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Conserved domains on  [gi|1757562850|ref|XP_030959985|]
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uncharacterized protein LOC115981775 isoform X1 [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. ...
 408-511 2.00e-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: 165.44  E-value: 2.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 408 ETRAAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMRKIEVEVERMRGQAHDRLMNKLAAARHKAEEKRAVAEAK 487
Cdd:pfam03763   3 ESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 1757562850 488 RNQEAAKTEQQSEYIRQTGRIPSS 511
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106
PHA03378 super family cl33729
EBNA-3B; Provisional
 272-341 5.71e-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: 5.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757562850 272 QSATTFLPPPPTARSVSMRDMGTemtpiASQEPSRTGTPVRATTPMRSPTSSRP--STPGRAAPALSPTDPP 341
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. ...
 408-511 2.00e-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: 165.44  E-value: 2.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 408 ETRAAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMRKIEVEVERMRGQAHDRLMNKLAAARHKAEEKRAVAEAK 487
Cdd:pfam03763   3 ESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 1757562850 488 RNQEAAKTEQQSEYIRQTGRIPSS 511
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106
PTZ00121 PTZ00121
MAEBL; Provisional
 383-500 1.60e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850  383 KEEEDKDASTSLKNITGEKPAKSVIETRAAAWEDAEKAKYTARFKR--EEMKIQAWENH--QKAKTEAEMRKIEVEVERM 458
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKkaEEAKKKAEEAKKADEAKKK 1478

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1757562850  459 RGQAH--DRLMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQSE 500
Cdd:PTZ00121  1479 AEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 401-488 8.20e-04

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: 40.16  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 401 KPAKSVIETRAAAWED----AEKAKYTArfkrEEMKIQAWENHQKAKTEAE------MRKIEVEVERMRGQAHDRLMNKL 470
Cdd:COG0711    23 PPILKALDERQEKIADglaeAERAKEEA----EAALAEYEEKLAEARAEAAeiiaeaRKEAEAIAEEAKAEAEAEAERII 98

                          90       100
                  ....*....|....*....|
gi 1757562850 471 AAARHK--AEEKRAVAEAKR 488
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 ...
 401-496 1.90e-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: 38.57  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 401 KPAKSVIETR----AAAWEDAEKAKYTArfkrEEMKIQAWENHQKAKTEAEmrKIeveVERMRGQAHDRLMNKLAAARHK 476
Cdd:cd06503    22 KPILKALDEReekiAESLEEAEKAKEEA----EELLAEYEEKLAEARAEAQ--EI---IEEARKEAEKIKEEILAEAKEE 92

                          90       100
                  ....*....|....*....|..
gi 1757562850 477 AEE--KRAVAEAKRNQEAAKTE 496
Cdd:cd06503    93 AERilEQAKAEIEQEKEKALAE 114
PHA03378 PHA03378
EBNA-3B; Provisional
 272-341 5.71e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 5.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757562850 272 QSATTFLPPPPTARSVSMRDMGTemtpiASQEPSRTGTPVRATTPMRSPTSSRP--STPGRAAPALSPTDPP 341
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. ...
 408-511 2.00e-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: 165.44  E-value: 2.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 408 ETRAAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMRKIEVEVERMRGQAHDRLMNKLAAARHKAEEKRAVAEAK 487
Cdd:pfam03763   3 ESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 1757562850 488 RNQEAAKTEQQSEYIRQTGRIPSS 511
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106
PTZ00121 PTZ00121
MAEBL; Provisional
 383-500 1.60e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850  383 KEEEDKDASTSLKNITGEKPAKSVIETRAAAWEDAEKAKYTARFKR--EEMKIQAWENH--QKAKTEAEMRKIEVEVERM 458
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKkaEEAKKKAEEAKKADEAKKK 1478

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1757562850  459 RGQAH--DRLMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQSE 500
Cdd:PTZ00121  1479 AEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
PTZ00121 PTZ00121
MAEBL; Provisional
 383-498 1.94e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850  383 KEEEDKDASTSLKNITGEKP-----AKSVIETRAAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMRKIEVEVER 457
Cdd:PTZ00121  1323 KAEEAKKKADAAKKKAEEAKkaaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1757562850  458 MRGQAHDrlMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQ 498
Cdd:PTZ00121  1403 DKKKADE--LKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
PTZ00121 PTZ00121
MAEBL; Provisional
 355-503 9.45e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 9.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850  355 KELQMKTRREIMVLGTQLGKMNiAAWASKEEEDKDASTSLKNitGEKPAKSVIETRAAAWEDAEKAKyTARFKREEMKIQ 434
Cdd:PTZ00121  1587 KKAEEARIEEVMKLYEEEKKMK-AEEAKKAEEAKIKAEELKK--AEEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENKIK 1662

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1757562850  435 AWENHQKAKTEA----EMRKIEvEVERMRGQAhdrlMNKLAAARHKAEE-KRAVAEAKRNQEAAKTEQQSEYIR 503
Cdd:PTZ00121  1663 AAEEAKKAEEDKkkaeEAKKAE-EDEKKAAEA----LKKEAEEAKKAEElKKKEAEEKKKAEELKKAEEENKIK 1731
PTZ00121 PTZ00121
MAEBL; Provisional
 351-504 1.56e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850  351 ELSEKELQMKTRREIMVLGTQLGKmniAAWASKEEEDKDASTSLKNITGEKPAKSVIETRAAAWEDAEKAKYTARFKR-- 428
Cdd:PTZ00121  1409 ELKKAAAAKKKADEAKKKAEEKKK---ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKka 1485

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1757562850  429 EEMKIQAWENHQKAKteaEMRKIEvEVERMRGQAHDRLMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQ--QSEYIRQ 504
Cdd:PTZ00121  1486 DEAKKKAEEAKKKAD---EAKKAA-EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEELKK 1559
PTZ00121 PTZ00121
MAEBL; Provisional
 381-499 5.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850  381 ASKEEEDKDASTSLKNITgEKPAKSVIETRAAAWEDAEKAKYTARFKREEMKIQAWE----NHQKAKTEAEMRKIEVEV- 455
Cdd:PTZ00121  1569 AKKAEEDKNMALRKAEEA-KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEKk 1647

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1757562850  456 --ERMRGQAHDRLMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQS 499
Cdd:PTZ00121  1648 kaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
PTZ00121 PTZ00121
MAEBL; Provisional
 349-498 7.59e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850  349 KHELSEKELQMKTRREiMVLGTQLGKMNIAAWASKEEEDKDASTSLKNITGEKPAKSVIETRAaawEDAEKAKYTARFKR 428
Cdd:PTZ00121  1608 KAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK---AEEDKKKAEEAKKA 1683

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1757562850  429 EEMKIQAWENHQKAKTEA----EMRKIEVE----VERMRGQAHDRLMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQ 498
Cdd:PTZ00121  1684 EEDEKKAAEALKKEAEEAkkaeELKKKEAEekkkAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 401-488 8.20e-04

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: 40.16  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 401 KPAKSVIETRAAAWED----AEKAKYTArfkrEEMKIQAWENHQKAKTEAE------MRKIEVEVERMRGQAHDRLMNKL 470
Cdd:COG0711    23 PPILKALDERQEKIADglaeAERAKEEA----EAALAEYEEKLAEARAEAAeiiaeaRKEAEAIAEEAKAEAEAEAERII 98

                          90       100
                  ....*....|....*....|
gi 1757562850 471 AAARHK--AEEKRAVAEAKR 488
Cdd:COG0711    99 AQAEAEieQERAKALAELRA 118
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
407-501 1.00e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.78  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 407 IETRAAAWEDAEKAKYTARFKREEM--KIQAWENHQKAKTEAEmRKIEVEVERMRGQAHDRLMNKlAAARHKAEE----- 479
Cdd:COG2268   234 IETARIAEAEAELAKKKAEERREAEtaRAEAEAAYEIAEANAE-REVQRQLEIAEREREIELQEK-EAEREEAELeadvr 311

                          90       100
                  ....*....|....*....|..
gi 1757562850 480 KRAVAEAKRNQEAAKTEQQSEY 501
Cdd:COG2268   312 KPAEAEKQAAEAEAEAEAEAIR 333
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
371-505 1.06e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 371 QLGKMNIAAWASKEEEDKDASTSLKNItgeKPAKSVIETRAAAWEDAEKAKYTARFKREEMK--IQAWENHQK-AKTEAE 447
Cdd:COG4717    64 RKPELNLKELKELEEELKEAEEKEEEY---AELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQElEALEAE 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 448 MRKIEVEVERMRGQAHDR--LMNKLAAARHKAEEKRAVAEAKRNQEAAKTEQQSEYIRQT 505
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 ...
 401-496 1.90e-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: 38.57  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 401 KPAKSVIETR----AAAWEDAEKAKYTArfkrEEMKIQAWENHQKAKTEAEmrKIeveVERMRGQAHDRLMNKLAAARHK 476
Cdd:cd06503    22 KPILKALDEReekiAESLEEAEKAKEEA----EELLAEYEEKLAEARAEAQ--EI---IEEARKEAEKIKEEILAEAKEE 92

                          90       100
                  ....*....|....*....|..
gi 1757562850 477 AEE--KRAVAEAKRNQEAAKTE 496
Cdd:cd06503    93 AERilEQAKAEIEQEKEKALAE 114
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
407-500 4.96e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.47  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 407 IETRAAAWEDAEKAkyTARFKREEMKIQAWENHQKAKTEAEmRKIEVEVERMRGQAHDRLMnKLAAARHKAEEKRAVAEA 486
Cdd:COG2268   191 RRKIAEIIRDARIA--EAEAERETEIAIAQANREAEEAELE-QEREIETARIAEAEAELAK-KKAEERREAETARAEAEA 266

                          90
                  ....*....|....
gi 1757562850 487 KRNQEAAKTEQQSE 500
Cdd:COG2268   267 AYEIAEANAEREVQ 280
PHA03378 PHA03378
EBNA-3B; Provisional
 272-341 5.71e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 5.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757562850 272 QSATTFLPPPPTARSVSMRDMGTemtpiASQEPSRTGTPVRATTPMRSPTSSRP--STPGRAAPALSPTDPP 341
Cdd:PHA03378  718 AAATGRARPPAAAPGRARPPAAA-----PGRARPPAAAPGRARPPAAAPGRARPpaAAPGAPTPQPPPQAPP 784
PTZ00121 PTZ00121
MAEBL; Provisional
 381-497 7.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 7.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850  381 ASKEEEDKDASTSLKNITGEKPAKSVIETRAAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMRKIEvEVERMRG 460
Cdd:PTZ00121  1114 ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE-EVRKAEE 1192

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1757562850  461 QAHDRLMNKLAAARhKAEEKRAVAEAKRNQEAAKTEQ 497
Cdd:PTZ00121  1193 LRKAEDARKAEAAR-KAEEERKAEEARKAEDAKKAEA 1228
PHA03247 PHA03247
large tegument protein UL36; Provisional
 274-341 7.95e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 7.95e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1757562850  274 ATTFLPPPPTARSVSMRDMGTEMTPIASQEPSRTGTPVRATTPMRSPTSSRPSTPgrAAPALSPTDPP 341
Cdd:PHA03247  2715 LVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAP--APPAAPAAGPP 2780
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 ...
 411-493 8.15e-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: 36.91  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 411 AAAWEDAEKAKYTARFKREEMKIQAWENHQKAKTEAEMrKIEVEVERMRGQAHDRLmnklaaarhKAEEKRAVAEAkRNQ 490
Cdd:pfam00430  50 AAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVA-AAEAEAERIIEQAAAEI---------EQEKDRALAEL-RQQ 118


                  ...
gi 1757562850 491 EAA 493
Cdd:pfam00430 119 VVA 121
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 404-500 8.83e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.63  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757562850 404 KSVIETRAAAWEDAEKAKYTARFKREEMKiQAWENHQKAKTEAemrKIEVEVERMRGQAhdrlmnklAAARHKAE-EKRA 482
Cdd:PRK09510  104 KQLEKERLAAQEQKKQAEEAAKQAALKQK-QAEEAAAKAAAAA---KAKAEAEAKRAAA--------AAKKAAAEaKKKA 171

                          90
                  ....*....|....*....
gi 1757562850 483 VAEAKRNQEA-AKTEQQSE 500
Cdd:PRK09510  172 EAEAAKKAAAeAKKKAEAE 190
 
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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