYL 560
Cdd:PLN02421  241 EEQYHFFRHYLR-PDDPEEVSDaeleelFVetnFYALASHLYWAIWAIVQAKMSPIDFDYL 300
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
317-518 1.19e-08

thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (thiK), and additional proteobacterial homologs taken to be orthologs with equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274268 [Multi-domain]  Cd Length: 256  Bit Score: 56.25  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 317 GLTNLSLKFEYDGKAYIYRHPG-VGTDEYINRKSEFFAQQKAKKLGFDDSYIYMDPekGWKLSYFIDQ--ARKLDYHQWD 393
Cdd:TIGR02721   7 GLTNRSWRIEHPGISFVWRPQSpVCKALGVDRQREYQILQALSALGLAPKPILVNE--HWLLVEWLEGevITLDQFVALD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 394 EVKQALEMIKDIHDQQLSG-EFEFNI-----WNkSCDfigklsqqDKDVFSDFDELFKLIESVKKYSDkdnVPLRLCHCD 467
Cdd:TIGR02721  85 LLLELAALLHQLHSQPRFGyPLSLKAriahyWL-QID--------PARRTPEWLRLYKQFRSAPEPAP---LPLAPLHMD 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2500175490 468 FYDPNILFSGNDLYLIDWEYAGVDDPGVDIGTFIACSDytyEEAMQ-VLELY 518
Cdd:TIGR02721 153 VHAYNLVVTPQGLKLIDWEYASDGDIALELAAIIRAND---EEQQQdFVQRY 201
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
438-518 2.29e-08

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 55.20  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 438 SDFDELFKLIESVKKYSDK---DNVPLRLCHCDFYDPNILFSGND--LYLIDWEYAGVDDPGVDIGtfIACSDYTYEEAM 512
Cdd:pfam01636 141 ELLDRLEELEERLLAALLAllpAELPPVLVHGDLHPGNLLVDPGGrvSGVIDFEDAGLGDPAYDLA--ILLNSWGRELGA 218

                  ....*.
gi 2500175490 513 QVLELY 518
Cdd:pfam01636 219 ELLAAY 224
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
62-118 2.38e-08

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 54.87  E-value: 2.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQ 118
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQ 57
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
61-143 1.14e-06

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 49.26  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490  61 NAIIMAAGMSSRFAplsyeRPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMK-EQFYYLEDKYNVKIVVNDDYYRY 139
Cdd:TIGR03310   1 DAIILAAGLSSRMG-----QNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEAdELVALLANHSNITLVHNPQYAEG 75

                  ....
gi 2500175490 140 NNTS 143
Cdd:TIGR03310  76 QSSS 79
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
460-518 4.74e-06

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 48.57  E-value: 4.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500175490 460 PLRLCHCDFYDPNILFSGND---LYLIDWEYAGVDDPGVDIGTFIAC---SDYTYEEAMQVLELY 518
Cdd:COG3173   191 PPVLVHGDLRPGNLLVDPDDgrlTAVIDWELATLGDPAADLAYLLLYwrlPDDLLGPRAAFLAAY 255
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
463-500 5.77e-06

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 46.53  E-value: 5.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2500175490 463 LCHCDFYDPNILFSGND--LYLIDWEYAGVDDPGVDIGTF 500
Cdd:cd05120   113 LTHGDLHPGNILVKPDGklSGIIDWEFAGYGPPAFDYAAA 152
lant_syn_V_LxmK NF038156
class V lanthionine synthetase subunit LxmK;
459-501 1.61e-05

class V lanthionine synthetase subunit LxmK;


Pssm-ID: 468390 [Multi-domain]  Cd Length: 347  Bit Score: 47.15  E-value: 1.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2500175490 459 VPLRLCHCDFYDPNILFSGNDLYLIDWEYAGVDDPGVDIGTFI 501
Cdd:NF038156  189 APRVPVHGDLRLDQFLVADGRLYLTDWEEFRLGDPARDVGAFA 231
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
61-131 4.18e-05

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 45.28  E-value: 4.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500175490  61 NAIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGY----MKEQFYYLEDKYNVKIV 131
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYrpedMVPFLKEYEKKLGIKIT 76
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
439-535 1.15e-04

Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC) and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. Along with PCho, it is involved in malignant transformation through Ras oncogenes in various human cancers such as breast, lung, colon, prostate, neuroblastoma, and hepatic lymphoma. In mammalian cells, there are three ChoK isoforms (A-1, A-2, and B) which are active in homo- or heterodimeric forms. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270705 [Multi-domain]  Cd Length: 326  Bit Score: 44.54  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 439 DFDELFKLIESVKKYSDKdnvPLRLCHCDFYDPNILFSGN-------DLYLIDWEYAGVDDPGVDIGTFIA--CSDYTYE 509
Cdd:cd05156   154 DLAKELGWLRSLLESTPS---PVVFCHNDLQEGNILLLNGpenseddKLVLIDFEYCSYNYRGFDLANHFCewAYDYTVP 230
                          90       100
                  ....*....|....*....|....*..
gi 2500175490 510 EAMQVLELYNKTPMDASmQRHFI-AYI 535
Cdd:cd05156   231 EPPYFKINPENYPTREQ-QLHFIrAYL 256
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
463-511 1.28e-04

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 44.17  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2500175490 463 LCHCDFYDPNILFSGNDLY-LIDWEYAGVDDPGVDIGtfIACSDYTYEEA 511
Cdd:cd05153   181 VIHADLFRDNVLFDGDRLSgIIDFYDACYDPLLYDLA--IALNDWCFDDD 228
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
62-127 2.39e-04

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 42.63  E-value: 2.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLG--YMKEQFYYLEDKYN 127
Cdd:cd02507     3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCehSQAIIEHLLKSKWS 70
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
63-172 3.09e-04

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 42.63  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490  63 IIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHErgITDITIVLGYMKEQFyyleDKYNVKIVVNDDYYRY--- 139
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAK--IFDSRFIFICRDEHN----TKFHLDESLKLLAPNAtvv 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2500175490 140 ---NNTS----TLMLVLDQLKN---TYICSSDNYFVENVFNPY 172
Cdd:cd04183    76 eldGETLgaacTVLLAADLIDNddpLLIFNCDQIVESDLLAFL 118
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
438-546 7.84e-04

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 41.83  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 438 SDFDELFKLIESVKKY--SDKDNVPLRLCHCDFYDPNILFSGNDL-YLIDWEYAGVDDPGVDIGTFIACSDYTYEEAMQV 514
Cdd:COG2334   154 EDRALLEELLDRLEARlaPLLGALPRGVIHGDLHPDNVLFDGDGVsGLIDFDDAGYGPRLYDLAIALNGWADGPLDPARL 233
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2500175490 515 LEL---YNKT-PMDASMQRH---FIAYIAIASYYWFVWA 546
Cdd:COG2334   234 AALlegYRAVrPLTEAELAAlppLLRLRALRFLAWRLRR 272
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
323-520 7.92e-04

Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444583 [Multi-domain]  Cd Length: 331  Bit Score: 41.80  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 323 LKFEYDGKAYIYRHPGVGTDEYI-NRKSEFFAQQKakklgfDDSYIYMDpekgWklsyfIDqARKLDYHQWDEVKQALEM 401
Cdd:COG5881    47 LLFIYEAQEHLKKNGFNNIPRIVpTKDGKPYVKYG------GKLYYLTE----W-----IE-GRECDYKNPEDLKKAAET 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175490 402 IKDIHdqQLSGEFEFNIWNKSCDFIGKLSQ----------------QDKDVFSDFDELF------------KLIESVKK- 452
Cdd:COG5881   111 LAEFH--KASKGFEPPPGSKGRSHLGKWPErfekrleelekfkkiaEKKKNKNEFDRLFlknidyfleqaeKALELLEKs 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500175490 453 -YSD---KDNVPLRLCHCDFYDPNILFSGND-LYLIDWEYAGVDDPGVDIGTFI--ACSDYTY--EEAMQVLELYNK 520
Cdd:COG5881   189 aYYKlvkEAKKEGGFCHHDYAYHNILIDEDGkIYIIDFDYCIYDLPVHDLAKLLrrVMKRGNWdiEKAKEILEAYNK 265
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
62-119 1.16e-03

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 41.23  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLG-YMKEQF 119
Cdd:COG1209     3 GIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQF 61
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
62-134 1.28e-03

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 40.33  E-value: 1.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVL--GYMKEQFYYLEDKYNVKIVVND 134
Cdd:cd04198     3 AVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVpeEEQAEISTYLRSFPLNLKQKLD 77
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
61-111 1.69e-03

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 39.87  E-value: 1.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2500175490  61 NAIIMAAGMSSRFAplsyeRPKGLLNVRGEVLIERQIRQLheRGITDITIV 111
Cdd:cd02503     2 TGVILAGGKSRRMG-----GDKALLELGGKPLLEHVLERL--KPLVDEVVI 45
thiK PRK10271
thiamine kinase; Provisional
460-492 2.09e-03

thiamine kinase; Provisional


Pssm-ID: 182349  Cd Length: 188  Bit Score: 39.73  E-value: 2.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2500175490 460 PLRLC--HCDFYDPNILFSGNDLYLIDWEYAGVDD 492
Cdd:PRK10271   74 PLRLAplHMDVHAGNLVHSASGLRLIDWEYAGDGD 108
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
62-135 2.19e-03

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 39.81  E-value: 2.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500175490  62 AIIMAAGMSSRFAplSyERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEQFYYLEDKYNVKIVVNDD 135
Cdd:cd02540     1 AVILAAGKGTRMK--S-DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVEFVLQEE 71
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
463-531 3.85e-03

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 38.40  E-value: 3.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500175490 463 LCHCDFYDPNILFSGNDLYLIDWEYA----GVDDPGVDIGTFI-----ACSDYTYEEAMQVLELYNKTPMDASMQRHF 531
Cdd:COG3642    72 IVHGDLTTSNILVDDGGVYLIDFGLArysdPLEDKAVDLAVLKrslesTHPDPAEELWEAFLEGYREVGPAEEVLRRL 149
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
62-100 5.06e-03

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 38.25  E-value: 5.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2500175490  62 AIIMAAGMSSRFAplsyeRPKGLLNVRGEVLIERQIRQL 100
Cdd:COG0746     7 GVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERL 40
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
463-501 5.08e-03

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 39.19  E-value: 5.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2500175490 463 LCHCDFYDPNILFSGNDLYLIDWEYAGVDDPGVDIGTFI 501
Cdd:TIGR02906 189 FCHQDYAYHNILLKDNEVYVIDFDYCTIDLPVRDLRKLI 227
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
62-131 5.21e-03

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 38.66  E-value: 5.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500175490  62 AIIMAAGMSSRFAPlsyERPKGLLNVRGEVLIERQIRQL-HERGITDITIV-----LGYMKEQFYYLEDKyNVKIV 131
Cdd:cd02516     3 AIILAAGSGSRMGA---DIPKQFLELGGKPVLEHTLEAFlAHPAIDEIVVVvppddIDLAKELAKYGLSK-VVKIV 74
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
62-124 5.88e-03

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 39.05  E-value: 5.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500175490  62 AIIMAAGMSSRFAPLSYERPKGLLNVRGEVLIERQIRQLHERGITDITIVLGYMKEqfyYLED 124
Cdd:cd02541     3 AVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKR---AIED 62
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
457-502 6.05e-03

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 38.75  E-value: 6.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2500175490 457 DNVP----LRLCHCDFYDPNILFSGND--LYLIDWEYAGVDDPGVDIGTFIA 502
Cdd:cd05154   169 ANLPadgrPVLVHGDFRLGNLLFDPDGrvTAVLDWELATLGDPLEDLAWLLA 220
 
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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