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Conserved domains on  [gi|2451902454|ref|WP_274973455|]
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type II CAAX prenyl endopeptidase Rce1 family protein [Nocardiopsis sp. HUAS JQ3]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH113-like super family cl16298
Glycoside hydrolase family 113 beta-mannosidase and similar proteins; Family 113 glycoside ...
 442-568 9.80e-10

Glycoside hydrolase family 113 beta-mannosidase and similar proteins; Family 113 glycoside hydrolases cleave (1->4)-beta-glycosidic linkages, such as endo-1,4-beta-mannanase. This family also includes TIM-barrel domains found in gene transfer agent proteins.


The actual alignment was detected with superfamily member cd19608:

Pssm-ID: 449734  Cd Length: 310  Bit Score: 60.08  E-value: 9.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451902454 442 REMAGTARGGFHGPLTYGSGTWESVDWAPF----DVVGVDYYL------------DELTRRSYRQGLRRLR-AHGKPVVV 504
Cdd:cd19608   147 RALIAEVRSVYSGKLTYAANWDSEYESVPFwdalDYIGVDAYFpltdkptpsveeLAAGWQPILDQLEALAdKYGKPVLF 226

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2451902454 505 TEFGCCSYEGArdrggsGSDILDWSDLGDrrvrgghVRDERVQADLIGDLLDVFETEE-VHGAFV 568
Cdd:cd19608   227 TEIGYPSVDGA------AAEPWDWPGASG-------PVDLQEQANAYEAFFRAFWDRPwFAGVFW 278
YdiL super family cl47285
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 158-190 2.65e-04

Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG1266:

Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 40.54  E-value: 2.65e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2451902454 158 EELVFRGYAQHHLGLRYSPWAAVPGQAALYTLF 190
Cdd:COG1266    19 EELLFRGYLLGRLRRRFGPWLAILLSSLLFGLL 51
 
Name Accession Description Interval E-value
GH113_mannanase-like cd19608
Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins; Mannan endo-1,4-beta ...
 442-568 9.80e-10

Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins; Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1->4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1->4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences.


Pssm-ID: 381626  Cd Length: 310  Bit Score: 60.08  E-value: 9.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451902454 442 REMAGTARGGFHGPLTYGSGTWESVDWAPF----DVVGVDYYL------------DELTRRSYRQGLRRLR-AHGKPVVV 504
Cdd:cd19608   147 RALIAEVRSVYSGKLTYAANWDSEYESVPFwdalDYIGVDAYFpltdkptpsveeLAAGWQPILDQLEALAdKYGKPVLF 226

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2451902454 505 TEFGCCSYEGArdrggsGSDILDWSDLGDrrvrgghVRDERVQADLIGDLLDVFETEE-VHGAFV 568
Cdd:cd19608   227 TEIGYPSVDGA------AAEPWDWPGASG-------PVDLQEQANAYEAFFRAFWDRPwFAGVFW 278
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 158-190 2.65e-04

Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 40.54  E-value: 2.65e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2451902454 158 EELVFRGYAQHHLGLRYSPWAAVPGQAALYTLF 190
Cdd:COG1266    19 EELLFRGYLLGRLRRRFGPWLAILLSSLLFGLL 51
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 156-190 1.55e-03

Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive infection) family) contains putative IMPs and has homologs in all three domains of life, including Rce1 from S. cerevisiae. Rce1 is a type II CAAX prenyl protease that processes all farnesylated and geranylgeranylated CAAX proteins. It is an integral membrane endoprotease localized to the endoplasmic reticulum that mediates the cleavage of the carboxyl-terminal three amino acids from CaaX proteins. It is involved in processing the Ras family of small GTPases, the gamma-subunit of heterotrimeric GTPases, nuclear lamins, and protein kinases and phosphatases. Three residues of S. cerevisiae Rce1 -E156, H194 and H248- are critical for catalysis. The structure of Rce1 from the archaea Methanococcus (MmRce1) suggests that this group of proteins represents a novel IMP (intramembrane protease) family, the glutamate IMPs. There is a conserved sequence motif EExxxR.


Pssm-ID: 460578 [Multi-domain]  Cd Length: 92  Bit Score: 37.92  E-value: 1.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2451902454 156 LPEELVFRGYAQHHLGLRYSPWAAVPGQAALYTLF 190
Cdd:pfam02517  16 IGEELLFRGYLLPRLRRRLWPVLAILISSLLFGLA 50
ManB2 COG4124
Beta-mannanase [Carbohydrate transport and metabolism];
472-509 8.40e-03

Beta-mannanase [Carbohydrate transport and metabolism];


Pssm-ID: 443300  Cd Length: 330  Bit Score: 38.94  E-value: 8.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2451902454 472 DVVGVDYYLD----------ELTRRSYRQGLRRLRAHGKPVVVTEFGC 509
Cdd:COG4124   230 DIVGLDGYNDgptdpwqsfdELLDPGYDELRAFARAHGKPIAITETGP 277
 
Name Accession Description Interval E-value
GH113_mannanase-like cd19608
Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins; Mannan endo-1,4-beta ...
 442-568 9.80e-10

Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins; Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1->4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1->4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences.


Pssm-ID: 381626  Cd Length: 310  Bit Score: 60.08  E-value: 9.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451902454 442 REMAGTARGGFHGPLTYGSGTWESVDWAPF----DVVGVDYYL------------DELTRRSYRQGLRRLR-AHGKPVVV 504
Cdd:cd19608   147 RALIAEVRSVYSGKLTYAANWDSEYESVPFwdalDYIGVDAYFpltdkptpsveeLAAGWQPILDQLEALAdKYGKPVLF 226

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2451902454 505 TEFGCCSYEGArdrggsGSDILDWSDLGDrrvrgghVRDERVQADLIGDLLDVFETEE-VHGAFV 568
Cdd:cd19608   227 TEIGYPSVDGA------AAEPWDWPGASG-------PVDLQEQANAYEAFFRAFWDRPwFAGVFW 278
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 158-190 2.65e-04

Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 40.54  E-value: 2.65e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2451902454 158 EELVFRGYAQHHLGLRYSPWAAVPGQAALYTLF 190
Cdd:COG1266    19 EELLFRGYLLGRLRRRFGPWLAILLSSLLFGLL 51
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 156-190 1.55e-03

Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive infection) family) contains putative IMPs and has homologs in all three domains of life, including Rce1 from S. cerevisiae. Rce1 is a type II CAAX prenyl protease that processes all farnesylated and geranylgeranylated CAAX proteins. It is an integral membrane endoprotease localized to the endoplasmic reticulum that mediates the cleavage of the carboxyl-terminal three amino acids from CaaX proteins. It is involved in processing the Ras family of small GTPases, the gamma-subunit of heterotrimeric GTPases, nuclear lamins, and protein kinases and phosphatases. Three residues of S. cerevisiae Rce1 -E156, H194 and H248- are critical for catalysis. The structure of Rce1 from the archaea Methanococcus (MmRce1) suggests that this group of proteins represents a novel IMP (intramembrane protease) family, the glutamate IMPs. There is a conserved sequence motif EExxxR.


Pssm-ID: 460578 [Multi-domain]  Cd Length: 92  Bit Score: 37.92  E-value: 1.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2451902454 156 LPEELVFRGYAQHHLGLRYSPWAAVPGQAALYTLF 190
Cdd:pfam02517  16 IGEELLFRGYLLPRLRRRLWPVLAILISSLLFGLA 50
ManB2 COG4124
Beta-mannanase [Carbohydrate transport and metabolism];
472-509 8.40e-03

Beta-mannanase [Carbohydrate transport and metabolism];


Pssm-ID: 443300  Cd Length: 330  Bit Score: 38.94  E-value: 8.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2451902454 472 DVVGVDYYLD----------ELTRRSYRQGLRRLRAHGKPVVVTEFGC 509
Cdd:COG4124   230 DIVGLDGYNDgptdpwqsfdELLDPGYDELRAFARAHGKPIAITETGP 277
 
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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