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Conserved domains on  [gi|1406036213|gb|PZY67122|]
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hypothetical protein DIV17_01000 [Escherichia coli]

Protein Classification

peptidase M16 family protein( domain architecture ID 1000437)

peptidase M16 family protein may act as a peptidase cleaving small peptides close to a terminus, often including bonds on the amino side of basic residues such as arginine

CATH:  3.30.830.10
MEROPS:  M16

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PqqL super family cl33975
Predicted Zn-dependent peptidase, M16 family [General function prediction only];
54-161 4.02e-04

Predicted Zn-dependent peptidase, M16 family [General function prediction only];


The actual alignment was detected with superfamily member COG0612:

Pssm-ID: 440377 [Multi-domain]  Cd Length: 427  Bit Score: 39.52  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406036213  54 STSRESMELLEALAEAGVTIgNFFSNDLMTAYGrrqqnkraeaERIAKEQ-----RIQAERMREENMTDAEWQKElqrRE 128
Cdd:COG0612    69 TKKRSAGEIAEELEALGGSL-NAFTSFDYTVYY----------LSVLSEDlelalELLADRLLNPTFDEEELERE---RG 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1406036213 129 QVKAERRTY--------GENLRSA---THSAGRSRAAIVADLES 161
Cdd:COG0612   135 VVLEEIRRYeddpdglaFEALLAAlygDHPYGRPIIGTEESIEA 178
 
Name Accession Description Interval E-value
PqqL COG0612
Predicted Zn-dependent peptidase, M16 family [General function prediction only];
54-161 4.02e-04

Predicted Zn-dependent peptidase, M16 family [General function prediction only];


Pssm-ID: 440377 [Multi-domain]  Cd Length: 427  Bit Score: 39.52  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406036213  54 STSRESMELLEALAEAGVTIgNFFSNDLMTAYGrrqqnkraeaERIAKEQ-----RIQAERMREENMTDAEWQKElqrRE 128
Cdd:COG0612    69 TKKRSAGEIAEELEALGGSL-NAFTSFDYTVYY----------LSVLSEDlelalELLADRLLNPTFDEEELERE---RG 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1406036213 129 QVKAERRTY--------GENLRSA---THSAGRSRAAIVADLES 161
Cdd:COG0612   135 VVLEEIRRYeddpdglaFEALLAAlygDHPYGRPIIGTEESIEA 178
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 87-135 6.59e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 36.01  E-value: 6.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1406036213  87 RRQQNKRAEAERIAKEQRIQAERMREENMTDAEWQKELQRREQVKAERR 135
Cdd:pfam07946 275 KAAEEERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYEEKERKKEQRK 323
 
Name Accession Description Interval E-value
PqqL COG0612
Predicted Zn-dependent peptidase, M16 family [General function prediction only];
54-161 4.02e-04

Predicted Zn-dependent peptidase, M16 family [General function prediction only];


Pssm-ID: 440377 [Multi-domain]  Cd Length: 427  Bit Score: 39.52  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406036213  54 STSRESMELLEALAEAGVTIgNFFSNDLMTAYGrrqqnkraeaERIAKEQ-----RIQAERMREENMTDAEWQKElqrRE 128
Cdd:COG0612    69 TKKRSAGEIAEELEALGGSL-NAFTSFDYTVYY----------LSVLSEDlelalELLADRLLNPTFDEEELERE---RG 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1406036213 129 QVKAERRTY--------GENLRSA---THSAGRSRAAIVADLES 161
Cdd:COG0612   135 VVLEEIRRYeddpdglaFEALLAAlygDHPYGRPIIGTEESIEA 178
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 87-135 6.59e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 36.01  E-value: 6.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1406036213  87 RRQQNKRAEAERIAKEQRIQAERMREENMTDAEWQKELQRREQVKAERR 135
Cdd:pfam07946 275 KAAEEERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYEEKERKKEQRK 323
 
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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