NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1308675216|gb|PKM47166|]
View 

septum site-determining protein MinC [Firmicutes bacterium HGW-Firmicutes-8]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
minC super family cl46970
septum formation inhibitor; Reviewed
 65-174 2.28e-54

septum formation inhibitor; Reviewed


The actual alignment was detected with superfamily member PRK00513:

Pssm-ID: 179052 [Multi-domain]  Cd Length: 214  Bit Score: 171.55  E-value: 2.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308675216  65 VDENTIL-IKRTVRSGQSIQFDGNVVVLGDVNPGSEIVASGNIIVMGALRGVVHAGATGNKEATVSAFKLQPTQLRIANH 143
Cdd:PRK00513   98 KEEGETKyLRKTVRSGQVVRVPGNLLIIGDVNPGGEVIAGGNIIVLGALRGIAHAGATGNKEAVIAALQLEPTQLRIADV 177

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308675216 144 ITRAPDgDYLSPDHPETARIKDGIVVIEVYQ 174
Cdd:PRK00513  178 IARAPE-DKEKPNYPEVAYIKDGGIVVERLQ 207
 
Name Accession Description Interval E-value
minC PRK00513
septum formation inhibitor; Reviewed
 65-174 2.28e-54

septum formation inhibitor; Reviewed


Pssm-ID: 179052 [Multi-domain]  Cd Length: 214  Bit Score: 171.55  E-value: 2.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308675216  65 VDENTIL-IKRTVRSGQSIQFDGNVVVLGDVNPGSEIVASGNIIVMGALRGVVHAGATGNKEATVSAFKLQPTQLRIANH 143
Cdd:PRK00513   98 KEEGETKyLRKTVRSGQVVRVPGNLLIIGDVNPGGEVIAGGNIIVLGALRGIAHAGATGNKEAVIAALQLEPTQLRIADV 177

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308675216 144 ITRAPDgDYLSPDHPETARIKDGIVVIEVYQ 174
Cdd:PRK00513  178 IARAPE-DKEKPNYPEVAYIKDGGIVVERLQ 207
MinC COG0850
Septum site-determining protein MinC [Cell cycle control, cell division, chromosome ...
 67-175 1.30e-52

Septum site-determining protein MinC [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440611 [Multi-domain]  Cd Length: 223  Bit Score: 167.33  E-value: 1.30e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308675216  67 ENTILIKRTVRSGQSIQFDGNVVVLGDVNPGSEIVASGNIIVMGALRGVVHAGATGNKEATVSAFKLQPTQLRIANHITR 146
Cdd:COG0850   115 APTLVIRRPVRSGQQIYAPGDLVVLGDVNPGAEVIADGNIHVYGPLRGRAHAGASGNTEARIFALSLEPELLRIAGVYAR 194

                          90       100
                  ....*....|....*....|....*....
gi 1308675216 147 APDGDYLSPDHPETARIKDGIVVIEVYQL 175
Cdd:COG0850   195 AEDLPAELRGKPEQAYLEDGKIVIEPLSL 223
MinC_C pfam03775
Septum formation inhibitor MinC, C-terminal domain; In Escherichia coli Swiss:P06138 assembles ...
 71-170 6.02e-50

Septum formation inhibitor MinC, C-terminal domain; In Escherichia coli Swiss:P06138 assembles into a Z ring at midcell while assembly at polar sites is prevented by the min system. MinC, a component of this system, is an inhibitor of FtsZ assembly that is positioned within the cell by interaction with MinDE. MinC is an oligomer, probably a dimer. The C terminal half of MinC is the most conserved and interacts with MinD. The N terminal half is thought interact with FtsZ.


Pssm-ID: 461045  Cd Length: 101  Bit Score: 156.42  E-value: 6.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308675216  71 LIKRTVRSGQSIQFDGNVVVLGDVNPGSEIVASGNIIVMGALRGVVHAGATGNKEATVSAFKLQPTQLRIANHITRAPDG 150
Cdd:pfam03775   1 IVRGTLRSGQRIYAEGDLVILGDVNPGAEVIADGNIHVYGALRGRAHAGASGNTEARIFALSLEPEQLRIADYIARSPED 80

                          90       100
                  ....*....|....*....|.
gi 1308675216 151 DYLSP-DHPETARIKDGIVVI 170
Cdd:pfam03775  81 IPAELkGRPEIAQIEDDQIVI 101
minC TIGR01222
septum site-determining protein MinC; The minC protein assists in correct placement of the ...
 57-171 5.01e-29

septum site-determining protein MinC; The minC protein assists in correct placement of the septum for cell division by inhibiting septum formation at other sites. Homologs from Deinocoocus, Synechocystis PCC 6803, and Helicobacter pylori do not hit the full length of the model and score between the trusted and noise cutoffs. [Cellular processes, Cell division]


Pssm-ID: 273511 [Multi-domain]  Cd Length: 217  Bit Score: 106.72  E-value: 5.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308675216  57 KDPWQQAFVDENTILIKRTVRSGQSIQF-DGNVVVLGDVNPGSEIVASGNIIVMGALRGVVHAGATGNKEATVSAFKLQP 135
Cdd:TIGR01222 100 KNKKEATRVESTTKVIKTPVRSGQQIYAkHGDLIVLGNVNAGAEVLADGNIHVYGKLRGRALAGANGDTSAVIFALDLQA 179

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308675216 136 TQLRIANHITRAPDGDYLSPDHPETARIKDGIVVIE 171
Cdd:TIGR01222 180 ELISIAGRYKVSDDIERNFWGKPVQASLKGNRLVIE 215
 
Name Accession Description Interval E-value
minC PRK00513
septum formation inhibitor; Reviewed
 65-174 2.28e-54

septum formation inhibitor; Reviewed


Pssm-ID: 179052 [Multi-domain]  Cd Length: 214  Bit Score: 171.55  E-value: 2.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308675216  65 VDENTIL-IKRTVRSGQSIQFDGNVVVLGDVNPGSEIVASGNIIVMGALRGVVHAGATGNKEATVSAFKLQPTQLRIANH 143
Cdd:PRK00513   98 KEEGETKyLRKTVRSGQVVRVPGNLLIIGDVNPGGEVIAGGNIIVLGALRGIAHAGATGNKEAVIAALQLEPTQLRIADV 177

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308675216 144 ITRAPDgDYLSPDHPETARIKDGIVVIEVYQ 174
Cdd:PRK00513  178 IARAPE-DKEKPNYPEVAYIKDGGIVVERLQ 207
MinC COG0850
Septum site-determining protein MinC [Cell cycle control, cell division, chromosome ...
 67-175 1.30e-52

Septum site-determining protein MinC [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440611 [Multi-domain]  Cd Length: 223  Bit Score: 167.33  E-value: 1.30e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308675216  67 ENTILIKRTVRSGQSIQFDGNVVVLGDVNPGSEIVASGNIIVMGALRGVVHAGATGNKEATVSAFKLQPTQLRIANHITR 146
Cdd:COG0850   115 APTLVIRRPVRSGQQIYAPGDLVVLGDVNPGAEVIADGNIHVYGPLRGRAHAGASGNTEARIFALSLEPELLRIAGVYAR 194

                          90       100
                  ....*....|....*....|....*....
gi 1308675216 147 APDGDYLSPDHPETARIKDGIVVIEVYQL 175
Cdd:COG0850   195 AEDLPAELRGKPEQAYLEDGKIVIEPLSL 223
MinC_C pfam03775
Septum formation inhibitor MinC, C-terminal domain; In Escherichia coli Swiss:P06138 assembles ...
 71-170 6.02e-50

Septum formation inhibitor MinC, C-terminal domain; In Escherichia coli Swiss:P06138 assembles into a Z ring at midcell while assembly at polar sites is prevented by the min system. MinC, a component of this system, is an inhibitor of FtsZ assembly that is positioned within the cell by interaction with MinDE. MinC is an oligomer, probably a dimer. The C terminal half of MinC is the most conserved and interacts with MinD. The N terminal half is thought interact with FtsZ.


Pssm-ID: 461045  Cd Length: 101  Bit Score: 156.42  E-value: 6.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308675216  71 LIKRTVRSGQSIQFDGNVVVLGDVNPGSEIVASGNIIVMGALRGVVHAGATGNKEATVSAFKLQPTQLRIANHITRAPDG 150
Cdd:pfam03775   1 IVRGTLRSGQRIYAEGDLVILGDVNPGAEVIADGNIHVYGALRGRAHAGASGNTEARIFALSLEPEQLRIADYIARSPED 80

                          90       100
                  ....*....|....*....|.
gi 1308675216 151 DYLSP-DHPETARIKDGIVVI 170
Cdd:pfam03775  81 IPAELkGRPEIAQIEDDQIVI 101
minC TIGR01222
septum site-determining protein MinC; The minC protein assists in correct placement of the ...
 57-171 5.01e-29

septum site-determining protein MinC; The minC protein assists in correct placement of the septum for cell division by inhibiting septum formation at other sites. Homologs from Deinocoocus, Synechocystis PCC 6803, and Helicobacter pylori do not hit the full length of the model and score between the trusted and noise cutoffs. [Cellular processes, Cell division]


Pssm-ID: 273511 [Multi-domain]  Cd Length: 217  Bit Score: 106.72  E-value: 5.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308675216  57 KDPWQQAFVDENTILIKRTVRSGQSIQF-DGNVVVLGDVNPGSEIVASGNIIVMGALRGVVHAGATGNKEATVSAFKLQP 135
Cdd:TIGR01222 100 KNKKEATRVESTTKVIKTPVRSGQQIYAkHGDLIVLGNVNAGAEVLADGNIHVYGKLRGRALAGANGDTSAVIFALDLQA 179

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308675216 136 TQLRIANHITRAPDGDYLSPDHPETARIKDGIVVIE 171
Cdd:TIGR01222 180 ELISIAGRYKVSDDIERNFWGKPVQASLKGNRLVIE 215
minC PRK13992
septum site-determining protein MinC;
71-173 2.70e-19

septum site-determining protein MinC;


Pssm-ID: 237580 [Multi-domain]  Cd Length: 205  Bit Score: 80.93  E-value: 2.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308675216  71 LIKRTVRSGQSIQFDGNVVVLGDVNPGSEIVASGNIIVMGALRGVVHAGATGNKEATVSAFKLQPTQLRIANHITRapdg 150
Cdd:PRK13992  100 VIKKNLRSGQTVVHSGDVIVFGNVHKGAEILAGGSVVIFGKAQGIVRAGLNEGEQSVIAALSLQTSLIQISGFITQ---- 175

                          90       100
                  ....*....|....*....|...
gi 1308675216 151 DYLSPDHPETARIKDGIVVIEVY 173
Cdd:PRK13992  176 SKGEYNVPVIAHVKGGRIVIEPF 198
FapA COG1315
Flagellar assembly protein FapA, interacts with EIIAGlc [Cell motility];
82-130 8.54e-08

Flagellar assembly protein FapA, interacts with EIIAGlc [Cell motility];


Pssm-ID: 440926 [Multi-domain]  Cd Length: 401  Bit Score: 50.97  E-value: 8.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308675216  82 IQFDGNVVVLGDVNPGSEIVASGNIIVMGALRG---------VVHAGATGNKEATVSA 130
Cdd:COG1315   225 IDFDGSVIIKGDVLSGFSVKATGDIEVGGVVEGatieaggdiIIKGGIIGKGKGVIKA 282
minC PRK00556
septum formation inhibitor; Reviewed
 69-116 2.09e-07

septum formation inhibitor; Reviewed


Pssm-ID: 234791 [Multi-domain]  Cd Length: 194  Bit Score: 48.92  E-value: 2.09e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1308675216  69 TILIKRTVRSGQSIQFDGNVVVLGDVNPGSEIVASGNIIVMGALRGVV 116
Cdd:PRK00556   93 TTIYDRVIRSGEEIYSANDLIFLGRINNGAKIISEGNVSVYGECEGAI 140
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 76-130 2.78e-06

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 46.14  E-value: 2.78e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308675216  76 VRSGqSIQFDGNVVVLGDVNPGSEIVASGNIIVMGALRG---------VVHAGATGNKEATVSA 130
Cdd:pfam03961  11 LSTG-NIDFKGSVIIRGDVEEGMKVKASGDITVGGVVESatieaggdiTIKGGIIGRGKGKIKA 73
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 69-119 6.59e-04

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.21  E-value: 6.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308675216  69 TILIKRTVRSGQSIQFDGNVVVLGDVNpGSEIVASGNIIVM----GALRGVVHAG 119
Cdd:pfam03961  21 SVIIRGDVEEGMKVKASGDITVGGVVE-SATIEAGGDITIKggiiGRGKGKIKAG 74
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH