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Conserved domains on  [gi|1317229167|gb|PKX92702|]
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putative conserved membrane protein [Aspergillus novofumigatus IBT 16806]

Protein Classification

DSC3 family protein( domain architecture ID 10563342)

DSC3 (defective for SREBP cleavage 3) family protein similar to Saccharomyces cerevisiae DSC E3 ubiquitin ligase complex subunit 3 that is involved in endocytic protein trafficking

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dsc3_C pfam13373
DSC E3 ubiquitin ligase complex subunit 3, C-terminal domain; This is the C-terminal domain of ...
 176-310 5.14e-64

DSC E3 ubiquitin ligase complex subunit 3, C-terminal domain; This is the C-terminal domain of DSC E3 ubiquitin ligase complex subunit 3 (Dsc3), which contains two transmembrane helices and a characteriztic GFDRL sequence motif. Dsc3 is a component of the DSC E3 ubiquitin ligase complex (a Golgi-specific protein ubiquitination system) that functions in protein homeostasis under non-stress conditions, playing a role in protein quality control. Yeast DSC E3 ubiquitin ligase complex is the homolog of Hrd1 E3 ligase complex from mammals, in which Dsc1, Dsc2 and Dsc3 corresponds to Hrd1, Der1, and Usa1, respectively. Dsc3 is a Herp-like protein that acts as a bridge between Dsc1 and Dsc2 for their interaction.


:

Pssm-ID: 404283  Cd Length: 141  Bit Score: 198.30  E-value: 5.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317229167 176 RGFDRLLSAGFTPSEVSALRSQFMAIQSVSRTPDTMPTGAELRELEDRWMDEGSSAMAAGVGGGGEGISFADDDGGFGAG 255
Cdd:pfam13373   1 RGFDRLLSAGFSPAEVNALRLQFRSIYSSRHTPDTMPSPDTLRQLEERWMDSGANASGAALAGAPGGGGGGGGGGGGGFG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317229167 256 SR------GAMDDMLWGAVMGFFWPVGCAMWLRREEGVWSWRKGLAVFVGVVINVAFGAMR 310
Cdd:pfam13373  81 GDdgsdnsGHLDDLLWGLLIGFFLPLGALVWLLREEGVWNKRQKMAVIAGVLVNISFGLVR 141
Dsc3_N pfam10302
DSC E3 ubiquitin ligase complex subunit 3, ubiquitin-like domain; This is the N-terminal ...
 22-128 3.26e-54

DSC E3 ubiquitin ligase complex subunit 3, ubiquitin-like domain; This is the N-terminal ubiquitin-like domain of DSC E3 ubiquitin ligase complex subunit 3 (Dsc3). Dsc3 is a component of the DSC E3 ubiquitin ligase complex (a Golgi-specific protein ubiquitination system) that functions in protein homeostasis under non-stress conditions, playing a role in protein quality control through endosome and Golgi-associated degradation pathway (EGAD). Yeast DSC E3 ubiquitin ligase complex is the homolog of Hrd1 E3 ligase complex from mammals, in which Dsc1, Dsc2 and Dsc3 corresponds to Hrd1, Der1 and Usa1, respectively. Dsc3 is a Herp-like protein that acts as a bridge between Dsc1 and Dsc2 for their interaction.


:

Pssm-ID: 370959  Cd Length: 101  Bit Score: 172.08  E-value: 3.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317229167  22 LLLTVRFSASIPDLPLDIQNPDITTAAGLKQLIRTHLPPNLSSHRLRLIYAGRGLEDATPLSVSLKLPPSpsrtpvAQDD 101
Cdd:pfam10302   1 LFLVIRFSASIPDLPLDINDPNTTTIAGLKQLIRERLPPELSNRRLRLIYAGRLLNDTTTLARSLKLPPP------VHDA 74

                          90       100
                  ....*....|....*....|....*..
gi 1317229167 102 ATTAKGKGKAPVREQPRLYIHCSIGDI 128
Cdd:pfam10302  75 LSQSKGKGKAPVREQSRIYIHCSIGDE 101
 
Name Accession Description Interval E-value
Dsc3_C pfam13373
DSC E3 ubiquitin ligase complex subunit 3, C-terminal domain; This is the C-terminal domain of ...
 176-310 5.14e-64

DSC E3 ubiquitin ligase complex subunit 3, C-terminal domain; This is the C-terminal domain of DSC E3 ubiquitin ligase complex subunit 3 (Dsc3), which contains two transmembrane helices and a characteriztic GFDRL sequence motif. Dsc3 is a component of the DSC E3 ubiquitin ligase complex (a Golgi-specific protein ubiquitination system) that functions in protein homeostasis under non-stress conditions, playing a role in protein quality control. Yeast DSC E3 ubiquitin ligase complex is the homolog of Hrd1 E3 ligase complex from mammals, in which Dsc1, Dsc2 and Dsc3 corresponds to Hrd1, Der1, and Usa1, respectively. Dsc3 is a Herp-like protein that acts as a bridge between Dsc1 and Dsc2 for their interaction.


Pssm-ID: 404283  Cd Length: 141  Bit Score: 198.30  E-value: 5.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317229167 176 RGFDRLLSAGFTPSEVSALRSQFMAIQSVSRTPDTMPTGAELRELEDRWMDEGSSAMAAGVGGGGEGISFADDDGGFGAG 255
Cdd:pfam13373   1 RGFDRLLSAGFSPAEVNALRLQFRSIYSSRHTPDTMPSPDTLRQLEERWMDSGANASGAALAGAPGGGGGGGGGGGGGFG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317229167 256 SR------GAMDDMLWGAVMGFFWPVGCAMWLRREEGVWSWRKGLAVFVGVVINVAFGAMR 310
Cdd:pfam13373  81 GDdgsdnsGHLDDLLWGLLIGFFLPLGALVWLLREEGVWNKRQKMAVIAGVLVNISFGLVR 141
Dsc3_N pfam10302
DSC E3 ubiquitin ligase complex subunit 3, ubiquitin-like domain; This is the N-terminal ...
 22-128 3.26e-54

DSC E3 ubiquitin ligase complex subunit 3, ubiquitin-like domain; This is the N-terminal ubiquitin-like domain of DSC E3 ubiquitin ligase complex subunit 3 (Dsc3). Dsc3 is a component of the DSC E3 ubiquitin ligase complex (a Golgi-specific protein ubiquitination system) that functions in protein homeostasis under non-stress conditions, playing a role in protein quality control through endosome and Golgi-associated degradation pathway (EGAD). Yeast DSC E3 ubiquitin ligase complex is the homolog of Hrd1 E3 ligase complex from mammals, in which Dsc1, Dsc2 and Dsc3 corresponds to Hrd1, Der1 and Usa1, respectively. Dsc3 is a Herp-like protein that acts as a bridge between Dsc1 and Dsc2 for their interaction.


Pssm-ID: 370959  Cd Length: 101  Bit Score: 172.08  E-value: 3.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317229167  22 LLLTVRFSASIPDLPLDIQNPDITTAAGLKQLIRTHLPPNLSSHRLRLIYAGRGLEDATPLSVSLKLPPSpsrtpvAQDD 101
Cdd:pfam10302   1 LFLVIRFSASIPDLPLDINDPNTTTIAGLKQLIRERLPPELSNRRLRLIYAGRLLNDTTTLARSLKLPPP------VHDA 74

                          90       100
                  ....*....|....*....|....*..
gi 1317229167 102 ATTAKGKGKAPVREQPRLYIHCSIGDI 128
Cdd:pfam10302  75 LSQSKGKGKAPVREQSRIYIHCSIGDE 101
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 37-83 9.87e-03

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 34.11  E-value: 9.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1317229167  37 LDIQNPDITTAAGLKQLI--RTHLPPNlsshRLRLIYAGRGLEDATPLS 83
Cdd:cd17039    11 YTVEVDPDDTVADLKEKIeeKTGIPVE----QQRLIYNGKELKDDKTLS 55
 
Name Accession Description Interval E-value
Dsc3_C pfam13373
DSC E3 ubiquitin ligase complex subunit 3, C-terminal domain; This is the C-terminal domain of ...
 176-310 5.14e-64

DSC E3 ubiquitin ligase complex subunit 3, C-terminal domain; This is the C-terminal domain of DSC E3 ubiquitin ligase complex subunit 3 (Dsc3), which contains two transmembrane helices and a characteriztic GFDRL sequence motif. Dsc3 is a component of the DSC E3 ubiquitin ligase complex (a Golgi-specific protein ubiquitination system) that functions in protein homeostasis under non-stress conditions, playing a role in protein quality control. Yeast DSC E3 ubiquitin ligase complex is the homolog of Hrd1 E3 ligase complex from mammals, in which Dsc1, Dsc2 and Dsc3 corresponds to Hrd1, Der1, and Usa1, respectively. Dsc3 is a Herp-like protein that acts as a bridge between Dsc1 and Dsc2 for their interaction.


Pssm-ID: 404283  Cd Length: 141  Bit Score: 198.30  E-value: 5.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317229167 176 RGFDRLLSAGFTPSEVSALRSQFMAIQSVSRTPDTMPTGAELRELEDRWMDEGSSAMAAGVGGGGEGISFADDDGGFGAG 255
Cdd:pfam13373   1 RGFDRLLSAGFSPAEVNALRLQFRSIYSSRHTPDTMPSPDTLRQLEERWMDSGANASGAALAGAPGGGGGGGGGGGGGFG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317229167 256 SR------GAMDDMLWGAVMGFFWPVGCAMWLRREEGVWSWRKGLAVFVGVVINVAFGAMR 310
Cdd:pfam13373  81 GDdgsdnsGHLDDLLWGLLIGFFLPLGALVWLLREEGVWNKRQKMAVIAGVLVNISFGLVR 141
Dsc3_N pfam10302
DSC E3 ubiquitin ligase complex subunit 3, ubiquitin-like domain; This is the N-terminal ...
 22-128 3.26e-54

DSC E3 ubiquitin ligase complex subunit 3, ubiquitin-like domain; This is the N-terminal ubiquitin-like domain of DSC E3 ubiquitin ligase complex subunit 3 (Dsc3). Dsc3 is a component of the DSC E3 ubiquitin ligase complex (a Golgi-specific protein ubiquitination system) that functions in protein homeostasis under non-stress conditions, playing a role in protein quality control through endosome and Golgi-associated degradation pathway (EGAD). Yeast DSC E3 ubiquitin ligase complex is the homolog of Hrd1 E3 ligase complex from mammals, in which Dsc1, Dsc2 and Dsc3 corresponds to Hrd1, Der1 and Usa1, respectively. Dsc3 is a Herp-like protein that acts as a bridge between Dsc1 and Dsc2 for their interaction.


Pssm-ID: 370959  Cd Length: 101  Bit Score: 172.08  E-value: 3.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317229167  22 LLLTVRFSASIPDLPLDIQNPDITTAAGLKQLIRTHLPPNLSSHRLRLIYAGRGLEDATPLSVSLKLPPSpsrtpvAQDD 101
Cdd:pfam10302   1 LFLVIRFSASIPDLPLDINDPNTTTIAGLKQLIRERLPPELSNRRLRLIYAGRLLNDTTTLARSLKLPPP------VHDA 74

                          90       100
                  ....*....|....*....|....*..
gi 1317229167 102 ATTAKGKGKAPVREQPRLYIHCSIGDI 128
Cdd:pfam10302  75 LSQSKGKGKAPVREQSRIYIHCSIGDE 101
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 45-83 6.86e-03

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 34.84  E-value: 6.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1317229167  45 TTAAGLKQLI--RTHLPPNlsshRLRLIYAGRGLEDATPLS 83
Cdd:pfam00240  19 DTVLELKEKIaeKEGVPPE----QQRLIYSGKVLEDDQTLG 55
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 37-83 9.87e-03

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 34.11  E-value: 9.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1317229167  37 LDIQNPDITTAAGLKQLI--RTHLPPNlsshRLRLIYAGRGLEDATPLS 83
Cdd:cd17039    11 YTVEVDPDDTVADLKEKIeeKTGIPVE----QQRLIYNGKELKDDKTLS 55
 
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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