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Conserved domains on  [gi|1167803157|ref|NP_001336672|]
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transmembrane and coiled-coil domain-containing protein 3 isoform 4 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KefB COG0475
Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism]; ...
 209-283 1.52e-17

Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism];


:

Pssm-ID: 440243 [Multi-domain]  Cd Length: 384  Bit Score: 84.43  E-value: 1.52e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167803157 209 DIVTIGMLSLPCGWLCTAIGLPTMFGYIICGVLLGPSGLNSIKSIVQVETLGEFGVFFTLFLVGLEFSPEKLRKH 283
Cdd:COG0475     8 QLGLLLLAAVLAGLLARRLGLPSVLGYILAGILLGPSGLGLIEDSEALELLAELGVVLLLFLIGLELDLKRLRKM 82
ATP-synt_Fo_b super family cl21478
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 133-213 6.96e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


The actual alignment was detected with superfamily member cd06503:

Pssm-ID: 473877 [Multi-domain]  Cd Length: 132  Bit Score: 39.73  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157 133 ESSRQRLEALREAAIKEETEYMELLAAEKHQVEALKNmQHQNQSLSMLDEILEDVRKAADRL----EEEIE---EHAFDD 205
Cdd:cd06503    36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIE-EARKEAEKIKEEILAEAKEEAERIleqaKAEIEqekEKALAE 114


                  ....*...
gi 1167803157 206 NKSDIVTI 213
Cdd:cd06503   115 LRKEVADL 122
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-201 1.36e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157  50 VRDSCRKLSGLLRQknAVLNKLKTAIGAVEKDVGLSDEEKLFQVHT-FEIFQK---ELNESENSVFQAVYGLQRALQGDY 125
Cdd:COG4717   349 LQELLREAEELEEE--LQLEELEQEIAALLAEAGVEDEEELRAALEqAEEYQElkeELEELEEQLEELLGELEELLEALD 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157 126 KDVVNMK--------ESSRQRLEALRE--AAIKEE-------TEYMELLAAEKHQVEALKNMQHQNQSLSMLDEILEDVR 188
Cdd:COG4717   427 EEELEEEleeleeelEELEEELEELREelAELEAEleqleedGELAELLQELEELKAELRELAEEWAALKLALELLEEAR 506

                         170
                  ....*....|....*...
gi 1167803157 189 KAA-----DRLEEEIEEH 201
Cdd:COG4717   507 EEYreerlPPVLERASEY 524
 
Name Accession Description Interval E-value
KefB COG0475
Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism]; ...
 209-283 1.52e-17

Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism];


Pssm-ID: 440243 [Multi-domain]  Cd Length: 384  Bit Score: 84.43  E-value: 1.52e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167803157 209 DIVTIGMLSLPCGWLCTAIGLPTMFGYIICGVLLGPSGLNSIKSIVQVETLGEFGVFFTLFLVGLEFSPEKLRKH 283
Cdd:COG0475     8 QLGLLLLAAVLAGLLARRLGLPSVLGYILAGILLGPSGLGLIEDSEALELLAELGVVLLLFLIGLELDLKRLRKM 82
Na_H_Exchanger pfam00999
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH ...
 210-309 2.98e-16

Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family.


Pssm-ID: 425982 [Multi-domain]  Cd Length: 377  Bit Score: 80.38  E-value: 2.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157 210 IVTIGMLSLPCGWLCTAIGLPTMFGYIICGVLLGPSGLNSIKSI-VQVETLGEFGVFFTLFLVGLEFSPEKLRKHcRGSS 288
Cdd:pfam00999   1 IVLLILLALLAPLLARRLKLPPIVGLIIAGILLGPSGLGLISEVdEDLEVLSNLGLPPLLFLAGLELDLRELRKN-GGSI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1167803157 289 ---------------------PNPGFDWSDSFFTSGGFSFMS 309
Cdd:pfam00999  80 lllallgvlipfvliglllylLGLGIPLLEALLFGAILSATS 121
2a37 TIGR00932
transporter, monovalent cation:proton antiporter-2 (CPA2) family; [Transport and binding ...
 220-283 8.45e-12

transporter, monovalent cation:proton antiporter-2 (CPA2) family; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273348 [Multi-domain]  Cd Length: 273  Bit Score: 65.75  E-value: 8.45e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167803157 220 CGWLCTAIGLPTMFGYIICGVLLGPSGLNSIKSIVQVETLGEFGVFFTLFLVGLEFSPEKLRKH 283
Cdd:TIGR00932   7 AVPLSRRLGIPSVLGYLLAGVLIGPSGLGLISNVEGVNHLAEFGVILLMFLIGLELDLERLWKL 70
PRK03659 PRK03659
glutathione-regulated potassium-efflux system protein KefB; Provisional
 228-280 1.70e-07

glutathione-regulated potassium-efflux system protein KefB; Provisional


Pssm-ID: 179625 [Multi-domain]  Cd Length: 601  Bit Score: 53.88  E-value: 1.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1167803157 228 GLPTMFGYIICGVLLGPSGLNSIKSIVQVETLGEFGVFFTLFLVGLEFSPEKL 280
Cdd:PRK03659   28 GIGAVLGYLLAGIAIGPWGLGFISDVDEILHFSELGVVFLMFIIGLELNPSKL 80
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 133-213 6.96e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.73  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157 133 ESSRQRLEALREAAIKEETEYMELLAAEKHQVEALKNmQHQNQSLSMLDEILEDVRKAADRL----EEEIE---EHAFDD 205
Cdd:cd06503    36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIE-EARKEAEKIKEEILAEAKEEAERIleqaKAEIEqekEKALAE 114


                  ....*...
gi 1167803157 206 NKSDIVTI 213
Cdd:cd06503   115 LRKEVADL 122
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-201 1.36e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157  50 VRDSCRKLSGLLRQknAVLNKLKTAIGAVEKDVGLSDEEKLFQVHT-FEIFQK---ELNESENSVFQAVYGLQRALQGDY 125
Cdd:COG4717   349 LQELLREAEELEEE--LQLEELEQEIAALLAEAGVEDEEELRAALEqAEEYQElkeELEELEEQLEELLGELEELLEALD 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157 126 KDVVNMK--------ESSRQRLEALRE--AAIKEE-------TEYMELLAAEKHQVEALKNMQHQNQSLSMLDEILEDVR 188
Cdd:COG4717   427 EEELEEEleeleeelEELEEELEELREelAELEAEleqleedGELAELLQELEELKAELRELAEEWAALKLALELLEEAR 506

                         170
                  ....*....|....*...
gi 1167803157 189 KAA-----DRLEEEIEEH 201
Cdd:COG4717   507 EEYreerlPPVLERASEY 524
Com_YlbF pfam06133
Control of competence regulator ComK, YlbF/YmcA; YlbF Is a family of short Gram-positive and ...
 144-201 6.01e-03

Control of competence regulator ComK, YlbF/YmcA; YlbF Is a family of short Gram-positive and archaeal proteins that includes both YlbF and YmcA which may interact synergistically. The family is necessary for correct biofilm formation, as null mutants of ymcA and ylbF fail to form pellicles at air-liquid interfaces and grow on solid media as smooth, undifferentiated colonies. During development, YmcA, YlbF and YaaT, family PSPI, pfam04468, interact directly with one another forming a stable ternary complex, in vitro. All three proteins are required for competence, sporulation and the formation of biofilms. The YmcA-YlbF-YaaT complex affects the phosphotransfer between Spo0F and Spo0B, thus accelerating the production of Spo0A~P. The three processes of biofilm formation, mature spore formation and competence all require the active, phosphorylated form of Spo0A, as Spo0A-P.


Pssm-ID: 428784 [Multi-domain]  Cd Length: 103  Bit Score: 36.36  E-value: 6.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803157 144 EAAIKEETEYMELLAAEKhQVEA-------LKNMQHQNQSLSML----DEILEDVRKAADRLEEEIEEH 201
Cdd:pfam06133   7 AKAIKESEEYKRYKEAEE-ALEAdeeaqklIKEFRKLQEELQEKqmqgEELTEEEKQELQELYEELDQN 74
 
Name Accession Description Interval E-value
KefB COG0475
Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism]; ...
 209-283 1.52e-17

Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism];


Pssm-ID: 440243 [Multi-domain]  Cd Length: 384  Bit Score: 84.43  E-value: 1.52e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167803157 209 DIVTIGMLSLPCGWLCTAIGLPTMFGYIICGVLLGPSGLNSIKSIVQVETLGEFGVFFTLFLVGLEFSPEKLRKH 283
Cdd:COG0475     8 QLGLLLLAAVLAGLLARRLGLPSVLGYILAGILLGPSGLGLIEDSEALELLAELGVVLLLFLIGLELDLKRLRKM 82
Na_H_Exchanger pfam00999
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH ...
 210-309 2.98e-16

Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family.


Pssm-ID: 425982 [Multi-domain]  Cd Length: 377  Bit Score: 80.38  E-value: 2.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157 210 IVTIGMLSLPCGWLCTAIGLPTMFGYIICGVLLGPSGLNSIKSI-VQVETLGEFGVFFTLFLVGLEFSPEKLRKHcRGSS 288
Cdd:pfam00999   1 IVLLILLALLAPLLARRLKLPPIVGLIIAGILLGPSGLGLISEVdEDLEVLSNLGLPPLLFLAGLELDLRELRKN-GGSI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1167803157 289 ---------------------PNPGFDWSDSFFTSGGFSFMS 309
Cdd:pfam00999  80 lllallgvlipfvliglllylLGLGIPLLEALLFGAILSATS 121
2a37 TIGR00932
transporter, monovalent cation:proton antiporter-2 (CPA2) family; [Transport and binding ...
 220-283 8.45e-12

transporter, monovalent cation:proton antiporter-2 (CPA2) family; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273348 [Multi-domain]  Cd Length: 273  Bit Score: 65.75  E-value: 8.45e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167803157 220 CGWLCTAIGLPTMFGYIICGVLLGPSGLNSIKSIVQVETLGEFGVFFTLFLVGLEFSPEKLRKH 283
Cdd:TIGR00932   7 AVPLSRRLGIPSVLGYLLAGVLIGPSGLGLISNVEGVNHLAEFGVILLMFLIGLELDLERLWKL 70
PRK03659 PRK03659
glutathione-regulated potassium-efflux system protein KefB; Provisional
 228-280 1.70e-07

glutathione-regulated potassium-efflux system protein KefB; Provisional


Pssm-ID: 179625 [Multi-domain]  Cd Length: 601  Bit Score: 53.88  E-value: 1.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1167803157 228 GLPTMFGYIICGVLLGPSGLNSIKSIVQVETLGEFGVFFTLFLVGLEFSPEKL 280
Cdd:PRK03659   28 GIGAVLGYLLAGIAIGPWGLGFISDVDEILHFSELGVVFLMFIIGLELNPSKL 80
PRK03562 PRK03562
glutathione-regulated potassium-efflux system protein KefC; Provisional
 226-280 5.11e-06

glutathione-regulated potassium-efflux system protein KefC; Provisional


Pssm-ID: 235131 [Multi-domain]  Cd Length: 621  Bit Score: 49.22  E-value: 5.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1167803157 226 AIGLPTMFGYIICGVLLGPSGLNSIKSIVQVETLGEFGVFFTLFLVGLEFSPEKL 280
Cdd:PRK03562   26 RLGLGSVLGYLIAGCIIGPWGLRLVTDVESILHFAEFGVVLMLFVIGLELDPQRL 80
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 133-213 6.96e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.73  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157 133 ESSRQRLEALREAAIKEETEYMELLAAEKHQVEALKNmQHQNQSLSMLDEILEDVRKAADRL----EEEIE---EHAFDD 205
Cdd:cd06503    36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIE-EARKEAEKIKEEILAEAKEEAERIleqaKAEIEqekEKALAE 114


                  ....*...
gi 1167803157 206 NKSDIVTI 213
Cdd:cd06503   115 LRKEVADL 122
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-201 1.36e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157  50 VRDSCRKLSGLLRQknAVLNKLKTAIGAVEKDVGLSDEEKLFQVHT-FEIFQK---ELNESENSVFQAVYGLQRALQGDY 125
Cdd:COG4717   349 LQELLREAEELEEE--LQLEELEQEIAALLAEAGVEDEEELRAALEqAEEYQElkeELEELEEQLEELLGELEELLEALD 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157 126 KDVVNMK--------ESSRQRLEALRE--AAIKEE-------TEYMELLAAEKHQVEALKNMQHQNQSLSMLDEILEDVR 188
Cdd:COG4717   427 EEELEEEleeleeelEELEEELEELREelAELEAEleqleedGELAELLQELEELKAELRELAEEWAALKLALELLEEAR 506

                         170
                  ....*....|....*...
gi 1167803157 189 KAA-----DRLEEEIEEH 201
Cdd:COG4717   507 EEYreerlPPVLERASEY 524
NhaP COG0025
NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism];
210-283 1.42e-03

NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism];


Pssm-ID: 439796 [Multi-domain]  Cd Length: 506  Bit Score: 41.10  E-value: 1.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167803157 210 IVTIGMLSLPCGWLCTAIGLPTMFGYIICGVLLGPsGLNSI--KSIVQVETLGEFGVFFTLFLVGLEFSPEKLRKH 283
Cdd:COG0025     7 ILLLLLLGLLSQWLARRLKLPAPLLLLLAGILLGP-GLGLEldPELGDLEPLLELFLPPLLFEAALNLDLRELRRN 81
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
18-200 1.85e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157  18 WAVQAVEHEEVAQRVIKLHRGRGV-------------AAMQSRQWVRDSCRKLSGLLRQKNAVLNKLKTAIGAVEKDvgL 84
Cdd:COG4717    41 AFIRAMLLERLEKEADELFKPQGRkpelnlkelkeleEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE--L 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803157  85 SDEEKLFQVHTFEIFQKELNESENSVFQAVYGLQRALQgDYKDVVNMKESSRQRLEALREAAikEETEYMELLAAEKHQV 164
Cdd:COG4717   119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEEL--EELLEQLSLATEEELQ 195

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1167803157 165 EALKNMQHQNQSLSMLDEILEDVRKAADRLEEEIEE 200
Cdd:COG4717   196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
PLN03159 PLN03159
cation/H(+) antiporter 15; Provisional
 230-282 4.37e-03

cation/H(+) antiporter 15; Provisional


Pssm-ID: 215608 [Multi-domain]  Cd Length: 832  Bit Score: 39.87  E-value: 4.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167803157 230 PTMFGYIICGVLLGPSGLNSIK----------SIVQVETLGEFGVFFTLFLVGLEFSPEKLRK 282
Cdd:PLN03159   68 PRVISEILGGVILGPSVLGQSEvfantifplrSVMVLETMANLGLLYFLFLVGVEMDISVIRR 130
Com_YlbF pfam06133
Control of competence regulator ComK, YlbF/YmcA; YlbF Is a family of short Gram-positive and ...
 144-201 6.01e-03

Control of competence regulator ComK, YlbF/YmcA; YlbF Is a family of short Gram-positive and archaeal proteins that includes both YlbF and YmcA which may interact synergistically. The family is necessary for correct biofilm formation, as null mutants of ymcA and ylbF fail to form pellicles at air-liquid interfaces and grow on solid media as smooth, undifferentiated colonies. During development, YmcA, YlbF and YaaT, family PSPI, pfam04468, interact directly with one another forming a stable ternary complex, in vitro. All three proteins are required for competence, sporulation and the formation of biofilms. The YmcA-YlbF-YaaT complex affects the phosphotransfer between Spo0F and Spo0B, thus accelerating the production of Spo0A~P. The three processes of biofilm formation, mature spore formation and competence all require the active, phosphorylated form of Spo0A, as Spo0A-P.


Pssm-ID: 428784 [Multi-domain]  Cd Length: 103  Bit Score: 36.36  E-value: 6.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803157 144 EAAIKEETEYMELLAAEKhQVEA-------LKNMQHQNQSLSML----DEILEDVRKAADRLEEEIEEH 201
Cdd:pfam06133   7 AKAIKESEEYKRYKEAEE-ALEAdeeaqklIKEFRKLQEELQEKqmqgEELTEEEKQELQELYEELDQN 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.
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