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Conserved domains on  [gi|1852262194|ref|WP_173890697|]
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MULTISPECIES: dTMP kinase [Pseudomonas]

Protein Classification

dTMP kinase( domain architecture ID 11414784)

dTMP (thymidylate) kinase catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP) using ATP as a phosphoryl donor

CATH:  3.40.50.300
EC:  2.7.4.9
PubMed:  23394555
SCOP:  4004030

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
1-201 1.25e-99

Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis


:

Pssm-ID: 439895 [Multi-domain]  Cd Length: 206  Bit Score: 287.05  E-value: 1.25e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   1 MSGLFITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREPGGTPLAEKVRELLLApSDEPMAADTELLLVFAARAQHLAQ 80
Cdd:COG0125     1 MKGKFIVFEGIDGSGKSTQIKLLAEYLEARGYDVVLTREPGGTPLGEAIRELLLG-DNEDMSPRTELLLFAADRAQHVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  81 VIRPALARGAVVLCDRFTDATYAYQGGGRGLSVERIATLEQFVQGDLRPQLTLVFDLPVEVGLARAAARGR-LDRFEQEG 159
Cdd:COG0125    80 VIRPALAAGKIVICDRYVDSSLAYQGGGRGLDLEWIRQLNRFATGGLKPDLTILLDVPPEVALARARARGGeLDRFESED 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1852262194 160 QAFFQAVRQAYLQRARREPQRYSLLDAAQPLAAVQRAIDALL 201
Cdd:COG0125   160 LEFHERVREGYLELAAKEPERIVVIDASQSIEEVHAEIREAL 201
 
Name Accession Description Interval E-value
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
1-201 1.25e-99

Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 439895 [Multi-domain]  Cd Length: 206  Bit Score: 287.05  E-value: 1.25e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   1 MSGLFITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREPGGTPLAEKVRELLLApSDEPMAADTELLLVFAARAQHLAQ 80
Cdd:COG0125     1 MKGKFIVFEGIDGSGKSTQIKLLAEYLEARGYDVVLTREPGGTPLGEAIRELLLG-DNEDMSPRTELLLFAADRAQHVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  81 VIRPALARGAVVLCDRFTDATYAYQGGGRGLSVERIATLEQFVQGDLRPQLTLVFDLPVEVGLARAAARGR-LDRFEQEG 159
Cdd:COG0125    80 VIRPALAAGKIVICDRYVDSSLAYQGGGRGLDLEWIRQLNRFATGGLKPDLTILLDVPPEVALARARARGGeLDRFESED 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1852262194 160 QAFFQAVRQAYLQRARREPQRYSLLDAAQPLAAVQRAIDALL 201
Cdd:COG0125   160 LEFHERVREGYLELAAKEPERIVVIDASQSIEEVHAEIREAL 201
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
4-201 9.68e-91

Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).


Pssm-ID: 238835  Cd Length: 200  Bit Score: 264.52  E-value: 9.68e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   4 LFITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREPGGTPLAEKVRELLLAPSDEPMAADTELLLVFAARAQHLAQVIR 83
Cdd:cd01672     1 MFIVFEGIDGAGKTTLIELLAERLEARGYEVVLTREPGGTPIGEAIRELLLDPEDEKMDPRAELLLFAADRAQHVEEVIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  84 PALARGAVVLCDRFTDATYAYQGGGRGLSVERIATLEQFVQGDLRPQLTLVFDLPVEVGLARAAARGRLDRFEQEGQAFF 163
Cdd:cd01672    81 PALARGKIVLSDRFVDSSLAYQGAGRGLGEALIEALNDLATGGLKPDLTILLDIDPEVGLARIEARGRDDRDEQEGLEFH 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1852262194 164 QAVRQAYLQRARREPQRYSLLDAAQPLAAVQRAIDALL 201
Cdd:cd01672   161 ERVREGYLELAAQEPERIIVIDASQPLEEVLAEILKAI 198
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
1-197 3.94e-67

dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 161676  Cd Length: 195  Bit Score: 204.52  E-value: 3.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   1 MSGLFITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREPGGTPLAEKVRELLLAPSDEPMAADTELLLVFAARAQHLAQ 80
Cdd:TIGR00041   1 MRGMFIVIEGIDGAGKTTQANLLKKLLQENGYDVLFTREPGGTPIGEKIRELLLNENDEPLTDKAEALLFAADRHEHLED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  81 VIRPALARGAVVLCDRFTDATYAYQGGGRGLSVERIATLEQFVQGDlRPQLTLVFDLPVEVGLARAAARGRLDRFEQEGQ 160
Cdd:TIGR00041  81 KIKPALAEGKLVISDRYVFSSIAYQGGARGIDEDLVLELNEDALGD-MPDLTIYLDIDPEVALERLRKRGELDREEFEKL 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1852262194 161 AFFQAVRQAYLQRARREPQRYsLLDAAQPLAAVQRAI 197
Cdd:TIGR00041 160 DFFEKVRQRYLELADKEKSIH-VIDATNSVEEVEQDI 195
Thymidylate_kin pfam02223
Thymidylate kinase;
8-197 3.09e-50

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 160.93  E-value: 3.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   8 LEGPEGAGKSTNRDYLAARLREHGLDVVLTREPGGTPLAEKVRELLLapSDEPMAADTELLLVFAARAQHLAQVIRPALA 87
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIKVVFTREPGGTPIGEKIRELLL--RNEELSPLTEALLFAADRIQHLEQKIKPALK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  88 RGAVVLCDRFTDATYAYQGGGRGLsVERIATLEQFVQGdlRPQLTLVFDLPVEVGLARAAARGRLDRFEQEGQAFFQAVR 167
Cdd:pfam02223  79 QGKTVIVDRYLFSGIAYQGAKGGD-LDLVLSLNPDVPG--KPDLTFLLDVDPEVALKRLRRRGELEKTEFEQLDFLRKVR 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 1852262194 168 QAYLqRARREPQRYSLLDAAQPLAAVQRAI 197
Cdd:pfam02223 156 ERYL-ELAKFDERIKIIDASLSIEEVHEEI 184
PLN02924 PLN02924
thymidylate kinase
3-210 1.83e-12

thymidylate kinase


Pssm-ID: 178512  Cd Length: 220  Bit Score: 63.59  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   3 GLFITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREPG-GTPLAEKVRELLLAPSDepmAADTELLLVFAARAQHLAQV 81
Cdd:PLN02924   16 GALIVLEGLDRSGKSTQCAKLVSFLKGLGVAAELWRFPDrTTSVGQMISAYLSNKSQ---LDDRAIHLLFSANRWEKRSL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  82 IRPALARGAVVLCDRftdatYAYQG----GGRGLSVERIATLEqfvQGDLRPQLTLVFDLPVEvglaRAAARGRL--DRF 155
Cdd:PLN02924   93 MERKLKSGTTLVVDR-----YSYSGvafsAAKGLDLEWCKAPE---VGLPAPDLVLYLDISPE----EAAERGGYggERY 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1852262194 156 EQegQAFFQAVRQAYlqRARREPqRYSLLDAAQPLAAVQRAIDALLPAIVERCRG 210
Cdd:PLN02924  161 EK--LEFQKKVAKRF--QTLRDS-SWKIIDASQSIEEVEKKIREVVLDTVQRCLA 210
 
Name Accession Description Interval E-value
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
1-201 1.25e-99

Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 439895 [Multi-domain]  Cd Length: 206  Bit Score: 287.05  E-value: 1.25e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   1 MSGLFITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREPGGTPLAEKVRELLLApSDEPMAADTELLLVFAARAQHLAQ 80
Cdd:COG0125     1 MKGKFIVFEGIDGSGKSTQIKLLAEYLEARGYDVVLTREPGGTPLGEAIRELLLG-DNEDMSPRTELLLFAADRAQHVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  81 VIRPALARGAVVLCDRFTDATYAYQGGGRGLSVERIATLEQFVQGDLRPQLTLVFDLPVEVGLARAAARGR-LDRFEQEG 159
Cdd:COG0125    80 VIRPALAAGKIVICDRYVDSSLAYQGGGRGLDLEWIRQLNRFATGGLKPDLTILLDVPPEVALARARARGGeLDRFESED 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1852262194 160 QAFFQAVRQAYLQRARREPQRYSLLDAAQPLAAVQRAIDALL 201
Cdd:COG0125   160 LEFHERVREGYLELAAKEPERIVVIDASQSIEEVHAEIREAL 201
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
4-201 9.68e-91

Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).


Pssm-ID: 238835  Cd Length: 200  Bit Score: 264.52  E-value: 9.68e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   4 LFITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREPGGTPLAEKVRELLLAPSDEPMAADTELLLVFAARAQHLAQVIR 83
Cdd:cd01672     1 MFIVFEGIDGAGKTTLIELLAERLEARGYEVVLTREPGGTPIGEAIRELLLDPEDEKMDPRAELLLFAADRAQHVEEVIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  84 PALARGAVVLCDRFTDATYAYQGGGRGLSVERIATLEQFVQGDLRPQLTLVFDLPVEVGLARAAARGRLDRFEQEGQAFF 163
Cdd:cd01672    81 PALARGKIVLSDRFVDSSLAYQGAGRGLGEALIEALNDLATGGLKPDLTILLDIDPEVGLARIEARGRDDRDEQEGLEFH 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1852262194 164 QAVRQAYLQRARREPQRYSLLDAAQPLAAVQRAIDALL 201
Cdd:cd01672   161 ERVREGYLELAAQEPERIIVIDASQPLEEVLAEILKAI 198
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
1-197 3.94e-67

dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 161676  Cd Length: 195  Bit Score: 204.52  E-value: 3.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   1 MSGLFITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREPGGTPLAEKVRELLLAPSDEPMAADTELLLVFAARAQHLAQ 80
Cdd:TIGR00041   1 MRGMFIVIEGIDGAGKTTQANLLKKLLQENGYDVLFTREPGGTPIGEKIRELLLNENDEPLTDKAEALLFAADRHEHLED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  81 VIRPALARGAVVLCDRFTDATYAYQGGGRGLSVERIATLEQFVQGDlRPQLTLVFDLPVEVGLARAAARGRLDRFEQEGQ 160
Cdd:TIGR00041  81 KIKPALAEGKLVISDRYVFSSIAYQGGARGIDEDLVLELNEDALGD-MPDLTIYLDIDPEVALERLRKRGELDREEFEKL 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1852262194 161 AFFQAVRQAYLQRARREPQRYsLLDAAQPLAAVQRAI 197
Cdd:TIGR00041 160 DFFEKVRQRYLELADKEKSIH-VIDATNSVEEVEQDI 195
Thymidylate_kin pfam02223
Thymidylate kinase;
8-197 3.09e-50

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 160.93  E-value: 3.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   8 LEGPEGAGKSTNRDYLAARLREHGLDVVLTREPGGTPLAEKVRELLLapSDEPMAADTELLLVFAARAQHLAQVIRPALA 87
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIKVVFTREPGGTPIGEKIRELLL--RNEELSPLTEALLFAADRIQHLEQKIKPALK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  88 RGAVVLCDRFTDATYAYQGGGRGLsVERIATLEQFVQGdlRPQLTLVFDLPVEVGLARAAARGRLDRFEQEGQAFFQAVR 167
Cdd:pfam02223  79 QGKTVIVDRYLFSGIAYQGAKGGD-LDLVLSLNPDVPG--KPDLTFLLDVDPEVALKRLRRRGELEKTEFEQLDFLRKVR 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 1852262194 168 QAYLqRARREPQRYSLLDAAQPLAAVQRAI 197
Cdd:pfam02223 156 ERYL-ELAKFDERIKIIDASLSIEEVHEEI 184
PLN02924 PLN02924
thymidylate kinase
3-210 1.83e-12

thymidylate kinase


Pssm-ID: 178512  Cd Length: 220  Bit Score: 63.59  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   3 GLFITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREPG-GTPLAEKVRELLLAPSDepmAADTELLLVFAARAQHLAQV 81
Cdd:PLN02924   16 GALIVLEGLDRSGKSTQCAKLVSFLKGLGVAAELWRFPDrTTSVGQMISAYLSNKSQ---LDDRAIHLLFSANRWEKRSL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  82 IRPALARGAVVLCDRftdatYAYQG----GGRGLSVERIATLEqfvQGDLRPQLTLVFDLPVEvglaRAAARGRL--DRF 155
Cdd:PLN02924   93 MERKLKSGTTLVVDR-----YSYSGvafsAAKGLDLEWCKAPE---VGLPAPDLVLYLDISPE----EAAERGGYggERY 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1852262194 156 EQegQAFFQAVRQAYlqRARREPqRYSLLDAAQPLAAVQRAIDALLPAIVERCRG 210
Cdd:PLN02924  161 EK--LEFQKKVAKRF--QTLRDS-SWKIIDASQSIEEVEKKIREVVLDTVQRCLA 210
PRK07933 PRK07933
dTMP kinase;
6-159 4.56e-09

dTMP kinase;


Pssm-ID: 236133  Cd Length: 213  Bit Score: 54.21  E-value: 4.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   6 ITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREP--GGTPLAEKVRELL------LAPSDEPMAadtellLVFAARAQH 77
Cdd:PRK07933    3 IAIEGVDGAGKRTLTEALRAALEARGRSVATLAFPryGRSVHADLAAEALhgrhgdLADSVYAMA------TLFALDRAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  78 LAQVIRPALARGAVVLCDRFTDATYAYQ-----GGGRGLSVERIATLEQFVQGDLRPQLTLVFDLPVEVGLARAAARGR- 151
Cdd:PRK07933   77 ARDELAGLLAAHDVVILDRYVASNAAYSaarlhQDADGEAVAWVAELEFGRLGLPVPDLQVLLDVPVELAAERARRRAAq 156
                         170
                  ....*....|...
gi 1852262194 152 -----LDRFEQEG 159
Cdd:PRK07933  157 dadraRDAYERDD 169
AAA_22 pfam13401
AAA domain;
1-95 1.27e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.71  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   1 MSGLFITLEGPEGAGKSTNRDYLAARLREHGLDVVLTREPGGTPLAEKVRELLLAPSDEPMAADTELLLVfaaraQHLAQ 80
Cdd:pfam13401   3 FGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALGLPLSGRLSKEELL-----AALQQ 77
                          90
                  ....*....|....*
gi 1852262194  81 VIRpALARGAVVLCD 95
Cdd:pfam13401  78 LLL-ALAVAVVLIID 91
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
5-151 1.80e-03

Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA.


Pssm-ID: 238836  Cd Length: 193  Bit Score: 37.98  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   5 FITLEGPEGAGKSTnrdyLAARLREH-GLDVVLtrEPGGTplaEKVRELLLAPSDEPM---AADTElLLVFAARAQHLAQ 80
Cdd:cd01673     1 VIVVEGNIGAGKST----LAKELAEHlGYEVVP--EPVEP---DVEGNPFLEKFYEDPkrwAFPFQ-LYFLLSRLKQYKD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  81 VIRpALARGAVVLCDR-------FTDATYAYqgggRGLSVERIATLEQF----VQGDLRPQLTLVFDLPVEVGLARAAAR 149
Cdd:cd01673    71 ALE-HLSTGQGVILERsifsdrvFAEANLKE----GGIMKTEYDLYNELfdnlIPELLPPDLVIYLDASPETCLKRIKKR 145

                  ..
gi 1852262194 150 GR 151
Cdd:cd01673   146 GR 147
AAA_28 pfam13521
AAA domain;
5-170 4.16e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 36.47  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194   5 FITLEGPEGAGKSTnrdyLAARLREHgLDVVLTREPGGTPLAEKVRelllapSDEPMAADTELLLVFAARAQHLAQVIRP 84
Cdd:pfam13521   1 RIVITGGPSTGKTT----LAEALAAR-FGYPVVPEAAREILEELGA------DGGDALPWVEDLLAFARGVLEAQLEDEA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852262194  85 ALARGAVVLCDRFTDATYAYQ---GGGRGLSVERIATLeqfvqgdLRPQLTLVFDLPVEVglarAAARGRLDRFEqEGQA 161
Cdd:pfam13521  70 AAAANDLLFFDRGPLDTLAYSrayGGPCPPELEAAARA-------SRYDLVFLLPPDPEI----VQDGERREDPE-ERER 137

                  ....*....
gi 1852262194 162 FFQAVRQAY 170
Cdd:pfam13521 138 FHERLREAL 146
 
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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