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Conserved domains on  [gi|490248560|ref|WP_004146678|]
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MULTISPECIES: plasmid segregation protein ParM [Klebsiella]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 1-314 2.48e-147

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member pfam06406:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 317  Bit Score: 416.85  E-value: 2.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560    1 MRIFIDDGSTNIKMLWEQDGETFTHISPNSFKRGWSATFGSGKPFNYTVDDEKYSFDLITPDALPTNNIDWQYSPLNSIA 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSVSLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560   81 VHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLRDVKLNKGVVFNITKVTVRPESIPAGISLCDELK 160
Cdd:pfam06406  81 IHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFEVLKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  161 PSHSVLIIDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARANTDTSSYNVDQIIINRHDEEYLTDNIND 240
Cdd:pfam06406 161 ELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQRINN 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490248560  241 PDAVSEVKKVINNSIERLTTRVLTAIDSFKGYSHAIVIGGGAPLVADAIRERMGLREDRFVVAEEPQFALVRGL 314
Cdd:pfam06406 241 EDKRASVMEVINEAVKKLEQRVIRALSRFSGYTHVMVVGGGAELIATAIKKHTGVPDARFIKVDNPQFALVNGM 314
 
Name Accession Description Interval E-value
StbA pfam06406
StbA protein; This family consists of several bacterial StbA plasmid stability proteins.
 1-314 2.48e-147

StbA protein; This family consists of several bacterial StbA plasmid stability proteins.


Pssm-ID: 310773 [Multi-domain]  Cd Length: 317  Bit Score: 416.85  E-value: 2.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560    1 MRIFIDDGSTNIKMLWEQDGETFTHISPNSFKRGWSATFGSGKPFNYTVDDEKYSFDLITPDALPTNNIDWQYSPLNSIA 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSVSLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560   81 VHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLRDVKLNKGVVFNITKVTVRPESIPAGISLCDELK 160
Cdd:pfam06406  81 IHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFEVLKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  161 PSHSVLIIDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARANTDTSSYNVDQIIINRHDEEYLTDNIND 240
Cdd:pfam06406 161 ELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQRINN 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490248560  241 PDAVSEVKKVINNSIERLTTRVLTAIDSFKGYSHAIVIGGGAPLVADAIRERMGLREDRFVVAEEPQFALVRGL 314
Cdd:pfam06406 241 EDKRASVMEVINEAVKKLEQRVIRALSRFSGYTHVMVVGGGAELIATAIKKHTGVPDARFIKVDNPQFALVNGM 314
ASKHA_NBD_ParM_R1-like cd24022
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ...
 3-314 1.58e-91

nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.


Pssm-ID: 466872 [Multi-domain]  Cd Length: 324  Bit Score: 275.30  E-value: 1.58e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560   3 IFIDDGSTNIKM-LWEQDGETFTHISPNSFKRGWSATFGSGK---PFNYTVDDEKYSFDLITPDALPTNNIDWQYSPLNS 78
Cdd:cd24022    1 VGIDDGSANIKVaWGEDDGKIKTFKIPSRARRGAAVSGSLGGgsqVFNYEVDGERYTVGDVVSDPIDTRNDDYQTSDLNR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  79 IAVHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLRDVKLNKGV-VFNITKVTVRPESIPAGISLC- 156
Cdd:cd24022   81 VLVHHALHQAGLGGRKVDIVTGLPVSQYYYKDGQKNTELIERKKKNLKKPVTLLGGKsPATIVSVKVMPEGVAAYFDYLl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 157 -------DELKPSHSVLIIDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARA--NTDTSSYNVDQIIIN 227
Cdd:cd24022  161 dedgngtDEEEEEGPVAVIDIGGTTTDIAVVSGGLSIDHARSGTIELGVLDVRDALKDALKKRfgLSSISDAELDRALRT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 228 RHDeeyltdnINDPDAVSEVKKVINNSIERLTTRVLTAIDSFKG----YSHAIVIGGGAPLVADAIRERMGlreDRFVVA 303
Cdd:cd24022  241 GKF-------RLNGGKEVDVSDLVNEAIAEVAERILNEIKRRLGdasdLDRVIFVGGGAELLEDELKEALG---PNAIIV 310

                        330
                 ....*....|.
gi 490248560 304 EEPQFALVRGL 314
Cdd:cd24022  311 DEPEFANARGM 321
PRK13917 PRK13917
plasmid segregation protein ParM; Provisional
 72-314 3.24e-04

plasmid segregation protein ParM; Provisional


Pssm-ID: 184393 [Multi-domain]  Cd Length: 344  Bit Score: 41.80  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  72 QYSPLNSIAVHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKksllRDVKLN-KGVVFNITKVTVRPEsiP 150
Cdd:PRK13917  89 QFKTLVKCALAGLAARTVPEEVVEVVVATGMPSEEIGTDKVAKFEKLLNKS----RLIEINgIAVTINVKGVKVVAQ--P 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 151 AGISL----------CDELKPSHSVLIIDLGGTTLDISMVAGQMTSVSRIYGDPKLgvslVTDAVKLALAR-ANTDTSSY 219
Cdd:PRK13917 163 MGTLLdlyldndgvvADKAFEEGKVSVIDFGSGTTDLDTIQNLKRVEEESFVIPKG----TIDVYKRIASHiSKKEEGAS 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 220 NVDQIIINRHDEEYLTDNINDP-DAVSEVKKVINNSIERLTTRVLTAIDSFKGYSHAIVIGGGAPLVADAIRERMGlred 298
Cdd:PRK13917 239 ITPYMLEKGLEYGACKLNQKTViDFKDEFYKEQDSVIDEVMSGFEIAVGNINSFDRVIVTGGGANIFFDSLSHWYS---- 314

                        250
                 ....*....|....*.
gi 490248560 299 RFVVAEEPQFALVRGL 314
Cdd:PRK13917 315 DVEKADESQFANVRGY 330
 
Name Accession Description Interval E-value
StbA pfam06406
StbA protein; This family consists of several bacterial StbA plasmid stability proteins.
 1-314 2.48e-147

StbA protein; This family consists of several bacterial StbA plasmid stability proteins.


Pssm-ID: 310773 [Multi-domain]  Cd Length: 317  Bit Score: 416.85  E-value: 2.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560    1 MRIFIDDGSTNIKMLWEQDGETFTHISPNSFKRGWSATFGSGKPFNYTVDDEKYSFDLITPDALPTNNIDWQYSPLNSIA 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSVSLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560   81 VHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLRDVKLNKGVVFNITKVTVRPESIPAGISLCDELK 160
Cdd:pfam06406  81 IHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFEVLKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  161 PSHSVLIIDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARANTDTSSYNVDQIIINRHDEEYLTDNIND 240
Cdd:pfam06406 161 ELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQRINN 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490248560  241 PDAVSEVKKVINNSIERLTTRVLTAIDSFKGYSHAIVIGGGAPLVADAIRERMGLREDRFVVAEEPQFALVRGL 314
Cdd:pfam06406 241 EDKRASVMEVINEAVKKLEQRVIRALSRFSGYTHVMVVGGGAELIATAIKKHTGVPDARFIKVDNPQFALVNGM 314
ASKHA_NBD_ParM_R1-like cd24022
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ...
 3-314 1.58e-91

nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.


Pssm-ID: 466872 [Multi-domain]  Cd Length: 324  Bit Score: 275.30  E-value: 1.58e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560   3 IFIDDGSTNIKM-LWEQDGETFTHISPNSFKRGWSATFGSGK---PFNYTVDDEKYSFDLITPDALPTNNIDWQYSPLNS 78
Cdd:cd24022    1 VGIDDGSANIKVaWGEDDGKIKTFKIPSRARRGAAVSGSLGGgsqVFNYEVDGERYTVGDVVSDPIDTRNDDYQTSDLNR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  79 IAVHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLRDVKLNKGV-VFNITKVTVRPESIPAGISLC- 156
Cdd:cd24022   81 VLVHHALHQAGLGGRKVDIVTGLPVSQYYYKDGQKNTELIERKKKNLKKPVTLLGGKsPATIVSVKVMPEGVAAYFDYLl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 157 -------DELKPSHSVLIIDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARA--NTDTSSYNVDQIIIN 227
Cdd:cd24022  161 dedgngtDEEEEEGPVAVIDIGGTTTDIAVVSGGLSIDHARSGTIELGVLDVRDALKDALKKRfgLSSISDAELDRALRT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 228 RHDeeyltdnINDPDAVSEVKKVINNSIERLTTRVLTAIDSFKG----YSHAIVIGGGAPLVADAIRERMGlreDRFVVA 303
Cdd:cd24022  241 GKF-------RLNGGKEVDVSDLVNEAIAEVAERILNEIKRRLGdasdLDRVIFVGGGAELLEDELKEALG---PNAIIV 310

                        330
                 ....*....|.
gi 490248560 304 EEPQFALVRGL 314
Cdd:cd24022  311 DEPEFANARGM 321
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
 3-314 3.18e-19

nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466825 [Multi-domain]  Cd Length: 263  Bit Score: 85.27  E-value: 3.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560   3 IFIDDGSTNIKMLWEQDGETFThisPNSFKR---GWSATFGSGKPFNYTVDDEKYSFD---LITPDALPTNNIDWQYSPL 76
Cdd:cd10227    1 IGIDIGNGNTKVVTGGGKEFKF---PSAVAEareSSLDDGLLEDDIIVEYNGKRYLVGelaLREGGGGRSTGDDKKKSED 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  77 NSIAVHHAL-LTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLRDVKLNkgvvFNITKVTVRPESIPAGISL 155
Cdd:cd10227   78 ALLLLLAALaLLGDDEEVDVNLVVGLPISEYKEEKKELKKKLLKGLHEFTFNGKERR----ITINDVKVLPEGAGAYLDY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 156 CDELKPSHS--VLIIDLGGTTLDISMVAGqmtsvsriyGDPKLGVSLVTDavklalarantdtssynvdqiiinrHDEEY 233
Cdd:cd10227  154 LLDDDELEDgnVLVIDIGGGTTDILTFEN---------GKPIEESSDTLP-------------------------GGEEA 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 234 LTDNINdpDAVSEVKKVINNSIERlttrvltaIDSFkgyshaIVIGGGAPLVADAIRERmglREDRFVVAEEPQFALVRG 313
Cdd:cd10227  200 LEKYAD--DILNELLKKLGDELDS--------ADKI------LLTGGGAELLKDYLKEA---YFPNIIVLDDPQFANARG 260


                 .
gi 490248560 314 L 314
Cdd:cd10227  261 L 261
ASKHA_NBD_ParM_Psk41-like cd24021
nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and ...
 43-318 2.06e-13

nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and similar proteins from the ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Staphylococcus aureus pSK41 actin-like ParM protein, which is functionally homologous to R1 ParM, a known actin homologue, suggesting that it may also form filaments to drive partition. However, pSK41 ParM shows the strongest structural homology to the archaeal actin-like protein Thermoplasma acidophilum Ta0583, but not R1 ParM.


Pssm-ID: 466871 [Multi-domain]  Cd Length: 298  Bit Score: 69.24  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  43 KPFNYTVDDEKYSFDLITPDALPTNNIDWQYSP----LNSIAVHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNI 118
Cdd:cd24021   51 NGEEYVWGEDIYKSGKDEEIASTYSGEDRYKSEefklLSLIALAKLAKDYDEDVVEVVVVTGLPSEDYDTEVEEELKKVL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 119 ERKKKsllrdVKLN-KGVVFNITKVTVRPESI---------PAGISLCDELKpSHSVLIIDLGGTTLDISMVAGQmtsvs 188
Cdd:cd24021  131 KGEHT-----VKINgKERTINVKDVYVIPQPLgtlynllldENGEVKNEELE-DSKVLIIDIGGGTTDVDVINGL----- 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 189 riygdpklgvslvtdavKLALARANTDTSSYNVDQIIINRhdeeyltdnindpdavsEVKKVINNSIERLTTRVLTAI-- 266
Cdd:cd24021  200 -----------------KIDENRFQIETGMKDVYDEIAKE-----------------DITEIVEKAIEEYAEEIVAEInn 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490248560 267 --DSFKGYSHAIVIGGGAPLVADAIRERmgLREDRFVVAEEPQFALVRGLKIIG 318
Cdd:cd24021  246 afKDLDSFDKVIFTGGGANILNKYLKEK--LEGDNFVFVENPQTANVRGYYKYG 297
ASKHA_NBD_ParM_Alp7A-like cd24023
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar ...
 75-316 9.43e-11

nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Bacillus subtilis actin-like protein Alp7A, a plasmid partitioning protein that functions in plasmid segregation. The subfamily also includes Bacillus thuringiensis ParM hybrid fusion protein.


Pssm-ID: 466873 [Multi-domain]  Cd Length: 368  Bit Score: 61.96  E-value: 9.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  75 PLNSIAVHhALLTSGLEPQDVEIVVT------LPLTEfydedaqYRLDNIERKKKSLLRD---VKLNKG------VVFNI 139
Cdd:cd24023  100 TLTAIAYY-AVKEAYEDDIKDEIEVKvdlstgLPISE-------YKKEGAKEFFERFLKGehtVTFLDGpgkgvtVTIKF 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 140 TKVTVRPESIPAGISL-------------CDELKPSHSVLIIDLGGTTLDISMVAGQMTSVSRIYGDpKLGV-SLVTDAV 205
Cdd:cd24023  172 EDVKVLPEGVAALFALiydedgnervedtEDEDLKEKNILIIDIGGGTTDVAVFEGGKFDPDLSTGI-DLGIgTALDEII 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 206 KLALARANTDTSSYNVDQIIINRHDEEYLTDNINDPDAVSEVKKVINNSIERLTTRVLTAI-DSFKGYSHAIVIGGGAPL 284
Cdd:cd24023  251 KELKKEYGVEFDRRRLLFELIIKKKEYKDKNRGKKVDLTDIVEKALEELAEEILDEIEKKWnKAGNDIEVIYVYGGGSIL 330

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490248560 285 VADAIRERMGLREDR------FVVAEEPQFALVRGLKI 316
Cdd:cd24023  331 LKDYLKELLKELCDEskipliFIPEEYAQFLNARGLLI 368
ASKHA_NBD_ParM_Alp12-like cd24026
nucleotide-binding domain (NBD) of Clostridium tetani actin-like protein Alp12 and similar ...
 44-318 2.34e-10

nucleotide-binding domain (NBD) of Clostridium tetani actin-like protein Alp12 and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Clostridium tetani actin-like protein Alp12. It is a dynamically unstable force-generating motor involved in segregating the pE88 plasmid, which encodes the lethal tetanus toxin. Alp12 filaments have a unique polymer structure that is entirely different from F-actin and display dynamic behavior like microtubules. Alp12 can be repeatedly cycled between states of polymerization and dissociation, making it a novel candidate for incorporation into fuel-propelled nanobiopolymer machines.


Pssm-ID: 466876 [Multi-domain]  Cd Length: 308  Bit Score: 60.38  E-value: 2.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  44 PFNYTV--DDEKYsfdLITPDALPTNNIDWQYSPLNSIAVHHALLTSGLEPQDVEI--VVTLPLTEFYDEDA--QYRlDN 117
Cdd:cd24026   43 GNSYKVeyDGKEY---LIGEQGEEYDYDTSKASLLHKLCTYTAIAKLLENDKGNEVnlVVGCPLNIYKNKELkeEYK-EF 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 118 IERKKK--SLLRDVKLNkgvvFNITKVTVRPESIPAgISLCDELKPSHSVLIIDLGGTTLDISMVAGQMTSVSRIYGDpK 195
Cdd:cd24026  119 IKGNGKiiIIVNGEKKS----FKITDVTVKPEGSGV-IYRNPEKFKNKNVGVIDIGGLNVNFCIYDNGIPIPESMFTD-N 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 196 LGVSLVTDAVKLAL-ARANTDTSSYNVDQIIINRhdeeYLTDNINDPDavsEVKKVINNSIERLTTRVLTAIDSFKG--- 271
Cdd:cd24026  193 LGGNVLENKIKEALnSYFGGNIQDYDILNILING----YIKFNGEIEE---ESKEIIEEIKDEHLKEIINKIKSRKWnle 265

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 490248560 272 YSHAIVIGGGAPLVADAIRERMglreDRFVVAEEPQFALVRGLKIIG 318
Cdd:cd24026  266 NMDIIFVGGTSLLLKDYIKELF----PNATISEDAQWDNVEGFLKVG 308
ASKHA_NBD_ParM_pCBH-like cd24025
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ...
 84-314 3.49e-09

nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Clostridium botulinum pCBH plasmid segregation protein ParM, an actin-like polymerizing motor. pCBH ParM filament structure is far more complex in comparison to the known filament structures of actin, MreB, and other ParMs. It is bipolar and stiff and like microtubules. The 15 polymerizing strands are likely to exert greater combined force relative to typical two-stranded actin-like filaments.


Pssm-ID: 466875 [Multi-domain]  Cd Length: 326  Bit Score: 56.90  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  84 ALLTSGLEpQDVEIVVTLPLTEFYDEDAQYRlDNIERKKKSLLRDVKLNKgVVFNITKVTVRPESIPAGISLC------- 156
Cdd:cd24025   94 ALLAAEDD-EPVSLVTGLPLSYYKTQKEALE-EMLKGLHAVVVGVDGGTE-KRITIDRVRVFPQGAGALYDALldddgqi 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 157 -DELKPSHSVLIIDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARANTDTSS-YNVDQIIinrhDEEYL 234
Cdd:cd24025  171 iDKALAKGRVGVIDIGYRTTDYVVFEDGEFLVPELSGSLETGMSTAYRAIANALEEEYGIDLDlHELDRAL----REGKI 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 235 TDNINDPDAVSEVKKVINNSIERLTTRVLTAIDSFKGYSHAIVI-GGGAPLVADAIRERMglreDRFVVAEEPQFALVRG 313
Cdd:cd24025  247 RVRGKEIDLSDLIDEALKELARQIANEIRSLWGDGLGDLDAIILaGGGAELLAPYLKEMF----PNAEVVPDPQFANARG 322


                 .
gi 490248560 314 L 314
Cdd:cd24025  323 Y 323
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 82-314 4.55e-08

nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466811 [Multi-domain]  Cd Length: 329  Bit Score: 53.65  E-value: 4.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  82 HHALLTSGLEPQDVEIVVTLPltEFYDEDAQYRLdnierkkKSLLRDVklnkGVVFNITKVTVRPESIPAGISLCDE--- 158
Cdd:cd10170   62 ELGDRIWELEKAPIEVVITVP--AGWSDAAREAL-------REAARAA----GFGSDSDNVRLVSEPEAAALYALEDkgd 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 159 ---LKPSHSVLIIDLGGTTLDISMVagQMTSVS-------RIYGDPKLGVSLVTDAV------KLALARANTDTSSYNVD 222
Cdd:cd10170  129 llpLKPGDVVLVCDAGGGTVDLSLY--EVTSGSpllleevAPGGGALLGGTDIDEAFekllreKLGDKGKDLGRSDADAL 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 223 QIIINRHDEEYLTDNINDPDAV------------------------SEVKKVINNSIERLTTRVLTAIDSFKGYS-HAIV 277
Cdd:cd10170  207 AKLLREFEEAKKRFSGGEEDERlvpsllggglpelglekgtlllteEEIRDLFDPVIDKILELIEEQLEAKSGTPpDAVV 286

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 490248560 278 IGGGA---PLVADAIRERMGLREDRFV-VAEEPQFALVRGL 314
Cdd:cd10170  287 LVGGFsrsPYLRERLRERFGSAGIIIVlRSDDPDTAVARGA 327
ASKHA_NBD_PilM cd24049
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
 124-295 1.89e-04

nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.


Pssm-ID: 466899 [Multi-domain]  Cd Length: 339  Bit Score: 42.65  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 124 SLLRDVKLNkgvvfnITKVTVRPESIPAGISLCDELKPSHSVLIIDLGGTTLDISMVAGQMTSVSRIygdPKLGVSLVTD 203
Cdd:cd24049  143 ELLKEAGLK------PVAIDVESFALARALEYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRS---IPVGGNDITE 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 204 AVklalarantdTSSYNVDQIIINRHDEEYLTDNINDPDAVSEVKKVINNSIERLTTRVLTAIDSFKG------YSHAIV 277
Cdd:cd24049  214 AI----------AKALGLSFEEAEELKREYGLLLEGEEGELKKVAEALRPVLERLVSEIRRSLDYYRSqnggepIDKIYL 283

                        170       180
                 ....*....|....*....|
gi 490248560 278 IGGGA--PLVADAIRERMGL 295
Cdd:cd24049  284 TGGGSllPGLDEYLSERLGI 303
PRK13917 PRK13917
plasmid segregation protein ParM; Provisional
 72-314 3.24e-04

plasmid segregation protein ParM; Provisional


Pssm-ID: 184393 [Multi-domain]  Cd Length: 344  Bit Score: 41.80  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  72 QYSPLNSIAVHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKksllRDVKLN-KGVVFNITKVTVRPEsiP 150
Cdd:PRK13917  89 QFKTLVKCALAGLAARTVPEEVVEVVVATGMPSEEIGTDKVAKFEKLLNKS----RLIEINgIAVTINVKGVKVVAQ--P 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 151 AGISL----------CDELKPSHSVLIIDLGGTTLDISMVAGQMTSVSRIYGDPKLgvslVTDAVKLALAR-ANTDTSSY 219
Cdd:PRK13917 163 MGTLLdlyldndgvvADKAFEEGKVSVIDFGSGTTDLDTIQNLKRVEEESFVIPKG----TIDVYKRIASHiSKKEEGAS 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 220 NVDQIIINRHDEEYLTDNINDP-DAVSEVKKVINNSIERLTTRVLTAIDSFKGYSHAIVIGGGAPLVADAIRERMGlred 298
Cdd:PRK13917 239 ITPYMLEKGLEYGACKLNQKTViDFKDEFYKEQDSVIDEVMSGFEIAVGNINSFDRVIVTGGGANIFFDSLSHWYS---- 314

                        250
                 ....*....|....*.
gi 490248560 299 RFVVAEEPQFALVRGL 314
Cdd:PRK13917 315 DVEKADESQFANVRGY 330
ASKHA_NBD_ParM_Ta0583-like cd24027
nucleotide-binding domain (NBD) of Thermoplasma acidophilum archaeal actin homolog and similar ...
 84-313 8.02e-04

nucleotide-binding domain (NBD) of Thermoplasma acidophilum archaeal actin homolog and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Thermoplasma acidophilum archaeal actin homolog Ta0583, which is the archaeal counterpart of the eukaryotic structural protein actin, such as MreB and ParM. Ta0583 could have a function in cellular organization. It polymerizes into bundles of filaments, forming a helix with a filament width of 5.5 nm and an axial repeating unit of 5.5 nm. Polymerization of Ta0583 requires NTP and is optimal with ATP, but GTP, UTP, CTP, and even the deoxy form of NTP can also support the polymerization reaction. Nucleoside diphosphate or AMP-PNP does not support polymerization.


Pssm-ID: 466877 [Multi-domain]  Cd Length: 323  Bit Score: 40.68  E-value: 8.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560  84 ALLTSGLE---PQDVEIVVTLPLTEFYDEDAqyrlDNIErKKKSLLRDVKLNKGVV--FNITKVTVRPESIPAGISLCDE 158
Cdd:cd24027   87 ALWESGIHndsPVDLFLGTGLPLGTFDLEVK----AAKE-ALENKVLTVTGPEGEVrkINITRLEIRPQGVGAALYLLNQ 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 159 LKPSHS------VLIIDLGGTTLDISMV-AGQMTSVSR-------IYGDPKLGVSLVTDavKLALARANTDTSSYNVDQI 224
Cdd:cd24027  162 GIIEESeqqpgyGVVIDVGSRTTDVLTIrLGDVVELSFslqigvaVYGRAIKALSRKIA--KETGFVVPFDLAQEALSHP 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248560 225 IINRHDEEYltdnindpdavsEVKKVINNSIERLTTRVLTAI-DSFKG----YSHAIVIGGGAPLVADAI-RERMGlreD 298
Cdd:cd24027  240 VLFRQKEQV------------DGPEVSGPILEDLANRIIENIrLNLRGevdrVTSLLLVGGGSNLIGDRFeEIAPG---T 304

                        250
                 ....*....|....*
gi 490248560 299 RFVVAEEPQFALVRG 313
Cdd:cd24027  305 LVKIKPEDQFANVLG 319
 
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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