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Conserved domains on  [gi|494151474|ref|WP_007091219|]
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hypothetical protein [Thalassospira xiamenensis]

Protein Classification

serine/threonine-protein kinase( domain architecture ID 10007648)

serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 72-234 8.94e-18

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: 78.08  E-value: 8.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474  72 LASEAEILHALNRADVLVPDLLEV--ADNWIAIGDngaILQTVISDAVKAGDEDrvAELIAKAGAALADLHISGFTHGAP 149
Cdd:COG3642    3 TRREARLLRELREAGVPVPKVLDVdpDDADLVMEY---IEGETLADLLEEGELP--PELLRELGRLLARLHRAGIVHGDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474 150 LLRNMtIRDDGRVGFIDFEEDPnKRMPLPDaQARDVLLFLFSIQR-GFKRRPDLLRAGWRAYLvvtgmtapQMKPLSHIV 228
Cdd:COG3642   78 TTSNI-LVDDGGVYLIDFGLAR-YSDPLED-KAVDLAVLKRSLEStHPDPAEELWEAFLEGYR--------EVGPAEEVL 146


                 ....*.
gi 494151474 229 RVIRPV 234
Cdd:COG3642  147 RRLREI 152
 
Name Accession Description Interval E-value
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 72-234 8.94e-18

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: 78.08  E-value: 8.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474  72 LASEAEILHALNRADVLVPDLLEV--ADNWIAIGDngaILQTVISDAVKAGDEDrvAELIAKAGAALADLHISGFTHGAP 149
Cdd:COG3642    3 TRREARLLRELREAGVPVPKVLDVdpDDADLVMEY---IEGETLADLLEEGELP--PELLRELGRLLARLHRAGIVHGDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474 150 LLRNMtIRDDGRVGFIDFEEDPnKRMPLPDaQARDVLLFLFSIQR-GFKRRPDLLRAGWRAYLvvtgmtapQMKPLSHIV 228
Cdd:COG3642   78 TTSNI-LVDDGGVYLIDFGLAR-YSDPLED-KAVDLAVLKRSLEStHPDPAEELWEAFLEGYR--------EVGPAEEVL 146


                 ....*.
gi 494151474 229 RVIRPV 234
Cdd:COG3642  147 RRLREI 152
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 12-167 1.57e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 47.59  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474   12 TIAQGVGARVFPLRWKGRRIWIKQAVPpkeKGWhrlqrfvatltRIP----MLRptvspggKAGLASEAEILHALNRADV 87
Cdd:TIGR03724   1 LIAKGAEAIIYLGDFLGRKAVIKERVP---KSY-----------RHPeldeRLR-------KERTRREARLLSRARKAGV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474   88 LVPDLLEVADNWIAIgdngaILQTVISDAVKAGDEDRVAELIAKAGAALADLHISGFTHGAPLLRNMTIRDDgRVGFIDF 167
Cdd:TIGR03724  60 NTPVIYDVDPDNKTI-----VMEYIEGKPLKDVIEENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDD-KVYLIDF 133
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
7-167 1.63e-05

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 45.65  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474   7 DIVEQTIAQGVGARVFPLRWKGRRIWIKQAVPpkeKGWhrlqrfvatltRIP----MLRptvspggKAGLASEAEILHAL 82
Cdd:PRK09605 335 KIPDHLIGKGAEADIKKGEYLGRDAVIKERVP---KGY-----------RHPeldeRLR-------TERTRAEARLLSEA 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474  83 NRADVLVPDLLEVADnwiaigDNGAILQTVISDAVKAGDEDRVAELIAKAGAALADLHISGFTHGAPLLRNMTIRDDgRV 162
Cdd:PRK09605 394 RRAGVPTPVIYDVDP------EEKTIVMEYIGGKDLKDVLEGNPELVRKVGEIVAKLHKAGIVHGDLTTSNFIVRDD-RL 466


                 ....*
gi 494151474 163 GFIDF 167
Cdd:PRK09605 467 YLIDF 471
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 68-168 2.88e-04

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: 40.36  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474  68 GKAGLASEAEILHALN-RADVLVPDLLEVADNwiaiGDNGAILQTVI-----SDAVKAGDEDRVAELIAKAGAALADLH- 140
Cdd:cd05120   32 LKKDLEKEAAMLQLLAgKLSLPVPKVYGFGES----DGWEYLLMERIegetlSEVWPRLSEEEKEKIADQLAEILAALHr 107

                         90       100       110
                 ....*....|....*....|....*....|.
gi 494151474 141 --ISGFTHGAPLLRNMTIRDDGRV-GFIDFE 168
Cdd:cd05120  108 idSSVLTHGDLHPGNILVKPDGKLsGIIDWE 138
 
Name Accession Description Interval E-value
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 72-234 8.94e-18

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: 78.08  E-value: 8.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474  72 LASEAEILHALNRADVLVPDLLEV--ADNWIAIGDngaILQTVISDAVKAGDEDrvAELIAKAGAALADLHISGFTHGAP 149
Cdd:COG3642    3 TRREARLLRELREAGVPVPKVLDVdpDDADLVMEY---IEGETLADLLEEGELP--PELLRELGRLLARLHRAGIVHGDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474 150 LLRNMtIRDDGRVGFIDFEEDPnKRMPLPDaQARDVLLFLFSIQR-GFKRRPDLLRAGWRAYLvvtgmtapQMKPLSHIV 228
Cdd:COG3642   78 TTSNI-LVDDGGVYLIDFGLAR-YSDPLED-KAVDLAVLKRSLEStHPDPAEELWEAFLEGYR--------EVGPAEEVL 146


                 ....*.
gi 494151474 229 RVIRPV 234
Cdd:COG3642  147 RRLREI 152
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 12-167 1.57e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 47.59  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474   12 TIAQGVGARVFPLRWKGRRIWIKQAVPpkeKGWhrlqrfvatltRIP----MLRptvspggKAGLASEAEILHALNRADV 87
Cdd:TIGR03724   1 LIAKGAEAIIYLGDFLGRKAVIKERVP---KSY-----------RHPeldeRLR-------KERTRREARLLSRARKAGV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474   88 LVPDLLEVADNWIAIgdngaILQTVISDAVKAGDEDRVAELIAKAGAALADLHISGFTHGAPLLRNMTIRDDgRVGFIDF 167
Cdd:TIGR03724  60 NTPVIYDVDPDNKTI-----VMEYIEGKPLKDVIEENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDD-KVYLIDF 133
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
7-167 1.63e-05

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 45.65  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474   7 DIVEQTIAQGVGARVFPLRWKGRRIWIKQAVPpkeKGWhrlqrfvatltRIP----MLRptvspggKAGLASEAEILHAL 82
Cdd:PRK09605 335 KIPDHLIGKGAEADIKKGEYLGRDAVIKERVP---KGY-----------RHPeldeRLR-------TERTRAEARLLSEA 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474  83 NRADVLVPDLLEVADnwiaigDNGAILQTVISDAVKAGDEDRVAELIAKAGAALADLHISGFTHGAPLLRNMTIRDDgRV 162
Cdd:PRK09605 394 RRAGVPTPVIYDVDP------EEKTIVMEYIGGKDLKDVLEGNPELVRKVGEIVAKLHKAGIVHGDLTTSNFIVRDD-RL 466


                 ....*
gi 494151474 163 GFIDF 167
Cdd:PRK09605 467 YLIDF 471
PRK14879 PRK14879
Kae1-associated kinase Bud32;
13-215 2.19e-05

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 44.51  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474  13 IAQGVGARVFPLRWKGRRIWIKQAVPpkeKGWhrlqrfvatltRIPML------RPTVSpggkaglasEAEILHALNRAD 86
Cdd:PRK14879   4 IKRGAEAEIYLGDFLGIKAVIKWRIP---KRY-----------RHPELderirrERTRR---------EARIMSRARKAG 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474  87 VLVPDLLEVADNwiaigdNGAILQTVI-----SDAVKAGdEDRVAELIAKAGAALADLHISGFTHGAPLLRNMtIRDDGR 161
Cdd:PRK14879  61 VNVPAVYFVDPE------NFIIVMEYIegeplKDLINSN-GMEELELSREIGRLVGKLHSAGIIHGDLTTSNM-ILSGGK 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494151474 162 VGFIDF--EEDPNKrmplPDAQARDVLLFLFSIQRGFKRRPD-LLRAGWRAYLVVTG 215
Cdd:PRK14879 133 IYLIDFglAEFSKD----LEDRAVDLHVLLRSLESTHPDWAEeLFEAFLEGYREVMG 185
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 68-168 2.88e-04

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: 40.36  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494151474  68 GKAGLASEAEILHALN-RADVLVPDLLEVADNwiaiGDNGAILQTVI-----SDAVKAGDEDRVAELIAKAGAALADLH- 140
Cdd:cd05120   32 LKKDLEKEAAMLQLLAgKLSLPVPKVYGFGES----DGWEYLLMERIegetlSEVWPRLSEEEKEKIADQLAEILAALHr 107

                         90       100       110
                 ....*....|....*....|....*....|.
gi 494151474 141 --ISGFTHGAPLLRNMTIRDDGRV-GFIDFE 168
Cdd:cd05120  108 idSSVLTHGDLHPGNILVKPDGKLsGIIDWE 138
 
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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