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Conserved domains on  [gi|505181585|ref|WP_015368687|]
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MULTISPECIES: plasmid stability protein StbA [Klebsiella]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

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 3.04e-148

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: 419.16  E-value: 3.04e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585    1 MRIFIDDGSTNIKMLWEQDGETFTHISPNSFKRGWSATFGAGKPFNYTVDDEKYSFDLITPDALPTNNIDWQYSPLNSIA 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSVSLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585   81 VHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLREVKLNKGVVFNITKVTVRPESIPAGISLCDELK 160
Cdd:pfam06406  81 IHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFEVLKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  161 PSHSVLIVDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARANTDTSSYNVDQIIINRHDEEYLTDNIND 240
Cdd:pfam06406 161 ELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQRINN 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505181585  241 PDAVSEVKKVISNSIERLTTRVLTAIDSFKGYSHAIVIGGGAPLVADAIRERMGLREDRFVVADEPQFALVRGL 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 3.04e-148

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


Pssm-ID: 310773 [Multi-domain]  Cd Length: 317  Bit Score: 419.16  E-value: 3.04e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585    1 MRIFIDDGSTNIKMLWEQDGETFTHISPNSFKRGWSATFGAGKPFNYTVDDEKYSFDLITPDALPTNNIDWQYSPLNSIA 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSVSLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585   81 VHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLREVKLNKGVVFNITKVTVRPESIPAGISLCDELK 160
Cdd:pfam06406  81 IHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFEVLKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  161 PSHSVLIVDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARANTDTSSYNVDQIIINRHDEEYLTDNIND 240
Cdd:pfam06406 161 ELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQRINN 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505181585  241 PDAVSEVKKVISNSIERLTTRVLTAIDSFKGYSHAIVIGGGAPLVADAIRERMGLREDRFVVADEPQFALVRGL 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 4.43e-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: 274.15  E-value: 4.43e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585   3 IFIDDGSTNIKM-LWEQDGETFTHISPNSFKRGWSATFGAGK---PFNYTVDDEKYSFDLITPDALPTNNIDWQYSPLNS 78
Cdd:cd24022    1 VGIDDGSANIKVaWGEDDGKIKTFKIPSRARRGAAVSGSLGGgsqVFNYEVDGERYTVGDVVSDPIDTRNDDYQTSDLNR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  79 IAVHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLREVKLNKGV-VFNITKVTVRPESIPAGISLC- 156
Cdd:cd24022   81 VLVHHALHQAGLGGRKVDIVTGLPVSQYYYKDGQKNTELIERKKKNLKKPVTLLGGKsPATIVSVKVMPEGVAAYFDYLl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 157 -------DELKPSHSVLIVDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARA--NTDTSSYNVDQIIIN 227
Cdd:cd24022  161 dedgngtDEEEEEGPVAVIDIGGTTTDIAVVSGGLSIDHARSGTIELGVLDVRDALKDALKKRfgLSSISDAELDRALRT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 228 RHDeeyltdnINDPDAVSEVKKVISNSIERLTTRVLTAIDSFKG----YSHAIVIGGGAPLVADAIRERMGlreDRFVVA 303
Cdd:cd24022  241 GKF-------RLNGGKEVDVSDLVNEAIAEVAERILNEIKRRLGdasdLDRVIFVGGGAELLEDELKEALG---PNAIIV 310

                        330
                 ....*....|.
gi 505181585 304 DEPQFALVRGL 314
Cdd:cd24022  311 DEPEFANARGM 321
PRK13917 PRK13917
plasmid segregation protein ParM; Provisional
 72-314 1.02e-03

plasmid segregation protein ParM; Provisional


Pssm-ID: 184393 [Multi-domain]  Cd Length: 344  Bit Score: 40.26  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  72 QYSPLNSIAVHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQyrlDNIER-KKKSLLREVKlNKGVVFNITKVTVRPEsiP 150
Cdd:PRK13917  89 QFKTLVKCALAGLAARTVPEEVVEVVVATGMPSEEIGTDKV---AKFEKlLNKSRLIEIN-GIAVTINVKGVKVVAQ--P 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 151 AGISL----------CDELKPSHSVLIVDLGGTTLDISMVAGQMTSVSRIYGDPKLgvslVTDAVKLALAR-ANTDTSSY 219
Cdd:PRK13917 163 MGTLLdlyldndgvvADKAFEEGKVSVIDFGSGTTDLDTIQNLKRVEEESFVIPKG----TIDVYKRIASHiSKKEEGAS 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 220 NVDQIIINRHDEEYLTDNINDP-DAVSEVKKVISNSIERLTTRVLTAIDSFKGYSHAIVIGGGAPLVADAIRERMGlred 298
Cdd:PRK13917 239 ITPYMLEKGLEYGACKLNQKTViDFKDEFYKEQDSVIDEVMSGFEIAVGNINSFDRVIVTGGGANIFFDSLSHWYS---- 314

                        250
                 ....*....|....*.
gi 505181585 299 RFVVADEPQFALVRGL 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 3.04e-148

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


Pssm-ID: 310773 [Multi-domain]  Cd Length: 317  Bit Score: 419.16  E-value: 3.04e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585    1 MRIFIDDGSTNIKMLWEQDGETFTHISPNSFKRGWSATFGAGKPFNYTVDDEKYSFDLITPDALPTNNIDWQYSPLNSIA 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSVSLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585   81 VHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLREVKLNKGVVFNITKVTVRPESIPAGISLCDELK 160
Cdd:pfam06406  81 IHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFEVLKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  161 PSHSVLIVDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARANTDTSSYNVDQIIINRHDEEYLTDNIND 240
Cdd:pfam06406 161 ELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQRINN 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505181585  241 PDAVSEVKKVISNSIERLTTRVLTAIDSFKGYSHAIVIGGGAPLVADAIRERMGLREDRFVVADEPQFALVRGL 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 4.43e-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: 274.15  E-value: 4.43e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585   3 IFIDDGSTNIKM-LWEQDGETFTHISPNSFKRGWSATFGAGK---PFNYTVDDEKYSFDLITPDALPTNNIDWQYSPLNS 78
Cdd:cd24022    1 VGIDDGSANIKVaWGEDDGKIKTFKIPSRARRGAAVSGSLGGgsqVFNYEVDGERYTVGDVVSDPIDTRNDDYQTSDLNR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  79 IAVHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLREVKLNKGV-VFNITKVTVRPESIPAGISLC- 156
Cdd:cd24022   81 VLVHHALHQAGLGGRKVDIVTGLPVSQYYYKDGQKNTELIERKKKNLKKPVTLLGGKsPATIVSVKVMPEGVAAYFDYLl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 157 -------DELKPSHSVLIVDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARA--NTDTSSYNVDQIIIN 227
Cdd:cd24022  161 dedgngtDEEEEEGPVAVIDIGGTTTDIAVVSGGLSIDHARSGTIELGVLDVRDALKDALKKRfgLSSISDAELDRALRT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 228 RHDeeyltdnINDPDAVSEVKKVISNSIERLTTRVLTAIDSFKG----YSHAIVIGGGAPLVADAIRERMGlreDRFVVA 303
Cdd:cd24022  241 GKF-------RLNGGKEVDVSDLVNEAIAEVAERILNEIKRRLGdasdLDRVIFVGGGAELLEDELKEALG---PNAIIV 310

                        330
                 ....*....|.
gi 505181585 304 DEPQFALVRGL 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 4.34e-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: 84.88  E-value: 4.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585   3 IFIDDGSTNIKMLWEQDGETFThisPNSFKR---GWSATFGAGKPFNYTVDDEKYSFD---LITPDALPTNNIDWQYSPL 76
Cdd:cd10227    1 IGIDIGNGNTKVVTGGGKEFKF---PSAVAEareSSLDDGLLEDDIIVEYNGKRYLVGelaLREGGGGRSTGDDKKKSED 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  77 NSIAVHHAL-LTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNIERKKKSLLRevklNKGVVFNITKVTVRPESIPAGISL 155
Cdd:cd10227   78 ALLLLLAALaLLGDDEEVDVNLVVGLPISEYKEEKKELKKKLLKGLHEFTFN----GKERRITINDVKVLPEGAGAYLDY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 156 CDELKPSHS--VLIVDLGGTTLDISMVAGqmtsvsriyGDPKLGVSLVTDavklalarantdtssynvdqiiinrHDEEY 233
Cdd:cd10227  154 LLDDDELEDgnVLVIDIGGGTTDILTFEN---------GKPIEESSDTLP-------------------------GGEEA 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 234 LTDNINdpDAVSEVKKVISNSIERlttrvltaIDSFkgyshaIVIGGGAPLVADAIRERmglREDRFVVADEPQFALVRG 313
Cdd:cd10227  200 LEKYAD--DILNELLKKLGDELDS--------ADKI------LLTGGGAELLKDYLKEA---YFPNIIVLDDPQFANARG 260


                 .
gi 505181585 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 4.11e-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: 68.47  E-value: 4.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  43 KPFNYTVDDEKYSFDLITPDALPTNNIDWQYSP----LNSIAVHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQYRLDNI 118
Cdd:cd24021   51 NGEEYVWGEDIYKSGKDEEIASTYSGEDRYKSEefklLSLIALAKLAKDYDEDVVEVVVVTGLPSEDYDTEVEEELKKVL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 119 ERKKksllrEVKLN-KGVVFNITKVTVRPESI---------PAGISLCDELKpSHSVLIVDLGGTTLDISMVAGQmtsvs 188
Cdd:cd24021  131 KGEH-----TVKINgKERTINVKDVYVIPQPLgtlynllldENGEVKNEELE-DSKVLIIDIGGGTTDVDVINGL----- 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 189 riygdpklgvslvtdavKLALARANTDTSSYNVDQIIINRhdeeyltdnindpdavsEVKKVISNSIERLTTRVLTAI-- 266
Cdd:cd24021  200 -----------------KIDENRFQIETGMKDVYDEIAKE-----------------DITEIVEKAIEEYAEEIVAEInn 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 505181585 267 --DSFKGYSHAIVIGGGAPLVADAIRERmgLREDRFVVADEPQFALVRGLKIIG 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 5.39e-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: 62.73  E-value: 5.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  75 PLNSIAVHhALLTSGLEPQDVEIVVT------LPLTEFYDEDAQyrldniERKKKSLLRE--VKLNKG------VVFNIT 140
Cdd:cd24023  100 TLTAIAYY-AVKEAYEDDIKDEIEVKvdlstgLPISEYKKEGAK------EFFERFLKGEhtVTFLDGpgkgvtVTIKFE 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 141 KVTVRPESIPAGISL-------------CDELKPSHSVLIVDLGGTTLDISMVAGQMTSVSRIYGDpKLGV-SLVTDAVK 206
Cdd:cd24023  173 DVKVLPEGVAALFALiydedgnervedtEDEDLKEKNILIIDIGGGTTDVAVFEGGKFDPDLSTGI-DLGIgTALDEIIK 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 207 LALARANTDTSSYNVDQIIINRHDEEYLTDNINDPDAVSEVKKVISNSIERLTTRVLTAI-DSFKGYSHAIVIGGGAPLV 285
Cdd:cd24023  252 ELKKEYGVEFDRRRLLFELIIKKKEYKDKNRGKKVDLTDIVEKALEELAEEILDEIEKKWnKAGNDIEVIYVYGGGSILL 331

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 505181585 286 ADAIRERMGLREDR------FVVADEPQFALVRGLKI 316
Cdd:cd24023  332 KDYLKELLKELCDEskipliFIPEEYAQFLNARGLLI 368
ASKHA_NBD_ParM_Alp12-like cd24026
nucleotide-binding domain (NBD) of Clostridium tetani actin-like protein Alp12 and similar ...
 44-318 6.42e-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: 59.22  E-value: 6.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  44 PFNYTV--DDEKYsfdLITPDALPTNNIDWQYSPLNSIAVHHALLTSGLEPQDVEI--VVTLPLTEFYDEDA--QYRlDN 117
Cdd:cd24026   43 GNSYKVeyDGKEY---LIGEQGEEYDYDTSKASLLHKLCTYTAIAKLLENDKGNEVnlVVGCPLNIYKNKELkeEYK-EF 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 118 IERKKK---SLLREVKLnkgvvFNITKVTVRPESIPAgISLCDELKPSHSVLIVDLGGTTLDISMVAGQMTSVSRIYGDp 194
Cdd:cd24026  119 IKGNGKiiiIVNGEKKS-----FKITDVTVKPEGSGV-IYRNPEKFKNKNVGVIDIGGLNVNFCIYDNGIPIPESMFTD- 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 195 KLGVSLVTDAVKLAL-ARANTDTSSYNVDQIIINRhdeeYLTDNINDPDavsEVKKVISNSIERLTTRVLTAIDSFKG-- 271
Cdd:cd24026  192 NLGGNVLENKIKEALnSYFGGNIQDYDILNILING----YIKFNGEIEE---ESKEIIEEIKDEHLKEIINKIKSRKWnl 264

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 505181585 272 -YSHAIVIGGGAPLVADAIRERMglreDRFVVADEPQFALVRGLKIIG 318
Cdd:cd24026  265 eNMDIIFVGGTSLLLKDYIKELF----PNATISEDAQWDNVEGFLKVG 308
ASKHA_NBD_ParM_pCBH-like cd24025
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ...
 84-314 1.09e-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: 58.45  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  84 ALLTSGLEpQDVEIVVTLPLTEFYDEDAQYRlDNIERKKKSLLREVKLNKgVVFNITKVTVRPESIPAGISLC------- 156
Cdd:cd24025   94 ALLAAEDD-EPVSLVTGLPLSYYKTQKEALE-EMLKGLHAVVVGVDGGTE-KRITIDRVRVFPQGAGALYDALldddgqi 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 157 -DELKPSHSVLIVDLGGTTLDISMVAGQMTSVSRIYGDPKLGVSLVTDAVKLALARANTDTSS-YNVDQIIINRhDEEYL 234
Cdd:cd24025  171 iDKALAKGRVGVIDIGYRTTDYVVFEDGEFLVPELSGSLETGMSTAYRAIANALEEEYGIDLDlHELDRALREG-KIRVR 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 235 TDNINDPDAVSEVKKVISNSIerlTTRVLTAIDSFKGYSHAIVI-GGGAPLVADAIRERMglreDRFVVADEPQFALVRG 313
Cdd:cd24025  250 GKEIDLSDLIDEALKELARQI---ANEIRSLWGDGLGDLDAIILaGGGAELLAPYLKEMF----PNAEVVPDPQFANARG 322


                 .
gi 505181585 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 4.15e-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: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  82 HHALLTSGLEPQDVEIVVTLPltEFYDEDAQYRLdnierkkKSLLREVklnkGVVFNITKVTVRPESIPAGISLCDE--- 158
Cdd:cd10170   62 ELGDRIWELEKAPIEVVITVP--AGWSDAAREAL-------REAARAA----GFGSDSDNVRLVSEPEAAALYALEDkgd 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 159 ---LKPSHSVLIVDLGGTTLDISMVagQMTSVS-------RIYGDPKLGVSLVTDAV------KLALARANTDTSSYNVD 222
Cdd:cd10170  129 llpLKPGDVVLVCDAGGGTVDLSLY--EVTSGSpllleevAPGGGALLGGTDIDEAFekllreKLGDKGKDLGRSDADAL 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 223 QIIINRHDEEYLTDNINDPDAV------------------------SEVKKVISNSIERLTTRVLTAIDSFKGYS-HAIV 277
Cdd:cd10170  207 AKLLREFEEAKKRFSGGEEDERlvpsllggglpelglekgtlllteEEIRDLFDPVIDKILELIEEQLEAKSGTPpDAVV 286

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 505181585 278 IGGGA---PLVADAIRERMGLREDRFV-VADEPQFALVRGL 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 1.30e-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: 43.04  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 124 SLLREVKLNkgvvfnITKVTVRPESIPAGISLCDELKPSHSVLIVDLGGTTLDISMVAGQMTSVSRIygdPKLGVSLVTD 203
Cdd:cd24049  143 ELLKEAGLK------PVAIDVESFALARALEYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRS---IPVGGNDITE 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 204 AVklalarantdTSSYNVDQIIINRHDEEYLTDNINDPDAVSEVKKVISNSIERLTTRVLTAIDSFKG------YSHAIV 277
Cdd:cd24049  214 AI----------AKALGLSFEEAEELKREYGLLLEGEEGELKKVAEALRPVLERLVSEIRRSLDYYRSqnggepIDKIYL 283

                        170       180
                 ....*....|....*....|
gi 505181585 278 IGGGA--PLVADAIRERMGL 295
Cdd:cd24049  284 TGGGSllPGLDEYLSERLGI 303
PRK13917 PRK13917
plasmid segregation protein ParM; Provisional
 72-314 1.02e-03

plasmid segregation protein ParM; Provisional


Pssm-ID: 184393 [Multi-domain]  Cd Length: 344  Bit Score: 40.26  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585  72 QYSPLNSIAVHHALLTSGLEPQDVEIVVTLPLTEFYDEDAQyrlDNIER-KKKSLLREVKlNKGVVFNITKVTVRPEsiP 150
Cdd:PRK13917  89 QFKTLVKCALAGLAARTVPEEVVEVVVATGMPSEEIGTDKV---AKFEKlLNKSRLIEIN-GIAVTINVKGVKVVAQ--P 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 151 AGISL----------CDELKPSHSVLIVDLGGTTLDISMVAGQMTSVSRIYGDPKLgvslVTDAVKLALAR-ANTDTSSY 219
Cdd:PRK13917 163 MGTLLdlyldndgvvADKAFEEGKVSVIDFGSGTTDLDTIQNLKRVEEESFVIPKG----TIDVYKRIASHiSKKEEGAS 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181585 220 NVDQIIINRHDEEYLTDNINDP-DAVSEVKKVISNSIERLTTRVLTAIDSFKGYSHAIVIGGGAPLVADAIRERMGlred 298
Cdd:PRK13917 239 ITPYMLEKGLEYGACKLNQKTViDFKDEFYKEQDSVIDEVMSGFEIAVGNINSFDRVIVTGGGANIFFDSLSHWYS---- 314

                        250
                 ....*....|....*.
gi 505181585 299 RFVVADEPQFALVRGL 314
Cdd:PRK13917 315 DVEKADESQFANVRGY 330
 
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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