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Conserved domains on  [gi|522073032|ref|WP_020584241|]
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serine/threonine protein kinase [Endozoicomonas elysicola]

Protein Classification

stress response kinase A( domain architecture ID 10013878)

stress response kinase A is involved in mediating the Cpx stress response pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
3-326 0e+00

serine/threonine protein kinase;


:

Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 549.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032   3 TPTQHPYDQLTPDRVLDAVESVGFISDARIMALNSYENRVYQVGIEESEPLIAKFYRPERWSKEQILEEHQFTLDLKAME 82
Cdd:PRK11768   2 NDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  83 LPVVAPsTDEHGNTLHEFEGFLFALFPRQGGHAPELDNLDNLLILGRTLGRMHKLGSAKPFQHRPEINLQRYGIDNVEFL 162
Cdd:PRK11768  82 IPVVAP-LAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 163 LENDFIPSSLLEAYQTLTRDLLHRLDRINHQHSWESIRVHGDCHSGNILWRsDAPHFVDFDDTCMAPAIQDIWMLLSGDR 242
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWARGDVRLLRLHGDCHPGNILWR-DGPHFVDLDDARMGPAVQDLWMLLSGDR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 243 REQTLQMAEILEGYGEFMDFSPSELNLVEYFRTLRLLNYSGWLAKRWDDPAFPKAFTWFNTERYWAEHILELREQLAALD 322
Cdd:PRK11768 240 AEQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQ 319

                 ....
gi 522073032 323 EPPL 326
Cdd:PRK11768 320 EPPL 323
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
3-326 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 549.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032   3 TPTQHPYDQLTPDRVLDAVESVGFISDARIMALNSYENRVYQVGIEESEPLIAKFYRPERWSKEQILEEHQFTLDLKAME 82
Cdd:PRK11768   2 NDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  83 LPVVAPsTDEHGNTLHEFEGFLFALFPRQGGHAPELDNLDNLLILGRTLGRMHKLGSAKPFQHRPEINLQRYGIDNVEFL 162
Cdd:PRK11768  82 IPVVAP-LAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 163 LENDFIPSSLLEAYQTLTRDLLHRLDRINHQHSWESIRVHGDCHSGNILWRsDAPHFVDFDDTCMAPAIQDIWMLLSGDR 242
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWARGDVRLLRLHGDCHPGNILWR-DGPHFVDLDDARMGPAVQDLWMLLSGDR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 243 REQTLQMAEILEGYGEFMDFSPSELNLVEYFRTLRLLNYSGWLAKRWDDPAFPKAFTWFNTERYWAEHILELREQLAALD 322
Cdd:PRK11768 240 AEQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQ 319

                 ....
gi 522073032 323 EPPL 326
Cdd:PRK11768 320 EPPL 323
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
15-320 8.29e-82

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: 250.23  E-value: 8.29e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  15 DRVLDAVESVGFISDARIMALNSYENRVYQVGIEESEPLIAKFYRPERWSKEQILEEHQFTLDLKAMELPVVAPSTDEHG 94
Cdd:COG2334    1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPTRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  95 NTLHEFEGFLFALFPRQGGHAPELDNLDNLLILGRTLGRMHKLGsaKPFQHRPEINLQRYGiDNVEFLLEnDFIPSsllE 174
Cdd:COG2334   81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRAL--ADFPRPNARDLAWWD-ELLERLLG-PLLPD---P 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 175 AYQTLTRDLLHRLDRINHQ--HSWESIRVHGDCHSGNILWRSD-APHFVDFDDTCMAPAIQDIWMLLSG--DRREQTLQM 249
Cdd:COG2334  154 EDRALLEELLDRLEARLAPllGALPRGVIHGDLHPDNVLFDGDgVSGLIDFDDAGYGPRLYDLAIALNGwaDGPLDPARL 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522073032 250 AEILEGYGEFMDFSPSELNLVEYFRTLRLLNYSGWLAKRW--DDPAFPkaftwfnteRYWAEHILELREQLAA 320
Cdd:COG2334  234 AALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVraKDPAFE---------RYLRRQIALAWAALEA 297
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
38-259 2.78e-23

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: 96.03  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032   38 YENRVYQVGIEESEpLIAKFYRPeRWSKEQILEEHQFtLDLKAMELPVVAPSTdEHGNTLHEFEGFLFALFPRQGGHAPE 117
Cdd:pfam01636   9 ASNRTYLVTTGDGR-YVLRLPPP-GRAAEELRRELAL-LRHLAAAGVPPVPRV-LAGCTDAELLGLPFLLMEYLPGEVLA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  118 LDNLDNLLIL-----GRTLGRMHKLGSAK-PFQHRPeinlqRYGIDNVEFLLE--NDFIPSSLLEAYQTLTRDLLHRLDR 189
Cdd:pfam01636  85 RPLLPEERGAllealGRALARLHAVDPAAlPLAGRL-----ARLLELLRQLEAalARLLAAELLDRLEELEERLLAALLA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522073032  190 iNHQHSWESIRVHGDCHSGNILWRSDAPH--FVDFDDTCMAPAIQDIWMLL-SGDRREQTLQMAEILEGYGEF 259
Cdd:pfam01636 160 -LLPAELPPVLVHGDLHPGNLLVDPGGRVsgVIDFEDAGLGDPAYDLAILLnSWGRELGAELLAAYLAAYGAF 231
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
38-293 5.92e-14

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: 71.14  E-value: 5.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  38 YENRVYQVGIEESEpLIAKFYRPeRWSKEQILEEHQFTLDLKAMELPVVAPSTDEHGNTLHEFEGFLFALFPRQGGHAPE 117
Cdd:cd05153   26 IENTNYFVTTTDGR-YVLTLFEK-RRSAAELPFELELLDHLAQAGLPVPRPLADKDGELLGELNGKPAALFPFLPGESLT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 118 LDNLDNLLILGRTLGRMHKLGSAKPFQHRPeinlqRYGIDNVEFLLEndfipsSLLEAYQTLTRDLLHRL-DRINHQHSW 196
Cdd:cd05153  104 TPTPEQCRAIGAALARLHLALAGFPPPRPN-----PRGLAWWKPLAE------RLKARLDLLAADDRALLeDELARLQAL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 197 ESIR-----VHGDCHSGNILWRSDA-PHFVDFDDTCMAPAIQDI------WMLLSGDRREQTLqMAEILEGYGEFMDFSP 264
Cdd:cd05153  173 APSDlprgvIHADLFRDNVLFDGDRlSGIIDFYDACYDPLLYDLaialndWCFDDDGKLDPER-AKALLAGYQSVRPLTE 251
                        250       260
                 ....*....|....*....|....*....
gi 522073032 265 SELNLVEYFRTLRLLNYSGWLAKRWDDPA 293
Cdd:cd05153  252 EEKAALPLLLRAAALRFWLSRLYDFHLPR 280
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
3-326 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 549.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032   3 TPTQHPYDQLTPDRVLDAVESVGFISDARIMALNSYENRVYQVGIEESEPLIAKFYRPERWSKEQILEEHQFTLDLKAME 82
Cdd:PRK11768   2 NDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  83 LPVVAPsTDEHGNTLHEFEGFLFALFPRQGGHAPELDNLDNLLILGRTLGRMHKLGSAKPFQHRPEINLQRYGIDNVEFL 162
Cdd:PRK11768  82 IPVVAP-LAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 163 LENDFIPSSLLEAYQTLTRDLLHRLDRINHQHSWESIRVHGDCHSGNILWRsDAPHFVDFDDTCMAPAIQDIWMLLSGDR 242
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWARGDVRLLRLHGDCHPGNILWR-DGPHFVDLDDARMGPAVQDLWMLLSGDR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 243 REQTLQMAEILEGYGEFMDFSPSELNLVEYFRTLRLLNYSGWLAKRWDDPAFPKAFTWFNTERYWAEHILELREQLAALD 322
Cdd:PRK11768 240 AEQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQ 319

                 ....
gi 522073032 323 EPPL 326
Cdd:PRK11768 320 EPPL 323
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
15-320 8.29e-82

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: 250.23  E-value: 8.29e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  15 DRVLDAVESVGFISDARIMALNSYENRVYQVGIEESEPLIAKFYRPERWSKEQILEEHQFTLDLKAMELPVVAPSTDEHG 94
Cdd:COG2334    1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPTRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  95 NTLHEFEGFLFALFPRQGGHAPELDNLDNLLILGRTLGRMHKLGsaKPFQHRPEINLQRYGiDNVEFLLEnDFIPSsllE 174
Cdd:COG2334   81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRAL--ADFPRPNARDLAWWD-ELLERLLG-PLLPD---P 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 175 AYQTLTRDLLHRLDRINHQ--HSWESIRVHGDCHSGNILWRSD-APHFVDFDDTCMAPAIQDIWMLLSG--DRREQTLQM 249
Cdd:COG2334  154 EDRALLEELLDRLEARLAPllGALPRGVIHGDLHPDNVLFDGDgVSGLIDFDDAGYGPRLYDLAIALNGwaDGPLDPARL 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522073032 250 AEILEGYGEFMDFSPSELNLVEYFRTLRLLNYSGWLAKRW--DDPAFPkaftwfnteRYWAEHILELREQLAA 320
Cdd:COG2334  234 AALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVraKDPAFE---------RYLRRQIALAWAALEA 297
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
38-259 2.78e-23

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: 96.03  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032   38 YENRVYQVGIEESEpLIAKFYRPeRWSKEQILEEHQFtLDLKAMELPVVAPSTdEHGNTLHEFEGFLFALFPRQGGHAPE 117
Cdd:pfam01636   9 ASNRTYLVTTGDGR-YVLRLPPP-GRAAEELRRELAL-LRHLAAAGVPPVPRV-LAGCTDAELLGLPFLLMEYLPGEVLA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  118 LDNLDNLLIL-----GRTLGRMHKLGSAK-PFQHRPeinlqRYGIDNVEFLLE--NDFIPSSLLEAYQTLTRDLLHRLDR 189
Cdd:pfam01636  85 RPLLPEERGAllealGRALARLHAVDPAAlPLAGRL-----ARLLELLRQLEAalARLLAAELLDRLEELEERLLAALLA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522073032  190 iNHQHSWESIRVHGDCHSGNILWRSDAPH--FVDFDDTCMAPAIQDIWMLL-SGDRREQTLQMAEILEGYGEF 259
Cdd:pfam01636 160 -LLPAELPPVLVHGDLHPGNLLVDPGGRVsgVIDFEDAGLGDPAYDLAILLnSWGRELGAELLAAYLAAYGAF 231
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
38-293 5.92e-14

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: 71.14  E-value: 5.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  38 YENRVYQVGIEESEpLIAKFYRPeRWSKEQILEEHQFTLDLKAMELPVVAPSTDEHGNTLHEFEGFLFALFPRQGGHAPE 117
Cdd:cd05153   26 IENTNYFVTTTDGR-YVLTLFEK-RRSAAELPFELELLDHLAQAGLPVPRPLADKDGELLGELNGKPAALFPFLPGESLT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 118 LDNLDNLLILGRTLGRMHKLGSAKPFQHRPeinlqRYGIDNVEFLLEndfipsSLLEAYQTLTRDLLHRL-DRINHQHSW 196
Cdd:cd05153  104 TPTPEQCRAIGAALARLHLALAGFPPPRPN-----PRGLAWWKPLAE------RLKARLDLLAADDRALLeDELARLQAL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 197 ESIR-----VHGDCHSGNILWRSDA-PHFVDFDDTCMAPAIQDI------WMLLSGDRREQTLqMAEILEGYGEFMDFSP 264
Cdd:cd05153  173 APSDlprgvIHADLFRDNVLFDGDRlSGIIDFYDACYDPLLYDLaialndWCFDDDGKLDPER-AKALLAGYQSVRPLTE 251
                        250       260
                 ....*....|....*....|....*....
gi 522073032 265 SELNLVEYFRTLRLLNYSGWLAKRWDDPA 293
Cdd:cd05153  252 EEKAALPLLLRAAALRFWLSRLYDFHLPR 280
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
166-290 8.91e-07

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 47.85  E-value: 8.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 166 DFIPSSLLEAYQTL----TRDLLHRLDRINHQHSWESIR---VHGDCHSGNILWRSD-APHFVDFDDTCMAPAIQDIWML 237
Cdd:COG0510   10 RFDLFARLERYLALgprdLPELLRRLEELERALAARPLPlvlCHGDLHPGNFLVTDDgRLYLIDWEYAGLGDPAFDLAAL 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 522073032 238 LSGDRREQTlQMAEILEGYGeFMDFSPSELNLVEYFRTLRLLNYSGWLAKRWD 290
Cdd:COG0510   90 LVEYGLSPE-QAEELLEAYG-FGRPTEELLRRLRAYRALADLLWALWALVRAA 140
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
10-258 6.11e-04

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 40.87  E-value: 6.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  10 DQLTPDRVLDAVESV--GFISDARIMALNS-YENRVYQVGIEEsePLIAKFYRPERWSKEQILEEHQFtldLKAME--LP 84
Cdd:COG3173    1 EELDEAALRALLAAQlpGLAGLPEVEPLSGgWSNLTYRLDTGD--RLVLRRPPRGLASAHDVRREARV---LRALAprLG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032  85 VVAPSTDEHGNTlHEFEGFLFALFPRQGGHAPELDNLDNLLIL--------GRTLGRMHK-------LGSAKPFQHRPEI 149
Cdd:COG3173   76 VPVPRPLALGED-GEVIGAPFYVMEWVEGETLEDALPDLSPAErralaralGEFLAALHAvdpaaagLADGRPEGLERQL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522073032 150 NLQRygiDNVEFLLENDfipssllEAYQTLTRDLLHRLDRinHQHSWESIR-VHGDCHSGNILWRSDAPHFV---DFDDT 225
Cdd:COG3173  155 ARWR---AQLRRALART-------DDLPALRERLAAWLAA--NLPEWGPPVlVHGDLRPGNLLVDPDDGRLTaviDWELA 222
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 522073032 226 CMAPAIQDIWMLLSGDRREQTL--QMAEILEGYGE 258
Cdd:COG3173  223 TLGDPAADLAYLLLYWRLPDDLlgPRAAFLAAYEE 257
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
201-258 3.95e-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: 37.25  E-value: 3.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522073032 201 VHGDCHSGNILWRSDAPHFVDFDDTCMAPAIQ----DIWMLL-----SGDRREQTLqMAEILEGYGE 258
Cdd:COG3642   73 VHGDLTTSNILVDDGGVYLIDFGLARYSDPLEdkavDLAVLKrslesTHPDPAEEL-WEAFLEGYRE 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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