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Conserved domains on  [gi|2082543535|gb|QZA75608|]
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VP6 [Porcine rotavirus A]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rota_Capsid_VP6 super family cl03051
Rotavirus major capsid protein VP6; Rotaviruses consist of three concentric protein shells. ...
1-396 0e+00

Rotavirus major capsid protein VP6; Rotaviruses consist of three concentric protein shells. The intermediate (middle) protein layer consists 260 trimers of VP6. VP6 in the most abundant protein in the virion. VP6 is also involved in virion assembly, and possesses the ability to interact with VP2, VP4 and VP7.


The actual alignment was detected with superfamily member pfam00980:

Pssm-ID: 395780  Cd Length: 396  Bit Score: 676.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535   1 MEVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMVVTMNGNDFQTGGIGNLPIKNWTFDFGLLGTTLLNLNANYVEN 80
Cdd:pfam00980   1 MDVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIITMNGNEFQTGGIGNLPIRNWNFQFGLLGTTLLNLDANYVET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535  81 AKTTIEYFIDFIDNVCMDEIARESQRNGIAPQSEALRKLSGIKFKRINFDNSSDYIENWNLQNRRQRTGFVFHKPNILPY 160
Cdd:pfam00980  81 ARNTIDYFVDFVDNVCMDEMVRESQRNGIAPQSDSLRKLSSIKFKRINFDNSSEYIENWNLQNRRQRTGFTFHKPNIFPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535 161 SASFTLNRSQPAHDNLMGTMWINAGSEIQVAGFDYSCAFNAPANIQQFEHVVPLRRALTTATITLLPDAERFSFPRVINS 240
Cdd:pfam00980 161 SASFTLNRSQPAHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANIQQFEHIVRLRRVLTTATITLLPDAERFSFPRVINS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535 241 ADGTTTWYFNPVILRPSNVEVEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLVRPPNMTPAVANLFPQAPPFIFHATV 320
Cdd:pfam00980 241 ADGATTWLFNPVILRPNNVEVEFLLNGQIINTYQARFGTITARNFDTIRLSFQLMRPPNMTPAVARLFPNAQPFEHHATV 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2082543535 321 GLTLRIESAVCESVLADASETLLANVTAVRQEYAIPVGPVFPPGMNWTELITNYSPSREDNLQRVFTVASIRSMLI 396
Cdd:pfam00980 321 GLTLRIESAVCESVLADASSTELANVTSVRQEYAIPVGPVFPPGMNWTDLITNYSPSREDNLQRVFTVASIRSMLM 396
 
Name Accession Description Interval E-value
Rota_Capsid_VP6 pfam00980
Rotavirus major capsid protein VP6; Rotaviruses consist of three concentric protein shells. ...
1-396 0e+00

Rotavirus major capsid protein VP6; Rotaviruses consist of three concentric protein shells. The intermediate (middle) protein layer consists 260 trimers of VP6. VP6 in the most abundant protein in the virion. VP6 is also involved in virion assembly, and possesses the ability to interact with VP2, VP4 and VP7.


Pssm-ID: 395780  Cd Length: 396  Bit Score: 676.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535   1 MEVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMVVTMNGNDFQTGGIGNLPIKNWTFDFGLLGTTLLNLNANYVEN 80
Cdd:pfam00980   1 MDVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIITMNGNEFQTGGIGNLPIRNWNFQFGLLGTTLLNLDANYVET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535  81 AKTTIEYFIDFIDNVCMDEIARESQRNGIAPQSEALRKLSGIKFKRINFDNSSDYIENWNLQNRRQRTGFVFHKPNILPY 160
Cdd:pfam00980  81 ARNTIDYFVDFVDNVCMDEMVRESQRNGIAPQSDSLRKLSSIKFKRINFDNSSEYIENWNLQNRRQRTGFTFHKPNIFPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535 161 SASFTLNRSQPAHDNLMGTMWINAGSEIQVAGFDYSCAFNAPANIQQFEHVVPLRRALTTATITLLPDAERFSFPRVINS 240
Cdd:pfam00980 161 SASFTLNRSQPAHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANIQQFEHIVRLRRVLTTATITLLPDAERFSFPRVINS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535 241 ADGTTTWYFNPVILRPSNVEVEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLVRPPNMTPAVANLFPQAPPFIFHATV 320
Cdd:pfam00980 241 ADGATTWLFNPVILRPNNVEVEFLLNGQIINTYQARFGTITARNFDTIRLSFQLMRPPNMTPAVARLFPNAQPFEHHATV 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2082543535 321 GLTLRIESAVCESVLADASETLLANVTAVRQEYAIPVGPVFPPGMNWTELITNYSPSREDNLQRVFTVASIRSMLI 396
Cdd:pfam00980 321 GLTLRIESAVCESVLADASSTELANVTSVRQEYAIPVGPVFPPGMNWTDLITNYSPSREDNLQRVFTVASIRSMLM 396
 
Name Accession Description Interval E-value
Rota_Capsid_VP6 pfam00980
Rotavirus major capsid protein VP6; Rotaviruses consist of three concentric protein shells. ...
1-396 0e+00

Rotavirus major capsid protein VP6; Rotaviruses consist of three concentric protein shells. The intermediate (middle) protein layer consists 260 trimers of VP6. VP6 in the most abundant protein in the virion. VP6 is also involved in virion assembly, and possesses the ability to interact with VP2, VP4 and VP7.


Pssm-ID: 395780  Cd Length: 396  Bit Score: 676.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535   1 MEVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMVVTMNGNDFQTGGIGNLPIKNWTFDFGLLGTTLLNLNANYVEN 80
Cdd:pfam00980   1 MDVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIITMNGNEFQTGGIGNLPIRNWNFQFGLLGTTLLNLDANYVET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535  81 AKTTIEYFIDFIDNVCMDEIARESQRNGIAPQSEALRKLSGIKFKRINFDNSSDYIENWNLQNRRQRTGFVFHKPNILPY 160
Cdd:pfam00980  81 ARNTIDYFVDFVDNVCMDEMVRESQRNGIAPQSDSLRKLSSIKFKRINFDNSSEYIENWNLQNRRQRTGFTFHKPNIFPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535 161 SASFTLNRSQPAHDNLMGTMWINAGSEIQVAGFDYSCAFNAPANIQQFEHVVPLRRALTTATITLLPDAERFSFPRVINS 240
Cdd:pfam00980 161 SASFTLNRSQPAHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANIQQFEHIVRLRRVLTTATITLLPDAERFSFPRVINS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082543535 241 ADGTTTWYFNPVILRPSNVEVEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLVRPPNMTPAVANLFPQAPPFIFHATV 320
Cdd:pfam00980 241 ADGATTWLFNPVILRPNNVEVEFLLNGQIINTYQARFGTITARNFDTIRLSFQLMRPPNMTPAVARLFPNAQPFEHHATV 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2082543535 321 GLTLRIESAVCESVLADASETLLANVTAVRQEYAIPVGPVFPPGMNWTELITNYSPSREDNLQRVFTVASIRSMLI 396
Cdd:pfam00980 321 GLTLRIESAVCESVLADASSTELANVTSVRQEYAIPVGPVFPPGMNWTDLITNYSPSREDNLQRVFTVASIRSMLM 396
 
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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