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Conserved domains on  [gi|1757562854|ref|XP_030959987|]
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uncharacterized protein LOC115981775 isoform X3 [Quercus lobata]

Protein Classification

remorin family protein( domain architecture ID 11145256)

remorin family protein similar to remorins which are plant-specific plasma membrane-associated proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 387-490 1.66e-49

Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.


:

Pssm-ID: 427493 [Multi-domain]  Cd Length: 106  Bit Score: 165.05  E-value: 1.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 387 ETRAAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMRKIEVEVERMRGQAHDRLMNKLAAARHKAEEKRAVAEAK 466
Cdd:pfam03763   3 ESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 1757562854 467 RNQEAAKTEQQSEYIRQTGRIPSS 490
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106
PHA03378 super family cl33729
EBNA-3B; Provisional
 251-320 5.39e-03

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 5.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757562854 251 QSATTFLPPPPTARSVSMRDMGTemtpiASQEPSRTGTPVRATTPMRSPTSSRP--STPGRAAPALSPTDPP 320
Cdd:PHA03378  718 AAATGRARPPAAAPGRARPPAAA-----PGRARPPAAAPGRARPPAAAPGRARPpaAAPGAPTPQPPPQAPP 784
 
Name Accession Description Interval E-value
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 387-490 1.66e-49

Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.


Pssm-ID: 427493 [Multi-domain]  Cd Length: 106  Bit Score: 165.05  E-value: 1.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 387 ETRAAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMRKIEVEVERMRGQAHDRLMNKLAAARHKAEEKRAVAEAK 466
Cdd:pfam03763   3 ESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 1757562854 467 RNQEAAKTEQQSEYIRQTGRIPSS 490
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106
PTZ00121 PTZ00121
MAEBL; Provisional
 362-479 1.84e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854  362 KEEEDKDASTSLKNITGEKPAKSVIETRAAAWEDAEKAKYTARFKR--EEMKIQAWENH--QKAKTEAEMRKIEVEVERM 437
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKkaEEAKKKAEEAKKADEAKKK 1478

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1757562854  438 RGQAH--DRLMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQSE 479
Cdd:PTZ00121  1479 AEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
350-484 9.88e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 9.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 350 QLGKMNIAAWASKEEEDKDASTSLKNItgeKPAKSVIETRAAAWEDAEKAKYTARFKREEMK--IQAWENHQK-AKTEAE 426
Cdd:COG4717    64 RKPELNLKELKELEEELKEAEEKEEEY---AELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQElEALEAE 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 427 MRKIEVEVERMRGQAHDR--LMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQSEYIRQT 484
Cdd:COG4717   141 LAELPERLEELEERLEELreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 380-475 2.07e-03

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: 38.19  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 380 KPAKSVIETR----AAAWEDAEKAKYTArfkrEEMKIQAWENHQKAKTEAEmrKIeveVERMRGQAHDRLMNKLAAARHK 455
Cdd:cd06503    22 KPILKALDEReekiAESLEEAEKAKEEA----EELLAEYEEKLAEARAEAQ--EI---IEEARKEAEKIKEEILAEAKEE 92

                          90       100
                  ....*....|....*....|..
gi 1757562854 456 AEE--KRAVAEAKRNQEAAKTE 475
Cdd:cd06503    93 AERilEQAKAEIEQEKEKALAE 114
PHA03378 PHA03378
EBNA-3B; Provisional
 251-320 5.39e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 5.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757562854 251 QSATTFLPPPPTARSVSMRDMGTemtpiASQEPSRTGTPVRATTPMRSPTSSRP--STPGRAAPALSPTDPP 320
Cdd:PHA03378  718 AAATGRARPPAAAPGRARPPAAA-----PGRARPPAAAPGRARPPAAAPGRARPpaAAPGAPTPQPPPQAPP 784
 
Name Accession Description Interval E-value
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 387-490 1.66e-49

Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.


Pssm-ID: 427493 [Multi-domain]  Cd Length: 106  Bit Score: 165.05  E-value: 1.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 387 ETRAAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMRKIEVEVERMRGQAHDRLMNKLAAARHKAEEKRAVAEAK 466
Cdd:pfam03763   3 ESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 1757562854 467 RNQEAAKTEQQSEYIRQTGRIPSS 490
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106
PTZ00121 PTZ00121
MAEBL; Provisional
 362-479 1.84e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854  362 KEEEDKDASTSLKNITGEKPAKSVIETRAAAWEDAEKAKYTARFKR--EEMKIQAWENH--QKAKTEAEMRKIEVEVERM 437
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKkaEEAKKKAEEAKKADEAKKK 1478

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1757562854  438 RGQAH--DRLMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQSE 479
Cdd:PTZ00121  1479 AEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
PTZ00121 PTZ00121
MAEBL; Provisional
 362-477 2.11e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854  362 KEEEDKDASTSLKNITGEKP-----AKSVIETRAAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMRKIEVEVER 436
Cdd:PTZ00121  1323 KAEEAKKKADAAKKKAEEAKkaaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1757562854  437 MRGQAHDrlMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQ 477
Cdd:PTZ00121  1403 DKKKADE--LKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
PTZ00121 PTZ00121
MAEBL; Provisional
 334-482 1.08e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854  334 KELQMKTRREIMVLGTQLGKMNiAAWASKEEEDKDASTSLKNITGEKpaKSVIETRAAAWEDAEKAKyTARFKREEMKIQ 413
Cdd:PTZ00121  1587 KKAEEARIEEVMKLYEEEKKMK-AEEAKKAEEAKIKAEELKKAEEEK--KKVEQLKKKEAEEKKKAE-ELKKAEEENKIK 1662

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1757562854  414 AWENHQKAKTEA----EMRKIEvEVERMRGQAhdrlMNKLAAARHKAEE-KRAVAEAKRNQEAAKTEQQSEYIR 482
Cdd:PTZ00121  1663 AAEEAKKAEEDKkkaeEAKKAE-EDEKKAAEA----LKKEAEEAKKAEElKKKEAEEKKKAEELKKAEEENKIK 1731
PTZ00121 PTZ00121
MAEBL; Provisional
 330-483 1.92e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854  330 ELSEKELQMKTRREIMVLGTQLGKmniAAWASKEEEDKDASTSLKNITGEKPAKSVIETRAAAWEDAEKAKYTARFKR-- 407
Cdd:PTZ00121  1409 ELKKAAAAKKKADEAKKKAEEKKK---ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKka 1485

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1757562854  408 EEMKIQAWENHQKAKteaEMRKIEvEVERMRGQAHDRLMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQ--QSEYIRQ 483
Cdd:PTZ00121  1486 DEAKKKAEEAKKKAD---EAKKAA-EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEELKK 1559
PTZ00121 PTZ00121
MAEBL; Provisional
 360-478 6.03e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 6.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854  360 ASKEEEDKDASTSLKNITgEKPAKSVIETRAAAWEDAEKAKYTARFKREEMKIQAWE----NHQKAKTEAEMRKIEVEV- 434
Cdd:PTZ00121  1569 AKKAEEDKNMALRKAEEA-KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEKk 1647

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1757562854  435 --ERMRGQAHDRLMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQS 478
Cdd:PTZ00121  1648 kaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
PTZ00121 PTZ00121
MAEBL; Provisional
 328-477 8.41e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 8.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854  328 KHELSEKELQMKTRREiMVLGTQLGKMNIAAWASKEEEDKDASTSLKNITGEKPAKSVIETRAaawEDAEKAKYTARFKR 407
Cdd:PTZ00121  1608 KAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK---AEEDKKKAEEAKKA 1683

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1757562854  408 EEMKIQAWENHQKAKTEA----EMRKIEVE----VERMRGQAHDRLMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQ 477
Cdd:PTZ00121  1684 EEDEKKAAEALKKEAEEAkkaeELKKKEAEekkkAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
350-484 9.88e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 9.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 350 QLGKMNIAAWASKEEEDKDASTSLKNItgeKPAKSVIETRAAAWEDAEKAKYTARFKREEMK--IQAWENHQK-AKTEAE 426
Cdd:COG4717    64 RKPELNLKELKELEEELKEAEEKEEEY---AELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQElEALEAE 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 427 MRKIEVEVERMRGQAHDR--LMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQSEYIRQT 484
Cdd:COG4717   141 LAELPERLEELEERLEELreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
386-480 1.03e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.40  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 386 IETRAAAWEDAEKAKYTARFKREEM--KIQAWENHQKAKTEAEmRKIEVEVERMRGQAHDRLMNKlAAARHKAEE----- 458
Cdd:COG2268   234 IETARIAEAEAELAKKKAEERREAEtaRAEAEAAYEIAEANAE-REVQRQLEIAEREREIELQEK-EAEREEAELeadvr 311

                          90       100
                  ....*....|....*....|..
gi 1757562854 459 KRAVAEAKRNQEAAKTEQQSEY 480
Cdd:COG2268   312 KPAEAEKQAAEAEAEAEAEAIR 333
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 380-467 1.07e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.77  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 380 KPAKSVIETRAAAWED----AEKAKYTArfkrEEMKIQAWENHQKAKTEAE------MRKIEVEVERMRGQAHDRLMNKL 449
Cdd:COG0711    23 PPILKALDERQEKIADglaeAERAKEEA----EAALAEYEEKLAEARAEAAeiiaeaRKEAEAIAEEAKAEAEAEAERII 98

                          90       100
                  ....*....|....*....|
gi 1757562854 450 AAARHK--AEEKRAVAEAKR 467
Cdd:COG0711    99 AQAEAEieQERAKALAELRA 118
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 380-475 2.07e-03

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: 38.19  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 380 KPAKSVIETR----AAAWEDAEKAKYTArfkrEEMKIQAWENHQKAKTEAEmrKIeveVERMRGQAHDRLMNKLAAARHK 455
Cdd:cd06503    22 KPILKALDEReekiAESLEEAEKAKEEA----EELLAEYEEKLAEARAEAQ--EI---IEEARKEAEKIKEEILAEAKEE 92

                          90       100
                  ....*....|....*....|..
gi 1757562854 456 AEE--KRAVAEAKRNQEAAKTE 475
Cdd:cd06503    93 AERilEQAKAEIEQEKEKALAE 114
PHA03378 PHA03378
EBNA-3B; Provisional
 251-320 5.39e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 5.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757562854 251 QSATTFLPPPPTARSVSMRDMGTemtpiASQEPSRTGTPVRATTPMRSPTSSRP--STPGRAAPALSPTDPP 320
Cdd:PHA03378  718 AAATGRARPPAAAPGRARPPAAA-----PGRARPPAAAPGRARPPAAAPGRARPpaAAPGAPTPQPPPQAPP 784
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
386-479 5.57e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.09  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 386 IETRAAAWEDAEKAkyTARFKREEMKIQAWENHQKAKTEAEmRKIEVEVERMRGQAHDRLMnKLAAARHKAEEKRAVAEA 465
Cdd:COG2268   191 RRKIAEIIRDARIA--EAEAERETEIAIAQANREAEEAELE-QEREIETARIAEAEAELAK-KKAEERREAETARAEAEA 266

                          90
                  ....*....|....
gi 1757562854 466 KRNQEAAKTEQQSE 479
Cdd:COG2268   267 AYEIAEANAEREVQ 280
PTZ00121 PTZ00121
MAEBL; Provisional
 360-476 7.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 7.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854  360 ASKEEEDKDASTSLKNITGEKPAKSVIETRAAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMRKIEvEVERMRG 439
Cdd:PTZ00121  1114 ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE-EVRKAEE 1192

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1757562854  440 QAHDRLMNKLAAARhKAEEKRAVAEAKRNQEAAKTEQ 476
Cdd:PTZ00121  1193 LRKAEDARKAEAAR-KAEEERKAEEARKAEDAKKAEA 1228
PHA03247 PHA03247
large tegument protein UL36; Provisional
 253-320 7.77e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 7.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1757562854  253 ATTFLPPPPTARSVSMRDMGTEMTPIASQEPSRTGTPVRATTPMRSPTSSRPSTPgrAAPALSPTDPP 320
Cdd:PHA03247  2715 LVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAP--APPAAPAAGPP 2780
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 383-479 8.64e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.63  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 383 KSVIETRAAAWEDAEKAKYTARFKREEMKiQAWENHQKAKTEAemrKIEVEVERMRGQAhdrlmnklAAARHKAE-EKRA 461
Cdd:PRK09510  104 KQLEKERLAAQEQKKQAEEAAKQAALKQK-QAEEAAAKAAAAA---KAKAEAEAKRAAA--------AAKKAAAEaKKKA 171

                          90
                  ....*....|....*....
gi 1757562854 462 VAEAKRNQEA-AKTEQQSE 479
Cdd:PRK09510  172 EAEAAKKAAAeAKKKAEAE 190
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 390-472 9.32e-03

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 36.52  E-value: 9.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562854 390 AAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMrKIEVEVERMRGQAHDRLmnklaaarhKAEEKRAVAEAkRNQ 469
Cdd:pfam00430  50 AAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVA-AAEAEAERIIEQAAAEI---------EQEKDRALAEL-RQQ 118


                  ...
gi 1757562854 470 EAA 472
Cdd:pfam00430 119 VVA 121
 
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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