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Conserved domains on  [gi|504458430|ref|WP_014645532|]
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phosphotransferase enzyme family protein [Stenotrophomonas muris]

Protein Classification

phosphotransferase enzyme family protein( domain architecture ID 11457111)

phosphotransferase enzyme family protein such as serine/threonine protein kinase RdoA, type II homoserine kinase, N-acetylhexosamine 1-kinase, hydroxylysine kinase, and amicoumacin kinase, all of which play crucial roles in transferring phosphate groups to specific substrates

CATH:  1.10.510.10
Gene Ontology:  GO:0016301|GO:0005524|GO:0016310
PubMed:  16244704
SCOP:  3000066

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
58-318 1.55e-32

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: 123.50  E-value: 1.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  58 VDDTRGAVFI-KRHHHSVRSAACLEEEHHFIAHLAAAGVPVVQVLPATDGHTAVEHGEWTFELHDvgvgddlYRDAVSWS 136
Cdd:COG2334   31 VETEDGRRYVlKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPTRDGETLLELEGRPAALFP-------FLPGRSPE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 137 LLTDvAQAREAGRTLAQLHRAAASYHAPQRSthllvardDLIRADDPIAAIKAGLDERPGLARYLARIpWEAQLQRdvlp 216
Cdd:COG2334  104 EPSP-EQLEELGRLLARLHRALADFPRPNAR--------DLAWWDELLERLLGPLLPDPEDRALLEEL-LDRLEAR---- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 217 whagLAERLRAEPRLWAHNDWHVSNLLWRNGEVSTVLDFGLASPTSALFDLATAIerNAVAWLELergreavRIDIALAL 296
Cdd:COG2334  170 ----LAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIAL--NGWADGPL-------DPARLAAL 236
                        250       260
                 ....*....|....*....|..
gi 504458430 297 LDGYREVLPLSAARVHLLADLL 318
Cdd:COG2334  237 LEGYRAVRPLTEAELAALPPLL 258
 
Name Accession Description Interval E-value
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
58-318 1.55e-32

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: 123.50  E-value: 1.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  58 VDDTRGAVFI-KRHHHSVRSAACLEEEHHFIAHLAAAGVPVVQVLPATDGHTAVEHGEWTFELHDvgvgddlYRDAVSWS 136
Cdd:COG2334   31 VETEDGRRYVlKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPTRDGETLLELEGRPAALFP-------FLPGRSPE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 137 LLTDvAQAREAGRTLAQLHRAAASYHAPQRSthllvardDLIRADDPIAAIKAGLDERPGLARYLARIpWEAQLQRdvlp 216
Cdd:COG2334  104 EPSP-EQLEELGRLLARLHRALADFPRPNAR--------DLAWWDELLERLLGPLLPDPEDRALLEEL-LDRLEAR---- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 217 whagLAERLRAEPRLWAHNDWHVSNLLWRNGEVSTVLDFGLASPTSALFDLATAIerNAVAWLELergreavRIDIALAL 296
Cdd:COG2334  170 ----LAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIAL--NGWADGPL-------DPARLAAL 236
                        250       260
                 ....*....|....*....|..
gi 504458430 297 LDGYREVLPLSAARVHLLADLL 318
Cdd:COG2334  237 LEGYRAVRPLTEAELAALPPLL 258
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
57-318 1.68e-25

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: 104.65  E-value: 1.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  57 IVDDTRGAVFIKRHHHsVRSAACLEEEHHFIAHLAAAGVPVVQVLPATDGHTAVEHGEWTFELHDVGVGDDLYRDavsws 136
Cdd:cd05153   32 FVTTTDGRYVLTLFEK-RRSAAELPFELELLDHLAQAGLPVPRPLADKDGELLGELNGKPAALFPFLPGESLTTP----- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 137 lltDVAQAREAGRTLAQLHRAAASYHAPQRSTHLLVARDDLIRADDPIAAIKAGlDERPGLARYLARIPweaqlqrdvlp 216
Cdd:cd05153  106 ---TPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWWKPLAERLKARLDLLAA-DDRALLEDELARLQ----------- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 217 whaglAERLRAEPRLWAHNDWHVSNLLWRNGEVSTVLDFGLASPTSALFDLATAIernaVAWLELERGREavRIDIALAL 296
Cdd:cd05153  171 -----ALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIAL----NDWCFDDDGKL--DPERAKAL 239
                        250       260
                 ....*....|....*....|..
gi 504458430 297 LDGYREVLPLSAARVHLLADLL 318
Cdd:cd05153  240 LAGYQSVRPLTEEEKAALPLLL 261
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
58-306 7.15e-14

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: 70.61  E-value: 7.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430   58 VDDTRGAVFIKRHHHSvRSAACLEEEHHFIAHLAAAGV-PVVQVLpatDGHTAVEHGEWTFELHDVGVGDDLYRDAVSWS 136
Cdd:pfam01636  16 VTTGDGRYVLRLPPPG-RAAEELRRELALLRHLAAAGVpPVPRVL---AGCTDAELLGLPFLLMEYLPGEVLARPLLPEE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  137 LltdVAQAREAGRTLAQLHRAAASYHAPQRSTHLLVARDDLIRADDpIAAIKAGLDERPglarylaripweAQLQRDVLP 216
Cdd:pfam01636  92 R---GALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAAL-ARLLAAELLDRL------------EELEERLLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  217 WHagLAERLRAEPRLWAHNDWHVSNLLWR-NGEVSTVLDFGLASPTSALFDLATaiernAVAWLELERGREAVRIDIALA 295
Cdd:pfam01636 156 AL--LALLPAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAI-----LLNSWGRELGAELLAAYLAAY 228
                         250
                  ....*....|.
gi 504458430  296 LLDGYREVLPL 306
Cdd:pfam01636 229 GAFGYARLREL 239
PRK05231 PRK05231
homoserine kinase; Provisional
88-318 1.10e-09

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 59.04  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  88 AHLAAAGVPVVQVLPATDGHTAvehgewtFELHDvgvgddlyRDAV-------SWSLLTDVAQAREAGRTLAQLHRAAAS 160
Cdd:PRK05231  69 QHLAARGVPVPAPVARRDGAAL-------GELAG--------KPAAivtflegKWPRAPTAAHCAEVGEMLARMHLAGRD 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 161 YHAPQRSTHLLVARDDLIraddPIAAIKAGLDERPGLARylaripwEAQLQRDVLPWHAglAERLraePRLWAHNDWHVS 240
Cdd:PRK05231 134 FPLERPNLRGLAWWRELA----PRLLPFLADEQAALLEA-------ELAAQLAFLASAA--WPAL---PRGVIHADLFRD 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504458430 241 NLLWRNGEVSTVLDFGLASPTSALFDLATAIerNavAW-LELERGREAVRidiALALLDGYREVLPLSAARVHLLADLL 318
Cdd:PRK05231 198 NVLFEGDRLSGFIDFYFACNDKLLYDVAITL--N--DWcFEADGSLDATK---ARALLAAYQSVRPLTAAERAALPVML 269
 
Name Accession Description Interval E-value
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
58-318 1.55e-32

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: 123.50  E-value: 1.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  58 VDDTRGAVFI-KRHHHSVRSAACLEEEHHFIAHLAAAGVPVVQVLPATDGHTAVEHGEWTFELHDvgvgddlYRDAVSWS 136
Cdd:COG2334   31 VETEDGRRYVlKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPTRDGETLLELEGRPAALFP-------FLPGRSPE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 137 LLTDvAQAREAGRTLAQLHRAAASYHAPQRSthllvardDLIRADDPIAAIKAGLDERPGLARYLARIpWEAQLQRdvlp 216
Cdd:COG2334  104 EPSP-EQLEELGRLLARLHRALADFPRPNAR--------DLAWWDELLERLLGPLLPDPEDRALLEEL-LDRLEAR---- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 217 whagLAERLRAEPRLWAHNDWHVSNLLWRNGEVSTVLDFGLASPTSALFDLATAIerNAVAWLELergreavRIDIALAL 296
Cdd:COG2334  170 ----LAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIAL--NGWADGPL-------DPARLAAL 236
                        250       260
                 ....*....|....*....|..
gi 504458430 297 LDGYREVLPLSAARVHLLADLL 318
Cdd:COG2334  237 LEGYRAVRPLTEAELAALPPLL 258
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
57-318 1.68e-25

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: 104.65  E-value: 1.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  57 IVDDTRGAVFIKRHHHsVRSAACLEEEHHFIAHLAAAGVPVVQVLPATDGHTAVEHGEWTFELHDVGVGDDLYRDavsws 136
Cdd:cd05153   32 FVTTTDGRYVLTLFEK-RRSAAELPFELELLDHLAQAGLPVPRPLADKDGELLGELNGKPAALFPFLPGESLTTP----- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 137 lltDVAQAREAGRTLAQLHRAAASYHAPQRSTHLLVARDDLIRADDPIAAIKAGlDERPGLARYLARIPweaqlqrdvlp 216
Cdd:cd05153  106 ---TPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWWKPLAERLKARLDLLAA-DDRALLEDELARLQ----------- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 217 whaglAERLRAEPRLWAHNDWHVSNLLWRNGEVSTVLDFGLASPTSALFDLATAIernaVAWLELERGREavRIDIALAL 296
Cdd:cd05153  171 -----ALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIAL----NDWCFDDDGKL--DPERAKAL 239
                        250       260
                 ....*....|....*....|..
gi 504458430 297 LDGYREVLPLSAARVHLLADLL 318
Cdd:cd05153  240 LAGYQSVRPLTEEEKAALPLLL 261
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
58-306 7.15e-14

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: 70.61  E-value: 7.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430   58 VDDTRGAVFIKRHHHSvRSAACLEEEHHFIAHLAAAGV-PVVQVLpatDGHTAVEHGEWTFELHDVGVGDDLYRDAVSWS 136
Cdd:pfam01636  16 VTTGDGRYVLRLPPPG-RAAEELRRELALLRHLAAAGVpPVPRVL---AGCTDAELLGLPFLLMEYLPGEVLARPLLPEE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  137 LltdVAQAREAGRTLAQLHRAAASYHAPQRSTHLLVARDDLIRADDpIAAIKAGLDERPglarylaripweAQLQRDVLP 216
Cdd:pfam01636  92 R---GALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAAL-ARLLAAELLDRL------------EELEERLLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  217 WHagLAERLRAEPRLWAHNDWHVSNLLWR-NGEVSTVLDFGLASPTSALFDLATaiernAVAWLELERGREAVRIDIALA 295
Cdd:pfam01636 156 AL--LALLPAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAI-----LLNSWGRELGAELLAAYLAAY 228
                         250
                  ....*....|.
gi 504458430  296 LLDGYREVLPL 306
Cdd:pfam01636 229 GAFGYARLREL 239
PRK05231 PRK05231
homoserine kinase; Provisional
88-318 1.10e-09

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 59.04  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  88 AHLAAAGVPVVQVLPATDGHTAvehgewtFELHDvgvgddlyRDAV-------SWSLLTDVAQAREAGRTLAQLHRAAAS 160
Cdd:PRK05231  69 QHLAARGVPVPAPVARRDGAAL-------GELAG--------KPAAivtflegKWPRAPTAAHCAEVGEMLARMHLAGRD 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 161 YHAPQRSTHLLVARDDLIraddPIAAIKAGLDERPGLARylaripwEAQLQRDVLPWHAglAERLraePRLWAHNDWHVS 240
Cdd:PRK05231 134 FPLERPNLRGLAWWRELA----PRLLPFLADEQAALLEA-------ELAAQLAFLASAA--WPAL---PRGVIHADLFRD 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504458430 241 NLLWRNGEVSTVLDFGLASPTSALFDLATAIerNavAW-LELERGREAVRidiALALLDGYREVLPLSAARVHLLADLL 318
Cdd:PRK05231 198 NVLFEGDRLSGFIDFYFACNDKLLYDVAITL--N--DWcFEADGSLDATK---ARALLAAYQSVRPLTAAERAALPVML 269
PRK06148 PRK06148
hypothetical protein; Provisional
63-320 3.72e-08

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 55.42  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430   63 GAVFIKRHHHSVRSAACLEEEHHFIAHLAAAG--VPVVQVLPATDGHTAVEHGEWTFELHDVGVgddlyrdaVSW---SL 137
Cdd:PRK06148   48 GADYILKIVNPSEPRVESDFQTAALDHLAAVApdLPVPRLIPSLSGASLASAQDPDGEPRLLRL--------LSWlpgTP 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  138 LTDVAQAREA-----GRTLAQLHRAAASYHAPQrsthllVARD---DLIRAD---DPIAAIkAGLDERPGLARYLARipw 206
Cdd:PRK06148  120 LAEAAPRTEAlldnlGRALGRLDRALQGFMHPG------ALRDldwDLRHAGrarDRLHFI-DDPEDRALVERFLAR--- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  207 eaqLQRDVLPwhaglaeRLRAEPRLWAHNDWHVSNLLWR---NGEVSTVLDFGLASPTSALFDLATAierNAVAWLELER 283
Cdd:PRK06148  190 ---FERNVAP-------RLAALPAQVIHNDANDYNILVDaddGERISGLIDFGDAVHAPRICEVAIA---AAYAILDHPD 256
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 504458430  284 GREAvridiALALLDGYREVLPLSAARVHLLADLLPM 320
Cdd:PRK06148  257 PIGA-----AAALVAGYHAVYPLQAQELDLLFDLIRM 288
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
29-316 1.32e-07

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 52.42  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  29 AWLSTRYPQLGGHSQPRWHSPRpLSAAAIVDDTRGAVFIKRHHHSVRSAACLEEEHHFIAHLAA-AGVPVVQVLPATDGH 107
Cdd:COG3173   10 ALLAAQLPGLAGLPEVEPLSGG-WSNLTYRLDTGDRLVLRRPPRGLASAHDVRREARVLRALAPrLGVPVPRPLALGEDG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 108 tavEHGEWTFELHDVGVGDDLYRDAVSWSLLTDVAQAREAGRTLAQLHRAAAsyhapqrsthllvarddlirADDPIAAI 187
Cdd:COG3173   89 ---EVIGAPFYVMEWVEGETLEDALPDLSPAERRALARALGEFLAALHAVDP--------------------AAAGLADG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 188 KAGLDERPgLARYLARIPWEAQLQRDVLPWHAGLAERLRA-----EPRLWAHNDWHVSNLLWR--NGEVSTVLDFGLASP 260
Cdd:COG3173  146 RPEGLERQ-LARWRAQLRRALARTDDLPALRERLAAWLAAnlpewGPPVLVHGDLRPGNLLVDpdDGRLTAVIDWELATL 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504458430 261 TSALFDLATAiernAVAWLELERGREAVRidialALLDGYREVL-PLSAARVHLLAD 316
Cdd:COG3173  225 GDPAADLAYL----LLYWRLPDDLLGPRA-----AFLAAYEEATgDLDDLTWWALAD 272
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
144-289 4.68e-06

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include 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). These proteins 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-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: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 47.23  E-value: 4.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 144 AREAGRTLAQLHRAAASyHAPQRSTHLLVARDDLIRADDPIAAIKAGLDERPGLARYLaripWEAQLQrdvLPWHAGlae 223
Cdd:cd05155   93 AEDLARFLAALHAIDPA-GPPNPGRGNPLRGRDLAVRDAEEALAALAGLLDVAAARAL----WERALA---APAWAG--- 161
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504458430 224 rlraePRLWAHNDWHVSNLLWRNGEVSTVLDFGLASPTSALFDLataiernAVAWLEL-ERGREAVR 289
Cdd:cd05155  162 -----PPVWLHGDLHPGNLLVRDGRLSAVIDFGDLGVGDPACDL-------AIAWTLFdAAARAAFR 216
PRK11768 PRK11768
serine/threonine protein kinase;
76-323 3.95e-05

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 45.16  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  76 SAACLEEEHHFIAHLAAAGVPVVQVLpATDGHTAVEHGEWTFELH--------DVGVGDDLYRdavswslltdvaqareA 147
Cdd:PRK11768  63 SDAQILEEHAFALELAEAEIPVVAPL-AFNGQTLHEHQGFRFALFprrggrapELDNLDQLEW----------------V 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 148 GRTLAQLHRAAASYHAPQR-----STHLLVARDDLIRADdpiaAIKAGLderpgLARYLARIpweaqlqRDVLpwhAGLA 222
Cdd:PRK11768 126 GRFLGRIHQVGAKRPFEHRptldlQEYGIEPRDWLLASD----LIPSDL-----RPAYLAAA-------DQLL---AAVE 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 223 ERLRAEP----RLwaHNDWHVSNLLWRNGevSTVLDfglasptsalFDLAtaieRNAVA----WLELERGREAVRIDIAl 294
Cdd:PRK11768 187 ACWARGDvrllRL--HGDCHPGNILWRDG--PHFVD----------LDDA----RMGPAvqdlWMLLSGDRAEQLMQLE- 247
                        250       260       270
                 ....*....|....*....|....*....|.
gi 504458430 295 ALLDGYREVLPLSAARVHLLADL--LPMVHF 323
Cdd:PRK11768 248 TLLEGYEEFCEFDPRELALIEPLraLRLIHY 278
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
232-308 1.12e-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: 39.17  E-value: 1.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504458430 232 WAHNDWHVSNLLWRNGEVsTVLDFGLASPTSALFDLATAIernAVAWLELERGREAVRIDIALALLDGYREVLPLSA 308
Cdd:COG3642   72 IVHGDLTTSNILVDDGGV-YLIDFGLARYSDPLEDKAVDL---AVLKRSLESTHPDPAEELWEAFLEGYREVGPAEE 144
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
39-271 7.86e-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: 37.60  E-value: 7.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430  39 GGHSQPRWhsprpLSAAAIVDDTRGAVF-IKRHHHSVRSAACLEEEHHFIAHLAAAGVPVVQVL-----PATDGHTAV-- 110
Cdd:cd05154    8 GGASNETY-----LVDAGGDGGGRRLVLrRPPPGGLLPSAHDLEREYRVLRALAGTGVPVPRVLalcedPSVLGAPFYvm 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 111 EH--GEWtfeLHDVGVGDDLYRDAVSwslltdvAQAREAGRTLAQLHRAaasyhapqrsthllvarddliraddPIAAIK 188
Cdd:cd05154   83 ERvdGRV---LPDPLPRPDLSPEERR-------ALARSLVDALAALHSV-------------------------DPAALG 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504458430 189 AGLDERPG--LARYLARipWEAQLQ---RDVLPWHAGLAERLRA------EPRLwAHNDWHVSNLLWR-NGEVSTVLDFG 256
Cdd:cd05154  128 LADLGRPEgyLERQVDR--WRRQLEaaaTDPPPALEEALRWLRAnlpadgRPVL-VHGDFRLGNLLFDpDGRVTAVLDWE 204
                        250
                 ....*....|....*
gi 504458430 257 LASPTSALFDLATAI 271
Cdd:cd05154  205 LATLGDPLEDLAWLL 219
 
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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