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Conserved domains on  [gi|1632238227|ref|XP_028947245|]
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uncharacterized protein LOC103430609 isoform X1 [Malus domestica]

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. ...
 407-510 3.53e-50

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: 167.36  E-value: 3.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227 407 ETRAAAWEESEKAKYMARFKREEMKIQAWENHQKAKTEAEMRKIEVEVERIRGRAHGKLMNKLAAARHKAQEKRTAAEAK 486
Cdd:pfam03763   3 ESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 1632238227 487 RNRQAAKAEHQAEYIRKTGRIPSS 510
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106
 
Name Accession Description Interval E-value
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 407-510 3.53e-50

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: 167.36  E-value: 3.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227 407 ETRAAAWEESEKAKYMARFKREEMKIQAWENHQKAKTEAEMRKIEVEVERIRGRAHGKLMNKLAAARHKAQEKRTAAEAK 486
Cdd:pfam03763   3 ESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 1632238227 487 RNRQAAKAEHQAEYIRKTGRIPSS 510
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
383-505 1.37e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.56  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227 383 KEEDKDASASQKTVleeqpgtsvIETRAAAWEESEKAKYMARFKREEM--KIQAWENHQKAKTEAEmRKIEVEVERIRGR 460
Cdd:COG2268   220 NREAEEAELEQERE---------IETARIAEAEAELAKKKAEERREAEtaRAEAEAAYEIAEANAE-REVQRQLEIAERE 289

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1632238227 461 AHGKLMNKlAAARHKAQEKRT---AAEAKRNRQAAKAEHQAEYIRKTG 505
Cdd:COG2268   290 REIELQEK-EAEREEAELEADvrkPAEAEKQAAEAEAEAEAEAIRAKG 336
PTZ00121 PTZ00121
MAEBL; Provisional
 345-503 4.20e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 4.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227  345 DQNTNKELSEKELQLKTRREIMVLGTQLGKMNIAAWASKEEDKDASASQKTvlEEQPGTSVIETRAAAWEESEKAKYMAR 424
Cdd:PTZ00121  1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAEEAKKADEAKKKAE 1480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227  425 FKR--EEMKIQAWENHQKAKteaEMRKIEVEVERIRGRAHGKLMNKLAAARhKAQEKRTAAEAKRNRQAAKAEH--QAEY 500
Cdd:PTZ00121  1481 EAKkaDEAKKKAEEAKKKAD---EAKKAAEAKKKADEAKKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADElkKAEE 1556


                   ...
gi 1632238227  501 IRK 503
Cdd:PTZ00121  1557 LKK 1559
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 383-503 1.33e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227 383 KEEDKDASASQKTVLEEQPGTSVIETRAAAWEESEKAKYMARFKREEMKiQAWENHQKAKTEAEmRKIEVEVER------ 456
Cdd:TIGR02794  71 KKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQK-QAEEAKAKQAAEAK-AKAEAEAERkakeea 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1632238227 457 IRGRAHGKLMNKLAAARHKAQE-----------------KRTAAEAKRNRQAAKAEHQAEYIRK 503
Cdd:TIGR02794 149 AKQAEEEAKAKAAAEAKKKAEEakkkaeaeakakaeaeaKAKAEEAKAKAEAAKAKAAAEAAAK 212
 
Name Accession Description Interval E-value
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 407-510 3.53e-50

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: 167.36  E-value: 3.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227 407 ETRAAAWEESEKAKYMARFKREEMKIQAWENHQKAKTEAEMRKIEVEVERIRGRAHGKLMNKLAAARHKAQEKRTAAEAK 486
Cdd:pfam03763   3 ESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 1632238227 487 RNRQAAKAEHQAEYIRKTGRIPSS 510
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
383-505 1.37e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.56  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227 383 KEEDKDASASQKTVleeqpgtsvIETRAAAWEESEKAKYMARFKREEM--KIQAWENHQKAKTEAEmRKIEVEVERIRGR 460
Cdd:COG2268   220 NREAEEAELEQERE---------IETARIAEAEAELAKKKAEERREAEtaRAEAEAAYEIAEANAE-REVQRQLEIAERE 289

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1632238227 461 AHGKLMNKlAAARHKAQEKRT---AAEAKRNRQAAKAEHQAEYIRKTG 505
Cdd:COG2268   290 REIELQEK-EAEREEAELEADvrkPAEAEKQAAEAEAEAEAEAIRAKG 336
PTZ00121 PTZ00121
MAEBL; Provisional
 345-503 4.20e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 4.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227  345 DQNTNKELSEKELQLKTRREIMVLGTQLGKMNIAAWASKEEDKDASASQKTvlEEQPGTSVIETRAAAWEESEKAKYMAR 424
Cdd:PTZ00121  1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAEEAKKADEAKKKAE 1480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227  425 FKR--EEMKIQAWENHQKAKteaEMRKIEVEVERIRGRAHGKLMNKLAAARhKAQEKRTAAEAKRNRQAAKAEH--QAEY 500
Cdd:PTZ00121  1481 EAKkaDEAKKKAEEAKKKAD---EAKKAAEAKKKADEAKKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADElkKAEE 1556


                   ...
gi 1632238227  501 IRK 503
Cdd:PTZ00121  1557 LKK 1559
PTZ00121 PTZ00121
MAEBL; Provisional
 378-503 8.39e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 8.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227  378 AAWASKEEDKDASASQKTVLEEQPGTSVIETRAAAWEESEKAKYMARFKREEMKIQAWENHQKA----KTEAEMRKieve 453
Cdd:PTZ00121  1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdelkKAAAAKKK---- 1419

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1632238227  454 VERIRGRAHGKlmNKLAAARHKAQEKRTAAEAKRN----RQAAKAEHQAEYIRK 503
Cdd:PTZ00121  1420 ADEAKKKAEEK--KKADEAKKKAEEAKKADEAKKKaeeaKKAEEAKKKAEEAKK 1471
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 383-503 1.33e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227 383 KEEDKDASASQKTVLEEQPGTSVIETRAAAWEESEKAKYMARFKREEMKiQAWENHQKAKTEAEmRKIEVEVER------ 456
Cdd:TIGR02794  71 KKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQK-QAEEAKAKQAAEAK-AKAEAEAERkakeea 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1632238227 457 IRGRAHGKLMNKLAAARHKAQE-----------------KRTAAEAKRNRQAAKAEHQAEYIRK 503
Cdd:TIGR02794 149 AKQAEEEAKAKAAAEAKKKAEEakkkaeaeakakaeaeaKAKAEEAKAKAEAAKAKAAAEAAAK 212
PTZ00121 PTZ00121
MAEBL; Provisional
 355-503 5.53e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227  355 KELQLKTRREIMVLGTQLGKMNiAAWASKEEDKDASASQKTVLEEQPgTSVIETRAAAWEESEKAKYMaRFKREEMKIQA 434
Cdd:PTZ00121  1587 KKAEEARIEEVMKLYEEEKKMK-AEEAKKAEEAKIKAEELKKAEEEK-KKVEQLKKKEAEEKKKAEEL-KKAEEENKIKA 1663

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1632238227  435 WENHQKA---KTEAEMRKIEVEVERirgrahgklmNKLAAARHKAQEKRTAAEAKrnRQAAKAEHQAEYIRK 503
Cdd:PTZ00121  1664 AEEAKKAeedKKKAEEAKKAEEDEK----------KAAEALKKEAEEAKKAEELK--KKEAEEKKKAEELKK 1723
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 403-503 5.98e-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: 37.46  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227 403 TSVIETRAAAWEESEKAkymARFKREEMKiqawenHQKAKTEAEMRKIEVEVERIRGRAHgklmnklAAARHKAQEKRTA 482
Cdd:COG0711    26 LKALDERQEKIADGLAE---AERAKEEAE------AALAEYEEKLAEARAEAAEIIAEAR-------KEAEAIAEEAKAE 89

                          90       100
                  ....*....|....*....|.
gi 1632238227 483 AEAKRNRQAAKAEHQAEYIRK 503
Cdd:COG0711    90 AEAEAERIIAQAEAEIEQERA 110
PTZ00121 PTZ00121
MAEBL; Provisional
 381-498 6.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 6.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632238227  381 ASKEEDKDASASQKTVLEEQPGTSVIETRAAAWEESEKAKYMARFKREEMKIQAWE----NHQKAKTEAEMRKIEVEV-- 454
Cdd:PTZ00121  1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEKkk 1648

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1632238227  455 -ERIRGRAHGKLMNKLAAARHKAQEKRTAAEAKRNRQAAKAEHQA 498
Cdd:PTZ00121  1649 aEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
 
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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