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Conserved domains on  [gi|446599879|ref|WP_000677225|]
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MULTISPECIES: dTMP kinase [Bacillus]

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
Gene Ontology:  GO:0004798|GO:0005524|GO:0016310|GO:0006233
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 ...
 1-207 1.54e-93

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: 271.65  E-value: 1.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   1 MKGLFVTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPGGIAISEDIRTILHKQEYTMmEARTEALLYAAARRQHLVE 80
Cdd:COG0125    1 MKGKFIVFEGIDGSGKSTQIKLLAEYLEARGYDVVLTREPGGTPLGEAIRELLLGDNEDM-SPRTELLLFAADRAQHVEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879  81 KVMPALNEDYLVLCDRFIDSSLAYQGYARGLGMDKVFEINRFATEDCMPSLTIYLDIEPEIGLARIEKdAGREVNRLDME 160
Cdd:COG0125   80 VIRPALAAGKIVICDRYVDSSLAYQGGGRGLDLEWIRQLNRFATGGLKPDLTILLDVPPEVALARARA-RGGELDRFESE 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446599879 161 DISFHKRVREGYLQVVERFSDRIVLVNADQPMEKLIEEVVQIIEDKL 207
Cdd:COG0125  159 DLEFHERVREGYLELAAKEPERIVVIDASQSIEEVHAEIREALAELL 205
 
Name Accession Description Interval E-value
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
 1-207 1.54e-93

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: 271.65  E-value: 1.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   1 MKGLFVTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPGGIAISEDIRTILHKQEYTMmEARTEALLYAAARRQHLVE 80
Cdd:COG0125    1 MKGKFIVFEGIDGSGKSTQIKLLAEYLEARGYDVVLTREPGGTPLGEAIRELLLGDNEDM-SPRTELLLFAADRAQHVEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879  81 KVMPALNEDYLVLCDRFIDSSLAYQGYARGLGMDKVFEINRFATEDCMPSLTIYLDIEPEIGLARIEKdAGREVNRLDME 160
Cdd:COG0125   80 VIRPALAAGKIVICDRYVDSSLAYQGGGRGLDLEWIRQLNRFATGGLKPDLTILLDVPPEVALARARA-RGGELDRFESE 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446599879 161 DISFHKRVREGYLQVVERFSDRIVLVNADQPMEKLIEEVVQIIEDKL 207
Cdd:COG0125  159 DLEFHERVREGYLELAAKEPERIVVIDASQSIEEVHAEIREALAELL 205
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
 4-205 1.46e-87

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: 256.43  E-value: 1.46e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   4 LFVTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPGGIAISEDIRTILHKQEYTMMEARTEALLYAAARRQHLVEKVM 83
Cdd:cd01672    1 MFIVFEGIDGAGKTTLIELLAERLEARGYEVVLTREPGGTPIGEAIRELLLDPEDEKMDPRAELLLFAADRAQHVEEVIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879  84 PALNEDYLVLCDRFIDSSLAYQGYARGLGMDKVFEINRFATEDCMPSLTIYLDIEPEIGLARIEKDAGREvnRLDMEDIS 163
Cdd:cd01672   81 PALARGKIVLSDRFVDSSLAYQGAGRGLGEALIEALNDLATGGLKPDLTILLDIDPEVGLARIEARGRDD--RDEQEGLE 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446599879 164 FHKRVREGYLQVVERFSDRIVLVNADQPMEKLIEEVVQIIED 205
Cdd:cd01672  159 FHERVREGYLELAAQEPERIIVIDASQPLEEVLAEILKAILE 200
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
 1-199 4.97e-65

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: 199.13  E-value: 4.97e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879    1 MKGLFVTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPGGIAISEDIRTILHKQEYTMMEARTEALLYAAARRQHLVE 80
Cdd:TIGR00041   1 MRGMFIVIEGIDGAGKTTQANLLKKLLQENGYDVLFTREPGGTPIGEKIRELLLNENDEPLTDKAEALLFAADRHEHLED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   81 KVMPALNEDYLVLCDRFIDSSLAYQGYARGLGMDKVFEINRFATEDcMPSLTIYLDIEPEIGLARIEKDagREVNRLDME 160
Cdd:TIGR00041  81 KIKPALAEGKLVISDRYVFSSIAYQGGARGIDEDLVLELNEDALGD-MPDLTIYLDIDPEVALERLRKR--GELDREEFE 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 446599879  161 DISFHKRVREGYLQVVERfSDRIVLVNADQPMEKLIEEV 199
Cdd:TIGR00041 158 KLDFFEKVRQRYLELADK-EKSIHVIDATNSVEEVEQDI 195
Thymidylate_kin pfam02223
Thymidylate kinase;
8-203 5.44e-46

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 150.14  E-value: 5.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879    8 IEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPGGIAISEDIRTILHKQEytMMEARTEALLYAAARRQHLVEKVMPALN 87
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIKVVFTREPGGTPIGEKIRELLLRNE--ELSPLTEALLFAADRIQHLEQKIKPALK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   88 EDYLVLCDRFIDSSLAYQGYARGlGMDKVFEINRFATEdcMPSLTIYLDIEPEIGLARIEKdaGREVNRLDMEDISFHKR 167
Cdd:pfam02223  79 QGKTVIVDRYLFSGIAYQGAKGG-DLDLVLSLNPDVPG--KPDLTFLLDVDPEVALKRLRR--RGELEKTEFEQLDFLRK 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446599879  168 VREGYLQVVeRFSDRIVLVNADQPmeklIEEVVQII 203
Cdd:pfam02223 154 VRERYLELA-KFDERIKIIDASLS----IEEVHEEI 184
PLN02924 PLN02924
thymidylate kinase
 2-205 1.34e-11

thymidylate kinase


Pssm-ID: 178512  Cd Length: 220  Bit Score: 61.28  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   2 KGLFVTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPG-GIAISEDIRTILhkQEYTMMEARTEALLYAAAR---RQH 77
Cdd:PLN02924  15 RGALIVLEGLDRSGKSTQCAKLVSFLKGLGVAAELWRFPDrTTSVGQMISAYL--SNKSQLDDRAIHLLFSANRwekRSL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879  78 LVEKVMPALNedylVLCDRFIDSSLAYQGyARGLGMD--KVFEINRFAtedcmPSLTIYLDIEPEIGLARiekdAGREVN 155
Cdd:PLN02924  93 MERKLKSGTT----LVVDRYSYSGVAFSA-AKGLDLEwcKAPEVGLPA-----PDLVLYLDISPEEAAER----GGYGGE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446599879 156 RldMEDISFHKRVREGYLQVVErfsDRIVLVNADQPMEKLIEEVVQIIED 205
Cdd:PLN02924 159 R--YEKLEFQKKVAKRFQTLRD---SSWKIIDASQSIEEVEKKIREVVLD 203
 
Name Accession Description Interval E-value
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
 1-207 1.54e-93

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: 271.65  E-value: 1.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   1 MKGLFVTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPGGIAISEDIRTILHKQEYTMmEARTEALLYAAARRQHLVE 80
Cdd:COG0125    1 MKGKFIVFEGIDGSGKSTQIKLLAEYLEARGYDVVLTREPGGTPLGEAIRELLLGDNEDM-SPRTELLLFAADRAQHVEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879  81 KVMPALNEDYLVLCDRFIDSSLAYQGYARGLGMDKVFEINRFATEDCMPSLTIYLDIEPEIGLARIEKdAGREVNRLDME 160
Cdd:COG0125   80 VIRPALAAGKIVICDRYVDSSLAYQGGGRGLDLEWIRQLNRFATGGLKPDLTILLDVPPEVALARARA-RGGELDRFESE 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446599879 161 DISFHKRVREGYLQVVERFSDRIVLVNADQPMEKLIEEVVQIIEDKL 207
Cdd:COG0125  159 DLEFHERVREGYLELAAKEPERIVVIDASQSIEEVHAEIREALAELL 205
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
 4-205 1.46e-87

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: 256.43  E-value: 1.46e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   4 LFVTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPGGIAISEDIRTILHKQEYTMMEARTEALLYAAARRQHLVEKVM 83
Cdd:cd01672    1 MFIVFEGIDGAGKTTLIELLAERLEARGYEVVLTREPGGTPIGEAIRELLLDPEDEKMDPRAELLLFAADRAQHVEEVIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879  84 PALNEDYLVLCDRFIDSSLAYQGYARGLGMDKVFEINRFATEDCMPSLTIYLDIEPEIGLARIEKDAGREvnRLDMEDIS 163
Cdd:cd01672   81 PALARGKIVLSDRFVDSSLAYQGAGRGLGEALIEALNDLATGGLKPDLTILLDIDPEVGLARIEARGRDD--RDEQEGLE 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446599879 164 FHKRVREGYLQVVERFSDRIVLVNADQPMEKLIEEVVQIIED 205
Cdd:cd01672  159 FHERVREGYLELAAQEPERIIVIDASQPLEEVLAEILKAILE 200
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
 1-199 4.97e-65

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: 199.13  E-value: 4.97e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879    1 MKGLFVTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPGGIAISEDIRTILHKQEYTMMEARTEALLYAAARRQHLVE 80
Cdd:TIGR00041   1 MRGMFIVIEGIDGAGKTTQANLLKKLLQENGYDVLFTREPGGTPIGEKIRELLLNENDEPLTDKAEALLFAADRHEHLED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   81 KVMPALNEDYLVLCDRFIDSSLAYQGYARGLGMDKVFEINRFATEDcMPSLTIYLDIEPEIGLARIEKDagREVNRLDME 160
Cdd:TIGR00041  81 KIKPALAEGKLVISDRYVFSSIAYQGGARGIDEDLVLELNEDALGD-MPDLTIYLDIDPEVALERLRKR--GELDREEFE 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 446599879  161 DISFHKRVREGYLQVVERfSDRIVLVNADQPMEKLIEEV 199
Cdd:TIGR00041 158 KLDFFEKVRQRYLELADK-EKSIHVIDATNSVEEVEQDI 195
Thymidylate_kin pfam02223
Thymidylate kinase;
8-203 5.44e-46

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 150.14  E-value: 5.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879    8 IEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPGGIAISEDIRTILHKQEytMMEARTEALLYAAARRQHLVEKVMPALN 87
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIKVVFTREPGGTPIGEKIRELLLRNE--ELSPLTEALLFAADRIQHLEQKIKPALK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   88 EDYLVLCDRFIDSSLAYQGYARGlGMDKVFEINRFATEdcMPSLTIYLDIEPEIGLARIEKdaGREVNRLDMEDISFHKR 167
Cdd:pfam02223  79 QGKTVIVDRYLFSGIAYQGAKGG-DLDLVLSLNPDVPG--KPDLTFLLDVDPEVALKRLRR--RGELEKTEFEQLDFLRK 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446599879  168 VREGYLQVVeRFSDRIVLVNADQPmeklIEEVVQII 203
Cdd:pfam02223 154 VRERYLELA-KFDERIKIIDASLS----IEEVHEEI 184
PLN02924 PLN02924
thymidylate kinase
 2-205 1.34e-11

thymidylate kinase


Pssm-ID: 178512  Cd Length: 220  Bit Score: 61.28  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   2 KGLFVTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPG-GIAISEDIRTILhkQEYTMMEARTEALLYAAAR---RQH 77
Cdd:PLN02924  15 RGALIVLEGLDRSGKSTQCAKLVSFLKGLGVAAELWRFPDrTTSVGQMISAYL--SNKSQLDDRAIHLLFSANRwekRSL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879  78 LVEKVMPALNedylVLCDRFIDSSLAYQGyARGLGMD--KVFEINRFAtedcmPSLTIYLDIEPEIGLARiekdAGREVN 155
Cdd:PLN02924  93 MERKLKSGTT----LVVDRYSYSGVAFSA-AKGLDLEwcKAPEVGLPA-----PDLVLYLDISPEEAAER----GGYGGE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446599879 156 RldMEDISFHKRVREGYLQVVErfsDRIVLVNADQPMEKLIEEVVQIIED 205
Cdd:PLN02924 159 R--YEKLEFQKKVAKRFQTLRD---SSWKIIDASQSIEEVEKKIREVVLD 203
PRK07933 PRK07933
dTMP kinase;
6-205 3.38e-06

dTMP kinase;


Pssm-ID: 236133  Cd Length: 213  Bit Score: 46.12  E-value: 3.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   6 VTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATREPG-GIAISEDI-RTILHKQEYTMME-ARTEALLYAAARRQhLVEKV 82
Cdd:PRK07933   3 IAIEGVDGAGKRTLTEALRAALEARGRSVATLAFPRyGRSVHADLaAEALHGRHGDLADsVYAMATLFALDRAG-ARDEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879  83 MPALNEDYLVLCDRFIDSSLAYQGyARgLGMDKV---------FEINRFATEdcMPSLTIYLDIEPEIGLARIEKDAGRE 153
Cdd:PRK07933  82 AGLLAAHDVVILDRYVASNAAYSA-AR-LHQDADgeavawvaeLEFGRLGLP--VPDLQVLLDVPVELAAERARRRAAQD 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446599879 154 VNR-LDM--EDISFHKRVREGYLQVVER--FSDRIVlVNADQPMEKLIEEVVQIIED 205
Cdd:PRK07933 158 ADRaRDAyeRDDGLQQRTGAVYAELAAQgwGGPWLV-VDPDVDPAALAARLAAALLP 213
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 2-105 2.46e-04

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 39.85  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   2 KGLFVTIEGPEGSGKTTLIKSLLPYFEQKEQKVMATrEPGGIAisediRTILhkQEYTMMEART-EALLYAAARRQhLVE 80
Cdd:cd17933   11 RNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLA-APTGKA-----AKRL--SESTGIEASTiHRLLGINPGGG-GFY 81

                         90       100
                 ....*....|....*....|....*..
gi 446599879  81 KVMPALNEDYLVLCDRF--IDSSLAYQ 105
Cdd:cd17933   82 YNEENPLDADLLIVDEAsmVDTRLMAA 108
AAA_28 pfam13521
AAA domain;
5-172 3.60e-04

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 39.55  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879    5 FVTIEGPEGSGKTTLIKSLlpyfeqkeqkvmaTREPGGIAISEDIRTILHKQ---EYTMMEARTEALLYAAARRQHLVEK 81
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEAL-------------AARFGYPVVPEAAREILEELgadGGDALPWVEDLLAFARGVLEAQLED 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599879   82 VMPALNEDYLVlCDRfidSSLAYQGYARGLG---MDKVFEINRFATEDcmpsLTIYLDIEPEiglarIEKDAGRevnRLD 158
Cdd:pfam13521  68 EAAAAANDLLF-FDR---GPLDTLAYSRAYGgpcPPELEAAARASRYD----LVFLLPPDPE-----IVQDGER---RED 131

                         170
                  ....*....|....*
gi 446599879  159 MED-ISFHKRVREGY 172
Cdd:pfam13521 132 PEErERFHERLREAL 146
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 2-24 5.13e-03

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 36.68  E-value: 5.13e-03
                         10        20
                 ....*....|....*....|...
gi 446599879   2 KGLFVTIEGPEGSGKTTLIKSLL 24
Cdd:cd03250   30 KGELVAIVGPVGSGKSSLLSALL 52
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 2-24 5.27e-03

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 36.74  E-value: 5.27e-03
                         10        20
                 ....*....|....*....|...
gi 446599879   2 KGLFVTIEGPEGSGKTTLIKSLL 24
Cdd:cd03235   24 PGEFLAIVGPNGAGKSTLLKAIL 46
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 2-24 6.08e-03

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 36.26  E-value: 6.08e-03
                         10        20
                 ....*....|....*....|...
gi 446599879   2 KGLFVTIEGPEGSGKTTLIKSLL 24
Cdd:cd03214   24 AGEIVGILGPNGAGKSTLLKTLA 46
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 2-24 9.17e-03

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 35.84  E-value: 9.17e-03
                         10        20
                 ....*....|....*....|...
gi 446599879   2 KGLFVTIEGPEGSGKTTLIKSLL 24
Cdd:COG1121   31 PGEFVAIVGPNGAGKSTLLKAIL 53
 
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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