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Conserved domains on  [gi|1694513029|ref|XP_029439072|]
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choline kinase alpha isoform X2 [Rhinatrema bivittatum]

Protein Classification

choline/ethanolamine kinase family protein( domain architecture ID 10142383)

choline/ethanolamine kinase family protein catalyzes the phosphorylation of choline and/or ethanolamine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
79-401 0e+00

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: 539.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  79 FHISVIRGGLSNKLFLCSLPDTVKTVADEPCSILLRLYGAILQGTEAMVMESVMFAILAERSLGPKLYGIFPQGRLEQFI 158
Cdd:cd05156     1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 159 PSRKLETEELHLPELSAEIAGKLAHFHGMKMPFNKEPKWLFGTMEKYLNQVLKIKFSRESH--VRKLNKLLSYDLPQEME 236
Cdd:cd05156    81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTkpSKQLELLLSYDLAKELG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 237 TLWSVLEATYSPVVFCHNDCQEGNILLLEGRESSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKFPFFKSNLT 316
Cdd:cd05156   161 WLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 317 KYPTKKEQIHFISSYMAEFQAGFENISNEEKSRIENEMLVEVNRFALASHFFWGLWSILQAKISTIEFGYLEYALARFDA 396
Cdd:cd05156   241 NYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDA 320

                  ....*
gi 1694513029 397 YYQQK 401
Cdd:cd05156   321 YFKQK 325
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
79-401 0e+00

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: 539.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  79 FHISVIRGGLSNKLFLCSLPDTVKTVADEPCSILLRLYGAILQGTEAMVMESVMFAILAERSLGPKLYGIFPQGRLEQFI 158
Cdd:cd05156     1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 159 PSRKLETEELHLPELSAEIAGKLAHFHGMKMPFNKEPKWLFGTMEKYLNQVLKIKFSRESH--VRKLNKLLSYDLPQEME 236
Cdd:cd05156    81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTkpSKQLELLLSYDLAKELG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 237 TLWSVLEATYSPVVFCHNDCQEGNILLLEGRESSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKFPFFKSNLT 316
Cdd:cd05156   161 WLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 317 KYPTKKEQIHFISSYMAEFQAGFENISNEEKSRIENEMLVEVNRFALASHFFWGLWSILQAKISTIEFGYLEYALARFDA 396
Cdd:cd05156   241 NYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDA 320

                  ....*
gi 1694513029 397 YYQQK 401
Cdd:cd05156   321 YFKQK 325
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
107-323 1.77e-82

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: 251.42  E-value: 1.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 107 EPCSILLRLYGAILQGTEAMVMESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRKLETEELHLPELSAEIAGKLAHFHG 186
Cdd:pfam01633   1 SPRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 187 MKMPFNKEPkWLFGTMEKYLNQVLKIK-FSRESHVRKLNKLLSYDLPQEMETLWSVLEATYSPVVFCHNDCQEGNILLLE 265
Cdd:pfam01633  81 LEMPGKKSP-SLWKTMRKWLSLLKNLGaPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLN 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1694513029 266 gressEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKfPFFKSNLTKYPTKKE 323
Cdd:pfam01633 160 -----ETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
63-404 1.49e-66

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 214.60  E-value: 1.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  63 CKEFLPGaWRQLQEENFHISVIRGGLSNKLflcsLPDTVKTVADEPCSILLRLYGAilqGTEAMV---MESVMFAILAER 139
Cdd:PLN02421    2 CKALFKG-WSDLDDSDFSVERISGGITNLL----LKVSVKEENGNEVSVTVRLFGP---NTDYVIdreRELQAIKYLSAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 140 SLGPKLYGIFPQGRLEQFIPSRKLETEELHLPELSAEIAGKLAHFHGMKMPFNKEPKwLFGTMEKYLNQVLKIKFSRESH 219
Cdd:PLN02421   74 GFGAKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQ-LWNDIFKFYEKASTVKFEDPEK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 220 VRKLNKLLSYDLPQEMETLWSVLEATYSPVVFCHNDCQEGNILLLEgressEKQKLMLIDFEYSSYNYRGFDIGNHFCEW 299
Cdd:PLN02421  153 QKKYETISFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLMLNE-----DEGKLYFIDFEYGSYSYRGYDIGNHFNEY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 300 M-YDYTYekfpffksnlTKYPTKKEQIHFISSYMAEFQAgfENISNEEksrIEnEMLVEVNRFALASHFFWGLWSILQAK 378
Cdd:PLN02421  228 AgFDCDY----------SLYPSKEEQYHFFRHYLRPDDP--EEVSDAE---LE-ELFVETNFYALASHLYWAIWAIVQAK 291
                         330       340
                  ....*....|....*....|....*.
gi 1694513029 379 ISTIEFGYLEYALARFDAYYQQKRKL 404
Cdd:PLN02421  292 MSPIDFDYLGYFFLRYKEYKRQKEKL 317
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
230-394 1.12e-12

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 65.19  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 230 DLPQEMETLWSVLEATYSPVVFCHNDCQEGNILLlegresSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDytyekfp 309
Cdd:COG0510    30 ELLRRLEELERALAARPLPLVLCHGDLHPGNFLV------TDDGRLYLIDWEYAGLGDPAFDLAALLVEYGLS------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 310 ffksnltkyptKKEQIHFISSYmaefqaGFENISNEEKSRIEnemlvevnRFALASHFFWGLWSILQAkISTIEFGYLEY 389
Cdd:COG0510    97 -----------PEQAEELLEAY------GFGRPTEELLRRLR--------AYRALADLLWALWALVRA-AQEANGDLLKY 150

                  ....*
gi 1694513029 390 ALARF 394
Cdd:COG0510   151 LLRRL 155
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
187-345 1.13e-05

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: 46.89  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 187 MKMPFNKEPKWLFG-----TMEKYLNQVLKIKfsreshvRKLNKLLSYDLPQEMETLWSvleatyspvvFCHNDCQEGNI 261
Cdd:TIGR02906 137 KKIALEKKYKDEFDklylkEVDYFLERGKKAL-------ELLNKSKYYDLCKEAKKIRG----------FCHQDYAYHNI 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 262 LLLEGressekqKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKFPFFKSNLTKY----PTKKEQIHFISSYMaEFQA 337
Cdd:TIGR02906 200 LLKDN-------EVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVWDLEKAKEIIEAYssinPLSKEEKEVLYIDL-AFPH 271

                  ....*...
gi 1694513029 338 GFENISNE 345
Cdd:TIGR02906 272 KFWKIGKQ 279
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
79-401 0e+00

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: 539.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  79 FHISVIRGGLSNKLFLCSLPDTVKTVADEPCSILLRLYGAILQGTEAMVMESVMFAILAERSLGPKLYGIFPQGRLEQFI 158
Cdd:cd05156     1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 159 PSRKLETEELHLPELSAEIAGKLAHFHGMKMPFNKEPKWLFGTMEKYLNQVLKIKFSRESH--VRKLNKLLSYDLPQEME 236
Cdd:cd05156    81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTkpSKQLELLLSYDLAKELG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 237 TLWSVLEATYSPVVFCHNDCQEGNILLLEGRESSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKFPFFKSNLT 316
Cdd:cd05156   161 WLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 317 KYPTKKEQIHFISSYMAEFQAGFENISNEEKSRIENEMLVEVNRFALASHFFWGLWSILQAKISTIEFGYLEYALARFDA 396
Cdd:cd05156   241 NYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDA 320

                  ....*
gi 1694513029 397 YYQQK 401
Cdd:cd05156   321 YFKQK 325
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
79-398 4.78e-103

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: 307.59  E-value: 4.78e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  79 FHISVIRGGLSNKLFLCSLPDTVKTVadepcSILLRLYGAilqGTEAMV---MESVMFAILAERSLGPKLYGIFPQGRLE 155
Cdd:cd05157     1 IKVKRITGGITNALYKVTYPSGDTPK-----TVLVRIYGP---GTELLIdrdRELRILQLLSRAGIGPKLYGRFENGRVE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 156 QFIPSRKLETEELHLPELSAEIAGKLAHFHGMKMPFNKEPKW---LFGTMEKYLNQVLKIKFSRESHVRKLNKLLSYDLP 232
Cdd:cd05157    73 EFLPGRTLTPEDLRDPKISRLIARRLAELHSIVPLGEIEGKKkpiLWTTIRKWLDLAPEVFEDEKNKEKKLEKVDLERLR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 233 QEMETLWSVLEATY-SPVVFCHNDCQEGNILLLEgressEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTyekfpff 311
Cdd:cd05157   153 KELEWLEKWLESLEkSPIVFCHNDLLYGNILYNE-----DDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYC------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 312 KSNLTKYPTKKEQIHFISSYMAEFQAGFENISNEEKsRIEnEMLVEVNRFALASHFFWGLWSILQAKISTIEFGYLEYAL 391
Cdd:cd05157   221 VLDYSRYPTKEEQRNFLRAYLESLDGLPGGEEVSEE-EVE-KLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAK 298

                  ....*..
gi 1694513029 392 ARFDAYY 398
Cdd:cd05157   299 ERLDEYW 305
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
107-323 1.77e-82

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: 251.42  E-value: 1.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 107 EPCSILLRLYGAILQGTEAMVMESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRKLETEELHLPELSAEIAGKLAHFHG 186
Cdd:pfam01633   1 SPRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 187 MKMPFNKEPkWLFGTMEKYLNQVLKIK-FSRESHVRKLNKLLSYDLPQEMETLWSVLEATYSPVVFCHNDCQEGNILLLE 265
Cdd:pfam01633  81 LEMPGKKSP-SLWKTMRKWLSLLKNLGaPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLN 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1694513029 266 gressEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKfPFFKSNLTKYPTKKE 323
Cdd:pfam01633 160 -----ETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
80-374 5.05e-82

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: 251.03  E-value: 5.05e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  80 HISVIRGGLSNKLFLCSLPDTVKTvaDEPCSILLRLYGAILQGTEAMVMESVMFAILAERSLGPKLYGIFPQGRLEQFIP 159
Cdd:cd14021     2 LVIRILSGLTNQVYKVSLKDESDS--LEPKKVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYID 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 160 SRKLETEELHLPELSAEIAGKLAHFHGMKMPfnkepkwlfgtmekylnqvlkikfsreshvrklnkllsydlpqemetlw 239
Cdd:cd14021    80 GRPLTTDELRNPSVLTSIAKLLAKFHKIKTP------------------------------------------------- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 240 svleatysPVVFCHNDCQEGNILLLegresSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKFPFFKSNLTKYP 319
Cdd:cd14021   111 --------PVVFCHNDLQENNILLT-----NDQDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHPEPPYFKIYKENYI 177
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1694513029 320 TKKEQIHFISSYMAEFQAGFENISNEEksrIENEMLVEVNRFALASHFFWGLWSI 374
Cdd:cd14021   178 SEEEKRLFVSVYLSEYLEKNVLPSLDK---LVEQFLQEVEIFTLGSHLYWGLWSI 229
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
63-404 1.49e-66

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 214.60  E-value: 1.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  63 CKEFLPGaWRQLQEENFHISVIRGGLSNKLflcsLPDTVKTVADEPCSILLRLYGAilqGTEAMV---MESVMFAILAER 139
Cdd:PLN02421    2 CKALFKG-WSDLDDSDFSVERISGGITNLL----LKVSVKEENGNEVSVTVRLFGP---NTDYVIdreRELQAIKYLSAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 140 SLGPKLYGIFPQGRLEQFIPSRKLETEELHLPELSAEIAGKLAHFHGMKMPFNKEPKwLFGTMEKYLNQVLKIKFSRESH 219
Cdd:PLN02421   74 GFGAKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQ-LWNDIFKFYEKASTVKFEDPEK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 220 VRKLNKLLSYDLPQEMETLWSVLEATYSPVVFCHNDCQEGNILLLEgressEKQKLMLIDFEYSSYNYRGFDIGNHFCEW 299
Cdd:PLN02421  153 QKKYETISFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLMLNE-----DEGKLYFIDFEYGSYSYRGYDIGNHFNEY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 300 M-YDYTYekfpffksnlTKYPTKKEQIHFISSYMAEFQAgfENISNEEksrIEnEMLVEVNRFALASHFFWGLWSILQAK 378
Cdd:PLN02421  228 AgFDCDY----------SLYPSKEEQYHFFRHYLRPDDP--EEVSDAE---LE-ELFVETNFYALASHLYWAIWAIVQAK 291
                         330       340
                  ....*....|....*....|....*.
gi 1694513029 379 ISTIEFGYLEYALARFDAYYQQKRKL 404
Cdd:PLN02421  292 MSPIDFDYLGYFFLRYKEYKRQKEKL 317
PLN02236 PLN02236
choline kinase
49-404 2.68e-64

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 209.13  E-value: 2.68e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  49 ELVDARTRRKAFRWCKEfLPGAWRQ-LQEENFHISVIRGGLSNKLFLCSLPdtvKTVADEPCSILLRLYGailQGTEAMV 127
Cdd:PLN02236    9 GLSSGRIPDELKRILHS-LASKWGDvVDDEALQVIPLKGAMTNEVFQIKWP---TKEGNLGRKVLVRIYG---EGVELFF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 128 M---ESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRKLETEELHLPELSAEIAGKLAHFHGMKMPFNKEPKwLFGTMEK 204
Cdd:PLN02236   82 DrddEIRTFECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 205 YLNQVLKIKFSRESHVRKLNKLlsydlpqEMETlwSVLEATYSPVV----FCHNDCQEGNILLLEgressEKQKLMLIDF 280
Cdd:PLN02236  161 WLKEAKNLCSPEEAKEFRLDSL-------EDEI--NLLEKELSGDDqeigFCHNDLQYGNIMIDE-----ETRAITIIDY 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 281 EYSSYNYRGFDIGNHFCEWMYDYTYEKfPFFKsNLTKYPTKKEQIHFISSYMaefqagfeNISNEEKSRIENEMLVE-VN 359
Cdd:PLN02236  227 EYASYNPVAYDIANHFCEMAADYHSET-PHIL-DYSKYPGEEERRRFIRTYL--------SSSGEEPSDEEVEQLLDdVE 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1694513029 360 RFALASHFFWGLWSILQAKISTIEFGYLEYALARFDAYYQQKRKL 404
Cdd:PLN02236  297 KYTLASHLFWGLWGIISGHVNKIDFDYMEYARQRFEQYWLRKPEL 341
PTZ00296 PTZ00296
choline kinase; Provisional
63-404 8.81e-54

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 184.71  E-value: 8.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  63 CKEFLPGaWRQLQEENFHISVIRGGLSNKLFLCSLP-DTVKTVADEPCSILLRLYGAILQGTEAMVMESVMFAILAERSL 141
Cdd:PTZ00296   93 CLEKVPE-WRRFTEDDVRVNQILSGLTNQLFEVSLKeETANNYPSIRRRVLFRIYGKDVDELYNPISEFEVYKTMSKYRI 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 142 GPKLYGIFPQGRLEQFIPSRKLETEELHLPELSAEIAGKLAHFHGMK----MP--FNKEPKwLFGTMEKYLNQVLKIKFS 215
Cdd:PTZ00296  172 APQLLNTFSGGRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLSrkrhLPehWDRTPC-IFKMMEKWKNQLSKYKNI 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 216 rESHVRKLNKLLsydlpQEME------TLWSVLEATYSPVVFCHNDCQEGNILllegresSEKQKLMLIDFEYSSYNYRG 289
Cdd:PTZ00296  251 -EKYQRDIHKYI-----KESEkfikfmKVYSKSDNLANDIVFCHNDLQENNII-------NTNKCLRLIDFEYSGYNFLA 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 290 FDIGNHFCEWMYDYTYEKFPFFKSNLTKYPTKKEQIHFISSYMAEFqagFENISNEEKSRIENEMLVEVNRFALASHFFW 369
Cdd:PTZ00296  318 TDIANFFIETTIDYSVSHYPFFAIDKKKYISYENRKLFITAYLSNY---LDKSLVVPNPKIIDQILEAVEVQALGAHLLW 394
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1694513029 370 GLWSIL---QAKiSTIEFGYLEYALARFDAYYQQKRKL 404
Cdd:PTZ00296  395 GFWSIIrgyQTK-SYNEFDFFLYAKERFKMYDEQKEYL 431
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
80-301 3.69e-30

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: 113.42  E-value: 3.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  80 HISVIRGGLSNKLFLCSLPDTvktvadepcSILLRLYGAilqGTEAMVM---ESVMFAILAERSLGPKLYGIFPQ--GRL 154
Cdd:cd05151     2 TIEPLKGGLTNKNYLVEVAGK---------KYVLRIPGA---GTELLIDrenEKANSKAAAELGIAPEVIYFDPEtgVKI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 155 EQFIPSRKLETEELHLPELSAEIAGKLAHFHGMKMPfnkepkwlfgtmekylnqvlkikfsreshvrklnkllsydlpqe 234
Cdd:cd05151    70 TEFIEGATLLTNDFSDPENLERIAALLRKLHSSPLE-------------------------------------------- 105
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1694513029 235 metlwsvleatysPVVFCHNDCQEGNILLLEGRessekqkLMLIDFEYSSYNYRGFDIGNHFCEWMY 301
Cdd:cd05151   106 -------------DLVLCHNDLVPGNFLLDDDR-------LYLIDWEYAGMNDPLFDLAALFSENNL 152
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
80-301 1.61e-19

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: 84.66  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  80 HISVIRGGLSNKLFLCSLPDTVktvadepcsiLLRLYGAILQgtEAMVMESVMFAILAERS--LGPKLYGIFP----QGR 153
Cdd:cd05120     2 SVKLIKEGGDNKVYLLGDPREY----------VLKIGPPRLK--KDLEKEAAMLQLLAGKLslPVPKVYGFGEsdgwEYL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 154 LEQFIPSRKLETEELHLPE-----LSAEIAGKLAHFHGMKMPfnkepkwlfgtmekylnqvlkikfsreshvrklnklls 228
Cdd:cd05120    70 LMERIEGETLSEVWPRLSEeekekIADQLAEILAALHRIDSS-------------------------------------- 111
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1694513029 229 ydlpqemetlwsvleatyspvVFCHNDCQEGNILLLEGRESSekqklMLIDFEYSSYNYRGFDIGNHFCEWMY 301
Cdd:cd05120   112 ---------------------VLTHGDLHPGNILVKPDGKLS-----GIIDWEFAGYGPPAFDYAAALRDWTE 158
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
230-394 1.12e-12

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 65.19  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 230 DLPQEMETLWSVLEATYSPVVFCHNDCQEGNILLlegresSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDytyekfp 309
Cdd:COG0510    30 ELLRRLEELERALAARPLPLVLCHGDLHPGNFLV------TDDGRLYLIDWEYAGLGDPAFDLAALLVEYGLS------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 310 ffksnltkyptKKEQIHFISSYmaefqaGFENISNEEKSRIEnemlvevnRFALASHFFWGLWSILQAkISTIEFGYLEY 389
Cdd:COG0510    97 -----------PEQAEELLEAY------GFGRPTEELLRRLR--------AYRALADLLWALWALVRA-AQEANGDLLKY 150

                  ....*
gi 1694513029 390 ALARF 394
Cdd:COG0510   151 LLRRL 155
PTZ00384 PTZ00384
choline kinase; Provisional
135-393 1.26e-10

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 62.49  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 135 ILAERSLGPKLYGIFPQGRLEQFIPSRKLETEELHLPELSAEIAGKLAHFHgmKMPFNKEPK-WLFGTMekYLNQVLKIK 213
Cdd:PTZ00384  108 LLGDNNFGPKIIGRFGDFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFH--KRVTELVPKeWDRTPM--FLTKISTWS 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 214 FSRESHVRKLNKLLSY-DLPQEMETLWSVL-------EATYSPVVFCHNDCQEGNILllegresSEKQKLMLIDFEYSSY 285
Cdd:PTZ00384  184 QHVERIIKKYNLDFDYnELVQNYELFKKILnnhlntsNSITNSVLFCHNDLFFTNIL-------DFNQGIYFIDFDFAGF 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 286 NYRGFDIGNHFCEWMYDYTYEKFPFFKSNLTKYPTKKEQIHFISSYMAEFQAgfENISNEEKsrIENEMLVEVNRFALAS 365
Cdd:PTZ00384  257 NYVGWEIANFFVKLYIVYDPPTPPYFNSDDSLALSEEMKTIFVSVYLSQLLG--KNVLPSDD--LVKEFLQSLEIHTLGV 332
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1694513029 366 HFFWGLWSI---------LQAKISTIEFGYLEYALAR 393
Cdd:PTZ00384  333 NLFWTYWGIvmndkpkneLSKPVKFEAYAKFQYNLFK 369
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
80-299 9.29e-06

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: 46.73  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029  80 HISVIRGGLSNKLFLcslpdtvktVADEPCSILLRLY--GAILQGTEAMVMEsvmFAILAERSLGPK---LYGIFPQGRL 154
Cdd:pfam01636   1 TLRPISSGASNRTYL---------VTTGDGRYVLRLPppGRAAEELRRELAL---LRHLAAAGVPPVprvLAGCTDAELL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 155 E------QFIPSRKLETEELH--LPELSAEIAGKLAHFHG---MKMPFNKEPKWLfgtmekylnqvlkIKFSRESHVRKL 223
Cdd:pfam01636  69 GlpfllmEYLPGEVLARPLLPeeRGALLEALGRALARLHAvdpAALPLAGRLARL-------------LELLRQLEAALA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 224 NKLLSYDLPQEMETLWSVLEA------TYSPVVFCHNDCQEGNILLLEGRESSEkqklmLIDFEYSSYNYRGFDIG---N 294
Cdd:pfam01636 136 RLLAAELLDRLEELEERLLAAllallpAELPPVLVHGDLHPGNLLVDPGGRVSG-----VIDFEDAGLGDPAYDLAillN 210

                  ....*
gi 1694513029 295 HFCEW 299
Cdd:pfam01636 211 SWGRE 215
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
187-345 1.13e-05

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: 46.89  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 187 MKMPFNKEPKWLFG-----TMEKYLNQVLKIKfsreshvRKLNKLLSYDLPQEMETLWSvleatyspvvFCHNDCQEGNI 261
Cdd:TIGR02906 137 KKIALEKKYKDEFDklylkEVDYFLERGKKAL-------ELLNKSKYYDLCKEAKKIRG----------FCHQDYAYHNI 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 262 LLLEGressekqKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKFPFFKSNLTKY----PTKKEQIHFISSYMaEFQA 337
Cdd:TIGR02906 200 LLKDN-------EVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVWDLEKAKEIIEAYssinPLSKEEKEVLYIDL-AFPH 271

                  ....*...
gi 1694513029 338 GFENISNE 345
Cdd:TIGR02906 272 KFWKIGKQ 279
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
141-297 3.83e-05

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: 45.33  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 141 LGPKLYGIFPqgrleqFIPSRKLETeelHLPELSAEIAGKLAHFHG------MKMPFNKEPKWlfgtMEKYLNQVLKIKF 214
Cdd:cd05153    86 LNGKPAALFP------FLPGESLTT---PTPEQCRAIGAALARLHLalagfpPPRPNPRGLAW----WKPLAERLKARLD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 215 SRESHVRKLnklLSYDLPQEMETLWSVLeatysPVVFCHNDCQEGNILLLEGRESSekqklmLIDFEYSSYNYRGFDIG- 293
Cdd:cd05153   153 LLAADDRAL---LEDELARLQALAPSDL-----PRGVIHADLFRDNVLFDGDRLSG------IIDFYDACYDPLLYDLAi 218

                  ....*.
gi 1694513029 294 --NHFC 297
Cdd:cd05153   219 alNDWC 224
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
139-293 3.31e-03

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: 39.14  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 139 RSLGPKLYGIFPqgrleqFIPSRKLETeelHLPELSAEIAGKLAHFH----GMKMPFNKEPKWLFGTMEKylnqvLKIKF 214
Cdd:COG2334    84 LELEGRPAALFP------FLPGRSPEE---PSPEQLEELGRLLARLHralaDFPRPNARDLAWWDELLER-----LLGPL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694513029 215 SRESHVRKLnkllsydLPQEMETLWSVLEATYSPVVF--CHNDCQEGNILLLEGRESsekqklMLIDFEYSSYNYRGFDI 292
Cdd:COG2334   150 LPDPEDRAL-------LEELLDRLEARLAPLLGALPRgvIHGDLHPDNVLFDGDGVS------GLIDFDDAGYGPRLYDL 216

                  .
gi 1694513029 293 G 293
Cdd:COG2334   217 A 217
 
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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