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Conserved domains on  [gi|973062926|gb|KUK34484|]
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DivIVA family protein [Caldanaerobacter subterraneus]

Protein Classification

DivIVA domain-containing protein( domain architecture ID 12060610)

DivIVA domain-containing protein similar to Bacillus subtilis septum site-determining protein DivIVA, which may act as a pilot protein, directing MinCD to the polar septation sites or by inhibiting MinCD at the midcell site of division

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 2-132 3.20e-50

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


:

Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 157.34  E-value: 3.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973062926    2 LTPMDIHNKEFRRSFRGYNEEEVDEFLDKIMEDYEMLYKENAELKDRINIMNEKLQSYINMENTLNNTLIVAQNTAEELK 81
Cdd:pfam05103   1 LTPLDIQNKEFKKKMRGYDPDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLILAQETAEEVK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 973062926   82 RNAEKEAQLIIQNAQQNAEKILEKANQEVVRIRMELERYRKQLNVFKAKFK 132
Cdd:pfam05103  81 ANAQKEAELIIKEAEAKAERIVDDANNEVKKINDEIEELKRQRRQFRTRFK 131
 
Name Accession Description Interval E-value
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 2-132 3.20e-50

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 157.34  E-value: 3.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973062926    2 LTPMDIHNKEFRRSFRGYNEEEVDEFLDKIMEDYEMLYKENAELKDRINIMNEKLQSYINMENTLNNTLIVAQNTAEELK 81
Cdd:pfam05103   1 LTPLDIQNKEFKKKMRGYDPDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLILAQETAEEVK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 973062926   82 RNAEKEAQLIIQNAQQNAEKILEKANQEVVRIRMELERYRKQLNVFKAKFK 132
Cdd:pfam05103  81 ANAQKEAELIIKEAEAKAERIVDDANNEVKKINDEIEELKRQRRQFRTRFK 131
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 1-123 2.36e-43

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 139.61  E-value: 2.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973062926   1 MLTPMDIHNKEFRRSFRGYNEEEVDEFLDKIMEDYEMLYKENAELKDRINIMNEKLQSYINMENTLNNTLIVAQNTAEEL 80
Cdd:COG3599    2 KLTPLDIRNKEFKKGFRGYDEDEVDEFLDEVAEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLVVAQETAEEV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 973062926  81 KRNAEKEAQLIIQNAQQNAEKILEKANQEVVRIRMELERYRKQ 123
Cdd:COG3599   82 KENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIEELKRQ 124
DivI1A_domain TIGR03544
DivIVA domain; This model describes a domain found in Bacillus subtilis cell division ...
 2-35 3.44e-15

DivIVA domain; This model describes a domain found in Bacillus subtilis cell division initiation protein DivIVA, and homologs, toward the N-terminus. It is also found as a repeated domain in certain other proteins, including family TIGR03543.


Pssm-ID: 274639 [Multi-domain]  Cd Length: 34  Bit Score: 65.14  E-value: 3.44e-15
                          10        20        30
                  ....*....|....*....|....*....|....
gi 973062926    2 LTPMDIHNKEFRRSFRGYNEEEVDEFLDKIMEDY 35
Cdd:TIGR03544   1 LTPEDIRNKRFKKKLRGYDAAEVDAFLDRVADDL 34
PRK14127 PRK14127
cell division regulator GpsB;
2-87 4.11e-12

cell division regulator GpsB;


Pssm-ID: 237616 [Multi-domain]  Cd Length: 109  Bit Score: 59.26  E-value: 4.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973062926   2 LTPMDIHNKEFRRSFRGYNEEEVDEFLDKIMEDYEM-------LYKENAELKDRINIMNEKLQSYINMENTLNNTLIVAQ 74
Cdd:PRK14127   6 LTPKDILEKEFKTSMRGYDQDEVDKFLDDVIKDYEAfqkeieeLQQENARLKAQVDELTKQVSVGASSSSVATTQPSSSA 85

                         90
                 ....*....|....*
gi 973062926  75 NTAEELKR--NAEKE 87
Cdd:PRK14127  86 TNYDILKRlsNLEKH 100
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 73-144 7.12e-03

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 35.57  E-value: 7.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973062926  73 AQNTAEELKRNAEKEAQLIIQNAQQNAEKILEKAN---QEVV--------RIRMELERYRKQLNVFkaKFKSLLEAqLES 141
Cdd:cd03404  182 ARQDKERLINEAQAYANEVIPRARGEAARIIQEAEaykAEVVaraegdaaRFLALLAEYRKAPEVT--RERLYLET-MEE 258


                 ...
gi 973062926 142 ILS 144
Cdd:cd03404  259 VLS 261
 
Name Accession Description Interval E-value
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 2-132 3.20e-50

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 157.34  E-value: 3.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973062926    2 LTPMDIHNKEFRRSFRGYNEEEVDEFLDKIMEDYEMLYKENAELKDRINIMNEKLQSYINMENTLNNTLIVAQNTAEELK 81
Cdd:pfam05103   1 LTPLDIQNKEFKKKMRGYDPDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLILAQETAEEVK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 973062926   82 RNAEKEAQLIIQNAQQNAEKILEKANQEVVRIRMELERYRKQLNVFKAKFK 132
Cdd:pfam05103  81 ANAQKEAELIIKEAEAKAERIVDDANNEVKKINDEIEELKRQRRQFRTRFK 131
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 1-123 2.36e-43

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 139.61  E-value: 2.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973062926   1 MLTPMDIHNKEFRRSFRGYNEEEVDEFLDKIMEDYEMLYKENAELKDRINIMNEKLQSYINMENTLNNTLIVAQNTAEEL 80
Cdd:COG3599    2 KLTPLDIRNKEFKKGFRGYDEDEVDEFLDEVAEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLVVAQETAEEV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 973062926  81 KRNAEKEAQLIIQNAQQNAEKILEKANQEVVRIRMELERYRKQ 123
Cdd:COG3599   82 KENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIEELKRQ 124
DivI1A_domain TIGR03544
DivIVA domain; This model describes a domain found in Bacillus subtilis cell division ...
 2-35 3.44e-15

DivIVA domain; This model describes a domain found in Bacillus subtilis cell division initiation protein DivIVA, and homologs, toward the N-terminus. It is also found as a repeated domain in certain other proteins, including family TIGR03543.


Pssm-ID: 274639 [Multi-domain]  Cd Length: 34  Bit Score: 65.14  E-value: 3.44e-15
                          10        20        30
                  ....*....|....*....|....*....|....
gi 973062926    2 LTPMDIHNKEFRRSFRGYNEEEVDEFLDKIMEDY 35
Cdd:TIGR03544   1 LTPEDIRNKRFKKKLRGYDAAEVDAFLDRVADDL 34
PRK14127 PRK14127
cell division regulator GpsB;
2-87 4.11e-12

cell division regulator GpsB;


Pssm-ID: 237616 [Multi-domain]  Cd Length: 109  Bit Score: 59.26  E-value: 4.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973062926   2 LTPMDIHNKEFRRSFRGYNEEEVDEFLDKIMEDYEM-------LYKENAELKDRINIMNEKLQSYINMENTLNNTLIVAQ 74
Cdd:PRK14127   6 LTPKDILEKEFKTSMRGYDQDEVDKFLDDVIKDYEAfqkeieeLQQENARLKAQVDELTKQVSVGASSSSVATTQPSSSA 85

                         90
                 ....*....|....*
gi 973062926  75 NTAEELKR--NAEKE 87
Cdd:PRK14127  86 TNYDILKRlsNLEKH 100
PRK12704 PRK12704
phosphodiesterase; Provisional
 72-157 1.99e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.45  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973062926  72 VAQNTAEELKRNAEKEAQLIIQNAQQNAEKILEK----ANQEVVRIRMELER-YRKQLNVFKAKFKSLLeaQLESILSiD 146
Cdd:PRK12704  24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEalleAKEEIHKLRNEFEKeLRERRNELQKLEKRLL--QKEENLD-R 100

                         90
                 ....*....|.
gi 973062926 147 EKELIPDEDEE 157
Cdd:PRK12704 101 KLELLEKREEE 111
PRK01005 PRK01005
V-type ATP synthase subunit E; Provisional
 69-110 2.88e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179204 [Multi-domain]  Cd Length: 207  Bit Score: 36.69  E-value: 2.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 973062926  69 TLIVAQNTAEELKRNAEKEAQLIIQNAQQNAEKILEKANQEV 110
Cdd:PRK01005  21 TLKPAEEEAGAIVHNAKEQAKRIIAEAQEEAEKIIRSAEETA 62
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 73-144 7.12e-03

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 35.57  E-value: 7.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973062926  73 AQNTAEELKRNAEKEAQLIIQNAQQNAEKILEKAN---QEVV--------RIRMELERYRKQLNVFkaKFKSLLEAqLES 141
Cdd:cd03404  182 ARQDKERLINEAQAYANEVIPRARGEAARIIQEAEaykAEVVaraegdaaRFLALLAEYRKAPEVT--RERLYLET-MEE 258


                 ...
gi 973062926 142 ILS 144
Cdd:cd03404  259 VLS 261
 
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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