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Conserved domains on  [gi|185179364|gb|ACC77637|]
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sigma C [Kampar orthoreovirus]

Protein Classification

COG4372 family protein( domain architecture ID 11468211)

COG4372 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
55-165 6.40e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185179364  55 NLTGIVSKHTTDISSITSDLSSLTGKLDSQLSELDELKTNVSSNLTDLQslssrvsSVSNDLAAVNSSLEQLSGKLNVTA 134
Cdd:COG4372   14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE-------QLEEELEQARSELEQLEEELEELN 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 185179364 135 TDVTNLQNSVSTMAAQLSALDSKLNDTAQRL 165
Cdd:COG4372   87 EQLQAAQAELAQAQEELESLQEEAEELQEEL 117
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
55-165 6.40e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185179364  55 NLTGIVSKHTTDISSITSDLSSLTGKLDSQLSELDELKTNVSSNLTDLQslssrvsSVSNDLAAVNSSLEQLSGKLNVTA 134
Cdd:COG4372   14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE-------QLEEELEQARSELEQLEEELEELN 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 185179364 135 TDVTNLQNSVSTMAAQLSALDSKLNDTAQRL 165
Cdd:COG4372   87 EQLQAAQAELAQAQEELESLQEEAEELQEEL 117
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 46-160 6.34e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 37.69  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185179364    46 LNSMSVALTNLTgivsKHTTDISSITSDLSSLTGKLDSQLSELDELKTNVSSNL-TDLQSLSSRVSSVSNDLAAVNSSLE 124
Cdd:smart00787 153 LEGLKEDYKLLM----KELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDpTELDRAKEKLKKLLQEIMIKVKKLE 228

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 185179364   125 QLSGKLNVTATDVTNLQNSVSTMAAQLSALDSKLND 160
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 66-163 7.53e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 37.39  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185179364  66 DISSITSDLSSLTGKLDSQLSELDELKTNVSSNLTDLQSLSSRVSSVSNDLAAVNSSLEQLSGKLNVTATDVTNLQNSVS 145
Cdd:cd21116   99 GLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQ 178

                         90
                 ....*....|....*...
gi 185179364 146 TMAAQLSALDSKLNDTAQ 163
Cdd:cd21116  179 TLDSDIKELITDLEDAES 196
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
55-165 6.40e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185179364  55 NLTGIVSKHTTDISSITSDLSSLTGKLDSQLSELDELKTNVSSNLTDLQslssrvsSVSNDLAAVNSSLEQLSGKLNVTA 134
Cdd:COG4372   14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE-------QLEEELEQARSELEQLEEELEELN 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 185179364 135 TDVTNLQNSVSTMAAQLSALDSKLNDTAQRL 165
Cdd:COG4372   87 EQLQAAQAELAQAQEELESLQEEAEELQEEL 117
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
23-165 1.29e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185179364  23 ALILTMTQSTSASRSDLSAVRSDLNSMSVALTNLTGIVSKHTTDISSITSDLSSLTGKLDSQLSELDELKTNVSSNLTDL 102
Cdd:COG4372   24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185179364 103 QSLSSRVSSVSNDLAAVNSSLEQLSGKLNVTATDVTNLQNSVSTMAAQLSALDSKLNDTAQRL 165
Cdd:COG4372  104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 46-160 6.34e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 37.69  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185179364    46 LNSMSVALTNLTgivsKHTTDISSITSDLSSLTGKLDSQLSELDELKTNVSSNL-TDLQSLSSRVSSVSNDLAAVNSSLE 124
Cdd:smart00787 153 LEGLKEDYKLLM----KELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDpTELDRAKEKLKKLLQEIMIKVKKLE 228

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 185179364   125 QLSGKLNVTATDVTNLQNSVSTMAAQLSALDSKLND 160
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 66-163 7.53e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 37.39  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185179364  66 DISSITSDLSSLTGKLDSQLSELDELKTNVSSNLTDLQSLSSRVSSVSNDLAAVNSSLEQLSGKLNVTATDVTNLQNSVS 145
Cdd:cd21116   99 GLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQ 178

                         90
                 ....*....|....*...
gi 185179364 146 TMAAQLSALDSKLNDTAQ 163
Cdd:cd21116  179 TLDSDIKELITDLEDAES 196
 
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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