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Conserved domains on  [gi|665408573|ref|NP_001286053|]
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uncharacterized protein Dmel_CG31751, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06148 super family cl32120
hypothetical protein; Provisional
64-392 6.13e-49

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PRK06148:

Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 178.68  E-value: 6.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573   64 PKVEPEDVESLLRRLYGITisevKEIVAYD---DRNFFVKEDSNVknplivthcphGYVLKILNSLDSKKEdfVDAQNQM 140
Cdd:PRK06148    9 PEFTTKDAEALLAQHFGIS----ATATPLDgerDLNFRLTTDDGA-----------DYILKIVNPSEPRVE--SDFQTAA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  141 LLYLGKHS--VKCPRPVANATGKYY-SVERLNGNSNVVRLLEFIPGEIF-HQVPVTKHLLYRSGEYLARLDRALKNFTHQ 216
Cdd:PRK06148   72 LDHLAAVApdLPVPRLIPSLSGASLaSAQDPDGEPRLLRLLSWLPGTPLaEAAPRTEALLDNLGRALGRLDRALQGFMHP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  217 AYeSHKTLWMLQSVPELRQFLYVVKDQEQRLICDEVIDAFEAKVLSQLPSMEHQIIHGDFNEQNIVVEQvpnQTEYTIKG 296
Cdd:PRK06148  152 GA-LRDLDWDLRHAGRARDRLHFIDDPEDRALVERFLARFERNVAPRLAALPAQVIHNDANDYNILVDA---DDGERISG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  297 VIDFGDTSKSPLIFEIGIALTYMILQAND-LANGGIFLSGYTSLNPIENSELALLKYCVTARFVQSLVMGLYTHTLHPTN 375
Cdd:PRK06148  228 LIDFGDAVHAPRICEVAIAAAYAILDHPDpIGAAAALVAGYHAVYPLQAQELDLLFDLIRMRLAVSVTNSASRREQTPDN 307
                         330
                  ....*....|....*..
gi 665408573  376 EYLLVTQEKGWKLLQKL 392
Cdd:PRK06148  308 PYLAISEAPAWRLLERL 324
 
Name Accession Description Interval E-value
PRK06148 PRK06148
hypothetical protein; Provisional
64-392 6.13e-49

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 178.68  E-value: 6.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573   64 PKVEPEDVESLLRRLYGITisevKEIVAYD---DRNFFVKEDSNVknplivthcphGYVLKILNSLDSKKEdfVDAQNQM 140
Cdd:PRK06148    9 PEFTTKDAEALLAQHFGIS----ATATPLDgerDLNFRLTTDDGA-----------DYILKIVNPSEPRVE--SDFQTAA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  141 LLYLGKHS--VKCPRPVANATGKYY-SVERLNGNSNVVRLLEFIPGEIF-HQVPVTKHLLYRSGEYLARLDRALKNFTHQ 216
Cdd:PRK06148   72 LDHLAAVApdLPVPRLIPSLSGASLaSAQDPDGEPRLLRLLSWLPGTPLaEAAPRTEALLDNLGRALGRLDRALQGFMHP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  217 AYeSHKTLWMLQSVPELRQFLYVVKDQEQRLICDEVIDAFEAKVLSQLPSMEHQIIHGDFNEQNIVVEQvpnQTEYTIKG 296
Cdd:PRK06148  152 GA-LRDLDWDLRHAGRARDRLHFIDDPEDRALVERFLARFERNVAPRLAALPAQVIHNDANDYNILVDA---DDGERISG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  297 VIDFGDTSKSPLIFEIGIALTYMILQAND-LANGGIFLSGYTSLNPIENSELALLKYCVTARFVQSLVMGLYTHTLHPTN 375
Cdd:PRK06148  228 LIDFGDAVHAPRICEVAIAAAYAILDHPDpIGAAAALVAGYHAVYPLQAQELDLLFDLIRMRLAVSVTNSASRREQTPDN 307
                         330
                  ....*....|....*..
gi 665408573  376 EYLLVTQEKGWKLLQKL 392
Cdd:PRK06148  308 PYLAISEAPAWRLLERL 324
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
69-391 1.84e-44

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: 156.24  E-value: 1.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  69 EDVESLLRRlYGI-TISEVKEIVAYDDRNFFVKEDSNVKnplivthcphgYVLKILNSLDSKKEDfVDAQNQMLLYLGKH 147
Cdd:COG2334    1 DELAAALER-YGLgPLSSLKPLNSGENRNYRVETEDGRR-----------YVLKLYRPGRWSPEE-IPFELALLAHLAAA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 148 SVKCPRPVANATGKYysVERLNGNsnVVRLLEFIPGEIFHQVpvTKHLLYRSGEYLARLDRALKNFTHQAyeSHKTLWML 227
Cdd:COG2334   68 GLPVPAPVPTRDGET--LLELEGR--PAALFPFLPGRSPEEP--SPEQLEELGRLLARLHRALADFPRPN--ARDLAWWD 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 228 QSVPELRQFLyvVKDQEQRLICDEVIDAFEAKVLSQLPSMEHQIIHGDFNEQNIVV--EQVPnqteytikGVIDFGDTSK 305
Cdd:COG2334  140 ELLERLLGPL--LPDPEDRALLEELLDRLEARLAPLLGALPRGVIHGDLHPDNVLFdgDGVS--------GLIDFDDAGY 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 306 SPLIFEIGIALTYMILQANDLANGGIFLSGYTSLNPIENSELALLKYCVTARFVQSLVMGLY-THTLHPTN-EYLLVTQE 383
Cdd:COG2334  210 GPRLYDLAIALNGWADGPLDPARLAALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRrVRAKDPAFeRYLRRQIA 289

                 ....*...
gi 665408573 384 KGWKLLQK 391
Cdd:COG2334  290 LAWAALEA 297
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
68-350 1.97e-33

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: 126.99  E-value: 1.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  68 PEDVESLLRRlYGI-TISEVKEIVA-YDDRNFFVkedsnvknplivtHCPHG-YVLKILNSLDSKKEdfVDAQNQMLLYL 144
Cdd:cd05153    1 DEELAEFLAH-YDLgELLSFEGIAAgIENTNYFV-------------TTTDGrYVLTLFEKRRSAAE--LPFELELLDHL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 145 GKHSVKCPRPVANATGKYYSveRLNGNsnVVRLLEFIPGEifHQVPVTKHLLYRSGEYLARLDRALKNFTHQAYESHKTL 224
Cdd:cd05153   65 AQAGLPVPRPLADKDGELLG--ELNGK--PAALFPFLPGE--SLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 225 WMLQSVPELRQFLYVVKDQEQRLICDEvIDAFEAKVLSQLPsmeHQIIHGDFNEQNIVVEqvpnqtEYTIKGVIDFGDTS 304
Cdd:cd05153  139 WWKPLAERLKARLDLLAADDRALLEDE-LARLQALAPSDLP---RGVIHADLFRDNVLFD------GDRLSGIIDFYDAC 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 665408573 305 KSPLIFEIGIALTYMILQANDLANGG---IFLSGYTSLNPIENSELALL 350
Cdd:cd05153  209 YDPLLYDLAIALNDWCFDDDGKLDPErakALLAGYQSVRPLTEEEKAAL 257
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
92-318 2.95e-20

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: 89.10  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573   92 YDDRNFFVKEDsnvKNPLIVTHCPHGYVLkilnsldskkeDFVDAQNQMLLYLGKHSV-KCPRPVAnatgkYYSVERLNG 170
Cdd:pfam01636   9 ASNRTYLVTTG---DGRYVLRLPPPGRAA-----------EELRRELALLRHLAAAGVpPVPRVLA-----GCTDAELLG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  171 NsnVVRLLEFIPGEIFHQVP---VTKHLLYRSGEYLARLDRALKNFTHQAYESHKTLWMLQSVPELRQFLYVVKDQEQRL 247
Cdd:pfam01636  70 L--PFLLMEYLPGEVLARPLlpeERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLE 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408573  248 ICDE-VIDAFEAKVLSQLPSmehQIIHGDFNEQNIVVEQvPNQteytIKGVIDFGDTSKSPLIFEIGIALTY 318
Cdd:pfam01636 148 ELEErLLAALLALLPAELPP---VLVHGDLHPGNLLVDP-GGR----VSGVIDFEDAGLGDPAYDLAILLNS 211
 
Name Accession Description Interval E-value
PRK06148 PRK06148
hypothetical protein; Provisional
64-392 6.13e-49

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 178.68  E-value: 6.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573   64 PKVEPEDVESLLRRLYGITisevKEIVAYD---DRNFFVKEDSNVknplivthcphGYVLKILNSLDSKKEdfVDAQNQM 140
Cdd:PRK06148    9 PEFTTKDAEALLAQHFGIS----ATATPLDgerDLNFRLTTDDGA-----------DYILKIVNPSEPRVE--SDFQTAA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  141 LLYLGKHS--VKCPRPVANATGKYY-SVERLNGNSNVVRLLEFIPGEIF-HQVPVTKHLLYRSGEYLARLDRALKNFTHQ 216
Cdd:PRK06148   72 LDHLAAVApdLPVPRLIPSLSGASLaSAQDPDGEPRLLRLLSWLPGTPLaEAAPRTEALLDNLGRALGRLDRALQGFMHP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  217 AYeSHKTLWMLQSVPELRQFLYVVKDQEQRLICDEVIDAFEAKVLSQLPSMEHQIIHGDFNEQNIVVEQvpnQTEYTIKG 296
Cdd:PRK06148  152 GA-LRDLDWDLRHAGRARDRLHFIDDPEDRALVERFLARFERNVAPRLAALPAQVIHNDANDYNILVDA---DDGERISG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  297 VIDFGDTSKSPLIFEIGIALTYMILQAND-LANGGIFLSGYTSLNPIENSELALLKYCVTARFVQSLVMGLYTHTLHPTN 375
Cdd:PRK06148  228 LIDFGDAVHAPRICEVAIAAAYAILDHPDpIGAAAALVAGYHAVYPLQAQELDLLFDLIRMRLAVSVTNSASRREQTPDN 307
                         330
                  ....*....|....*..
gi 665408573  376 EYLLVTQEKGWKLLQKL 392
Cdd:PRK06148  308 PYLAISEAPAWRLLERL 324
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
69-391 1.84e-44

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: 156.24  E-value: 1.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  69 EDVESLLRRlYGI-TISEVKEIVAYDDRNFFVKEDSNVKnplivthcphgYVLKILNSLDSKKEDfVDAQNQMLLYLGKH 147
Cdd:COG2334    1 DELAAALER-YGLgPLSSLKPLNSGENRNYRVETEDGRR-----------YVLKLYRPGRWSPEE-IPFELALLAHLAAA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 148 SVKCPRPVANATGKYysVERLNGNsnVVRLLEFIPGEIFHQVpvTKHLLYRSGEYLARLDRALKNFTHQAyeSHKTLWML 227
Cdd:COG2334   68 GLPVPAPVPTRDGET--LLELEGR--PAALFPFLPGRSPEEP--SPEQLEELGRLLARLHRALADFPRPN--ARDLAWWD 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 228 QSVPELRQFLyvVKDQEQRLICDEVIDAFEAKVLSQLPSMEHQIIHGDFNEQNIVV--EQVPnqteytikGVIDFGDTSK 305
Cdd:COG2334  140 ELLERLLGPL--LPDPEDRALLEELLDRLEARLAPLLGALPRGVIHGDLHPDNVLFdgDGVS--------GLIDFDDAGY 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 306 SPLIFEIGIALTYMILQANDLANGGIFLSGYTSLNPIENSELALLKYCVTARFVQSLVMGLY-THTLHPTN-EYLLVTQE 383
Cdd:COG2334  210 GPRLYDLAIALNGWADGPLDPARLAALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRrVRAKDPAFeRYLRRQIA 289

                 ....*...
gi 665408573 384 KGWKLLQK 391
Cdd:COG2334  290 LAWAALEA 297
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
68-350 1.97e-33

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: 126.99  E-value: 1.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  68 PEDVESLLRRlYGI-TISEVKEIVA-YDDRNFFVkedsnvknplivtHCPHG-YVLKILNSLDSKKEdfVDAQNQMLLYL 144
Cdd:cd05153    1 DEELAEFLAH-YDLgELLSFEGIAAgIENTNYFV-------------TTTDGrYVLTLFEKRRSAAE--LPFELELLDHL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 145 GKHSVKCPRPVANATGKYYSveRLNGNsnVVRLLEFIPGEifHQVPVTKHLLYRSGEYLARLDRALKNFTHQAYESHKTL 224
Cdd:cd05153   65 AQAGLPVPRPLADKDGELLG--ELNGK--PAALFPFLPGE--SLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 225 WMLQSVPELRQFLYVVKDQEQRLICDEvIDAFEAKVLSQLPsmeHQIIHGDFNEQNIVVEqvpnqtEYTIKGVIDFGDTS 304
Cdd:cd05153  139 WWKPLAERLKARLDLLAADDRALLEDE-LARLQALAPSDLP---RGVIHADLFRDNVLFD------GDRLSGIIDFYDAC 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 665408573 305 KSPLIFEIGIALTYMILQANDLANGG---IFLSGYTSLNPIENSELALL 350
Cdd:cd05153  209 YDPLLYDLAIALNDWCFDDDGKLDPErakALLAGYQSVRPLTEEEKAAL 257
PRK06149 PRK06149
aminotransferase;
51-390 6.23e-26

aminotransferase;


Pssm-ID: 235716 [Multi-domain]  Cd Length: 972  Bit Score: 110.47  E-value: 6.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  51 ADGDLLKPGSDVRPKVEPEDVESLLRRLYGITiSEVKEIVAYDDRNFFVKEDSNVknplivthcphgYVLKILNSLDSKK 130
Cdd:PRK06149   2 TDEALIDRSSLPAPDVSEAQAERILAEHYGLS-GTLTELGSQQDRNFRVDSDGGR------------FVLKICHAAYAAV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 131 EdfVDAQNQMLLYLGKHS--VKCPRPVANATGKYYSVERLNGNSNVVRLLEFIPGEIFHQVpvtKHLLYRS----GEYLA 204
Cdd:PRK06149  69 E--LEAQHAALRHLAEREpaLRVPVVIPALDGEELLTLDVRGQGLRVRLLDYLPGQPLTRL---GHLAPASvaglGALCA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 205 RLDRALKNFTHQAYesHKTL-WMLQ-SVPELRQFLYVVKDQEQR-LICDEVIDAfEAKVLSQLPSMEHQIIHGDFNEQNI 281
Cdd:PRK06149 144 RVARALADFDHPGL--DRTLqWDLRhAGPVVAHLLSHITDPAQRaRIAEATRDA-ARRLQPLAPALPLQAVHLDITDDNV 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 282 VVeQVPNQTEYTIKGVIDFGDTSKSPLIFEIGIALTYMILQandlANGGIF-----LSGYTSLNPIENSELALLKYCVTA 356
Cdd:PRK06149 221 VG-SRDADGRWQPDGVIDFGDLVRTWRVADLAVTCASLLHH----AGGDPFsilpaVRAYHAVRPLSEAELKALWPLVVA 295
                        330       340       350
                 ....*....|....*....|....*....|....
gi 665408573 357 RFVQSLVMGLYTHTLHPTNEYLLVTQEKGWKLLQ 390
Cdd:PRK06149 296 RAAVLVASSEQQLAVDPDNAYVRDNLAHEWEIFD 329
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
92-318 2.95e-20

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: 89.10  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573   92 YDDRNFFVKEDsnvKNPLIVTHCPHGYVLkilnsldskkeDFVDAQNQMLLYLGKHSV-KCPRPVAnatgkYYSVERLNG 170
Cdd:pfam01636   9 ASNRTYLVTTG---DGRYVLRLPPPGRAA-----------EELRRELALLRHLAAAGVpPVPRVLA-----GCTDAELLG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573  171 NsnVVRLLEFIPGEIFHQVP---VTKHLLYRSGEYLARLDRALKNFTHQAYESHKTLWMLQSVPELRQFLYVVKDQEQRL 247
Cdd:pfam01636  70 L--PFLLMEYLPGEVLARPLlpeERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLE 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408573  248 ICDE-VIDAFEAKVLSQLPSmehQIIHGDFNEQNIVVEQvPNQteytIKGVIDFGDTSKSPLIFEIGIALTY 318
Cdd:pfam01636 148 ELEErLLAALLALLPAELPP---VLVHGDLHPGNLLVDP-GGR----VSGVIDFEDAGLGDPAYDLAILLNS 211
PRK05231 PRK05231
homoserine kinase; Provisional
143-350 4.34e-09

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 57.50  E-value: 4.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 143 YLGKHSVKCPRPVANATGKYYSveRLNGNSNVvrLLEFIPGEifHQVPVTKHLLYRSGEYLARLDRALKNFT-HQAYE-S 220
Cdd:PRK05231  70 HLAARGVPVPAPVARRDGAALG--ELAGKPAA--IVTFLEGK--WPRAPTAAHCAEVGEMLARMHLAGRDFPlERPNLrG 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 221 HKtlWMLQSVPELRQFLyvvKDQEQRLICDEVidAFEAKVLSQ-----LPSmehQIIHGDFNEQNIVVEqvPNQteytIK 295
Cdd:PRK05231 144 LA--WWRELAPRLLPFL---ADEQAALLEAEL--AAQLAFLASaawpaLPR---GVIHADLFRDNVLFE--GDR----LS 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408573 296 GVIDFGDTSKSPLIFEIGIALtymilqaND---LANGGI-------FLSGYTSLNPIENSELALL 350
Cdd:PRK05231 208 GFIDFYFACNDKLLYDVAITL-------NDwcfEADGSLdatkaraLLAAYQSVRPLTAAERAAL 265
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
177-336 2.38e-06

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 48.96  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 177 LLEFIPGEIFHQV-----PVTKHLLYRS-GEYLARLDRAlkNFTHQAYESHKTLWMLQSVPELRQFLYVVKDQEQRLicD 250
Cdd:COG3173   97 VMEWVEGETLEDAlpdlsPAERRALARAlGEFLAALHAV--DPAAAGLADGRPEGLERQLARWRAQLRRALARTDDL--P 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408573 251 EVIDAFEAKVLSQLPSMEHQ-IIHGDFNEQNIVVeqvpNQTEYTIKGVIDFGDTSKSPLIFEIGIALTYMILQANDLANG 329
Cdd:COG3173  173 ALRERLAAWLAANLPEWGPPvLVHGDLRPGNLLV----DPDDGRLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPR 248

                 ....*..
gi 665408573 330 GIFLSGY 336
Cdd:COG3173  249 AAFLAAY 255
 
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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