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Conserved domains on  [gi|68482077|ref|XP_715056|]
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Ddi1p [Candida albicans SC5314]

Protein Classification

DNA damage-inducible protein 1; DNA damage inducible 1 family protein( domain architecture ID 10110370)

DNA damage-inducible protein 1 (DDI1) is a probable aspartic protease that may be involved in the regulation of exocytosis| DNA damage inducible 1 (Ddi1) family protein that contains an N-terminal ubiquitin-like (UBL) domain and a retropepsin-like domain involved in hydrolysis of peptide bonds of substrates; similar to human DDI1 that is a probable aspartic protease, and appears to act as a proteasomal shuttle which links the proteasome and replication fork proteins like RTF2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RP_DDI cd05479
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ...
 172-295 9.03e-56

RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI.


:

Pssm-ID: 133146  Cd Length: 124  Bit Score: 176.97  E-value: 9.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077 172 LAWEISPESFTSVNMLYIKVKINGVEQVALVDSGAAITTISEAIAEEVGLTRLIDRRFQPQAVGIGTQTVAGKIHSAPIE 251
Cdd:cd05479   2 NAMEHHPESFGKVPMLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQKILGRIHLAQVK 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 68482077 252 IGDSkiELPCSFHVVET-SVGILFGLDMLRRHRCTIDLERDVLVI 295
Cdd:cd05479  82 IGNL--FLPCSFTVLEDdDVDFLIGLDMLKRHQCVIDLKENVLRI 124
Ubl_Ddi1_like cd01796
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ...
 1-68 1.44e-16

ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, including yeast aspartyl protease DNA-damage inducible 1 (Ddi1) and Ddi1-like proteins from vertebrates and other eukaryotes, has been characterized by containing an N-terminal ubiquitin-like (Ubl) domain and a conserved retroviral aspartyl-protease-like domain (RVP) that is important in cell-cycle control. Yeast Ddi1 and many family members also contain a C-terminal ubiquitin-association (UBA) domain, however, Ddi1-like proteins from all vertebrates lack the UBA domain. Ddi1, also termed v-SNARE-master 1 (Vsm1), is an ubiquitin receptor involved in the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as an UBA-Ubl shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also termed transporter regulator RS1 (RS1), which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Ddi1-like proteins play a significant role in cell cycle control, growth control, and trafficking in yeast and may play a crucial role in embryogenesis in higher eukaryotes.


:

Pssm-ID: 340494 [Multi-domain]  Cd Length: 73  Bit Score: 72.98  E-value: 1.44e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68482077   1 MQLTISLDHSGDIISVDVPDSLCLEDFKAYLSAETGLEASVQVLKFNGRELVG-NATLSELQIHDNDLL 68
Cdd:cd01796   1 MKLTVTTEDDDRLFSLEVSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDdKKTLEALGLKDGDLL 69
 
Name Accession Description Interval E-value
RP_DDI cd05479
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ...
 172-295 9.03e-56

RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI.


Pssm-ID: 133146  Cd Length: 124  Bit Score: 176.97  E-value: 9.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077 172 LAWEISPESFTSVNMLYIKVKINGVEQVALVDSGAAITTISEAIAEEVGLTRLIDRRFQPQAVGIGTQTVAGKIHSAPIE 251
Cdd:cd05479   2 NAMEHHPESFGKVPMLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQKILGRIHLAQVK 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 68482077 252 IGDSkiELPCSFHVVET-SVGILFGLDMLRRHRCTIDLERDVLVI 295
Cdd:cd05479  82 IGNL--FLPCSFTVLEDdDVDFLIGLDMLKRHQCVIDLKENVLRI 124
Asp_protease pfam09668
Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to ...
 163-287 1.17e-43

Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to retroviral proteases which implies they function proteolytically during regulated protein turnover.


Pssm-ID: 312981  Cd Length: 124  Bit Score: 145.96  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077   163 EEAIEENMNLAWEISPESFTSVNMLYIKVKINGVEQVALVDSGAAITTISEAIAEEVGLTRLIDRRFQPQAVGIGTQTVA 242
Cdd:pfam09668   1 QENIDENLEHAMEHHPEVFGRVTMLYINCEINGVPVKAFVDSGAQTSIMSPRCAERCGIMRLVDTRFAGIAKGVGTARIL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 68482077   243 GKIHSAPIEIGDSkiELPCSFHVVE-TSVGILFGLDMLRRHRCTID 287
Cdd:pfam09668  81 GRIHMADVKIGGL--FLPCSFSVIEgQDMDLLLGLDMLKRHQCCID 124
Ubl_Ddi1_like cd01796
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ...
 1-68 1.44e-16

ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, including yeast aspartyl protease DNA-damage inducible 1 (Ddi1) and Ddi1-like proteins from vertebrates and other eukaryotes, has been characterized by containing an N-terminal ubiquitin-like (Ubl) domain and a conserved retroviral aspartyl-protease-like domain (RVP) that is important in cell-cycle control. Yeast Ddi1 and many family members also contain a C-terminal ubiquitin-association (UBA) domain, however, Ddi1-like proteins from all vertebrates lack the UBA domain. Ddi1, also termed v-SNARE-master 1 (Vsm1), is an ubiquitin receptor involved in the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as an UBA-Ubl shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also termed transporter regulator RS1 (RS1), which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Ddi1-like proteins play a significant role in cell cycle control, growth control, and trafficking in yeast and may play a crucial role in embryogenesis in higher eukaryotes.


Pssm-ID: 340494 [Multi-domain]  Cd Length: 73  Bit Score: 72.98  E-value: 1.44e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68482077   1 MQLTISLDHSGDIISVDVPDSLCLEDFKAYLSAETGLEASVQVLKFNGRELVG-NATLSELQIHDNDLL 68
Cdd:cd01796   1 MKLTVTTEDDDRLFSLEVSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDdKKTLEALGLKDGDLL 69
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
188-295 1.57e-08

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 53.03  E-value: 1.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077 188 YIKVKINGVEQVALVDSGAAITTISEAIAEEVGLTrlIDRRFQPQAVgigtQTVAGKIHSAPIEIgdSKIEL-PCSFHVV 266
Cdd:COG3577  43 VVEGTINGQPVRFLVDTGASTVVLSESDARRLGLD--PEDLGRPVRV----QTANGVVRAARVRL--DSVRIgGITLRNV 114

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 68482077 267 ETSVG-------ILFGLDMLRRHRCTIDleRDVLVI 295
Cdd:COG3577 115 RAVVLpggelddGLLGMSFLGRLDFEID--GDRLTL 148
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 10-74 5.28e-07

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: 46.40  E-value: 5.28e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68482077    10 SGDIISVDVPDSLCLEDFKAYLSAETGLEASVQVLKFNGRELVGNATLSELQIHDNDLLQLSKKQ 74
Cdd:pfam00240   7 DGKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEYGIEDGSTIHLVLRQ 71
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 1-70 6.89e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 37.62  E-value: 6.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077      1 MQLTISlDHSGDIISVDVPDSLCLEDFKAYLSAETGLEASVQVLKFNGRELVGNATLSELQIHDNDLLQL 70
Cdd:smart00213   1 IELTVK-TLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHL 69
 
Name Accession Description Interval E-value
RP_DDI cd05479
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ...
 172-295 9.03e-56

RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI.


Pssm-ID: 133146  Cd Length: 124  Bit Score: 176.97  E-value: 9.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077 172 LAWEISPESFTSVNMLYIKVKINGVEQVALVDSGAAITTISEAIAEEVGLTRLIDRRFQPQAVGIGTQTVAGKIHSAPIE 251
Cdd:cd05479   2 NAMEHHPESFGKVPMLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQKILGRIHLAQVK 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 68482077 252 IGDSkiELPCSFHVVET-SVGILFGLDMLRRHRCTIDLERDVLVI 295
Cdd:cd05479  82 IGNL--FLPCSFTVLEDdDVDFLIGLDMLKRHQCVIDLKENVLRI 124
Asp_protease pfam09668
Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to ...
 163-287 1.17e-43

Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to retroviral proteases which implies they function proteolytically during regulated protein turnover.


Pssm-ID: 312981  Cd Length: 124  Bit Score: 145.96  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077   163 EEAIEENMNLAWEISPESFTSVNMLYIKVKINGVEQVALVDSGAAITTISEAIAEEVGLTRLIDRRFQPQAVGIGTQTVA 242
Cdd:pfam09668   1 QENIDENLEHAMEHHPEVFGRVTMLYINCEINGVPVKAFVDSGAQTSIMSPRCAERCGIMRLVDTRFAGIAKGVGTARIL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 68482077   243 GKIHSAPIEIGDSkiELPCSFHVVE-TSVGILFGLDMLRRHRCTID 287
Cdd:pfam09668  81 GRIHMADVKIGGL--FLPCSFSVIEgQDMDLLLGLDMLKRHQCCID 124
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 189-281 6.52e-17

gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins.


Pssm-ID: 464060  Cd Length: 92  Bit Score: 74.54  E-value: 6.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077   189 IKVKINGVEQVALVDSGAAITTISEAIAEEVGLTRLIDRRFQpQAVGIGTQTVAGKIHSAPIEIGDskIELP-CSFHVVE 267
Cdd:pfam13975   1 VDVTINGRPVRFLVDTGASVTVISEALAERLGLDRLVDAYPV-TVRTANGTVRAARVRLDSVKIGG--IELRnVPAVVLP 77

                          90
                  ....*....|....*
gi 68482077   268 TS-VGILFGLDMLRR 281
Cdd:pfam13975  78 GDlDDVLLGMDFLKR 92
Ubl_Ddi1_like cd01796
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ...
 1-68 1.44e-16

ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, including yeast aspartyl protease DNA-damage inducible 1 (Ddi1) and Ddi1-like proteins from vertebrates and other eukaryotes, has been characterized by containing an N-terminal ubiquitin-like (Ubl) domain and a conserved retroviral aspartyl-protease-like domain (RVP) that is important in cell-cycle control. Yeast Ddi1 and many family members also contain a C-terminal ubiquitin-association (UBA) domain, however, Ddi1-like proteins from all vertebrates lack the UBA domain. Ddi1, also termed v-SNARE-master 1 (Vsm1), is an ubiquitin receptor involved in the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as an UBA-Ubl shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also termed transporter regulator RS1 (RS1), which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Ddi1-like proteins play a significant role in cell cycle control, growth control, and trafficking in yeast and may play a crucial role in embryogenesis in higher eukaryotes.


Pssm-ID: 340494 [Multi-domain]  Cd Length: 73  Bit Score: 72.98  E-value: 1.44e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68482077   1 MQLTISLDHSGDIISVDVPDSLCLEDFKAYLSAETGLEASVQVLKFNGRELVG-NATLSELQIHDNDLL 68
Cdd:cd01796   1 MKLTVTTEDDDRLFSLEVSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDdKKTLEALGLKDGDLL 69
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 189-280 4.07e-12

Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133136  Cd Length: 92  Bit Score: 61.58  E-value: 4.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077 189 IKVKINGVEQVALVDSGAAITTISEAIAEEVGLTRLIDR-RFQPQAVGIGTQTVAGKIHSAPIEIGDSKIElpCSFHVVE 267
Cdd:cd00303   1 LKGKINGVPVRALVDSGASVNFISESLAKKLGLPPRLLPtPLKVKGANGSSVKTLGVILPVTIGIGGKTFT--VDFYVLD 78

                        90
                ....*....|....
gi 68482077 268 T-SVGILFGLDMLR 280
Cdd:cd00303  79 LlSYDVILGRPWLE 92
retropepsin_like_bacteria cd05483
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ...
 185-280 5.49e-09

Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133150  Cd Length: 96  Bit Score: 52.63  E-value: 5.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077 185 NMLYIKVKINGVEQVALVDSGAAITTISEAIAEEVGLTRLIDRRFqpQAVGIGTQTVAGKIHSAPIEIGDSKIElPCSFH 264
Cdd:cd05483   1 GHFVVPVTINGQPVRFLLDTGASTTVISEELAERLGLPLTLGGKV--TVQTANGRVRAARVRLDSLQIGGITLR-NVPAV 77

                        90       100
                ....*....|....*....|
gi 68482077 265 VVETS----VGILfGLDMLR 280
Cdd:cd05483  78 VLPGDalgvDGLL-GMDFLR 96
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 189-277 7.34e-09

Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix.


Pssm-ID: 433378  Cd Length: 90  Bit Score: 52.29  E-value: 7.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077   189 IKVKINGVEQVALVDSGAAITTISEAIAEEVGLtRLIDRRFQPQAVGIGTQTVAGKIHSAPIEIGDSKIElPCSFHVVET 268
Cdd:pfam13650   1 VPVTINGKPVRFLVDTGASGTVISPSLAERLGL-KVRGLAYTVRVSTAGGRVSAARVRLDSLRLGGLTLE-NVPALVLDL 78

                          90
                  ....*....|.
gi 68482077   269 SVGI--LFGLD 277
Cdd:pfam13650  79 GDLIdgLLGMD 89
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
188-295 1.57e-08

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 53.03  E-value: 1.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077 188 YIKVKINGVEQVALVDSGAAITTISEAIAEEVGLTrlIDRRFQPQAVgigtQTVAGKIHSAPIEIgdSKIEL-PCSFHVV 266
Cdd:COG3577  43 VVEGTINGQPVRFLVDTGASTVVLSESDARRLGLD--PEDLGRPVRV----QTANGVVRAARVRL--DSVRIgGITLRNV 114

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 68482077 267 ETSVG-------ILFGLDMLRRHRCTIDleRDVLVI 295
Cdd:COG3577 115 RAVVLpggelddGLLGMSFLGRLDFEID--GDRLTL 148
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 10-70 1.30e-07

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: 47.98  E-value: 1.30e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68482077  10 SGDIISVDVPDSLCLEDFKAYLSAETGLEASVQVLKFNGRELVGNATLSELQIHDNDLLQL 70
Cdd:cd17039   7 DGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDYGIKDGSTIHL 67
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 10-74 5.28e-07

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: 46.40  E-value: 5.28e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68482077    10 SGDIISVDVPDSLCLEDFKAYLSAETGLEASVQVLKFNGRELVGNATLSELQIHDNDLLQLSKKQ 74
Cdd:pfam00240   7 DGKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEYGIEDGSTIHLVLRQ 71
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
 189-286 4.78e-06

Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026).


Pssm-ID: 425454  Cd Length: 101  Bit Score: 44.67  E-value: 4.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077   189 IKVKINGVEQVALVDSGAAITTISeaiaEEVGLTRLIDRRFQPQAVGIGTQTVAGKIHSAPIEIGDSKIELPCSFHVVET 268
Cdd:pfam00077   7 LTVKIGGKYFTALLDTGADDTVIS----QNDWPTNWPKQKATTNIQGIGGGINVRQSDQILILIGEDKFRGTVSPLILPT 82

                          90
                  ....*....|....*...
gi 68482077   269 SVGILFGLDMLRRHRCTI 286
Cdd:pfam00077  83 CPVNIIGRDLLQQLGGRL 100
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 1-70 6.89e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 37.62  E-value: 6.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077      1 MQLTISlDHSGDIISVDVPDSLCLEDFKAYLSAETGLEASVQVLKFNGRELVGNATLSELQIHDNDLLQL 70
Cdd:smart00213   1 IELTVK-TLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHL 69
Ubl_IQUB cd17061
ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) ...
 10-71 1.18e-03

ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) and similar proteins; IQUB is an IQ motif and ubiquitin domain-containing protein that may play roles in cilia formation and/or maintenance. It contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340581  Cd Length: 79  Bit Score: 37.24  E-value: 1.18e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68482077  10 SGDIISVDVPDSLCLEDFKAYLSAETGLEASVQVLKFNGRELVGNATLSELQIHDNDLLQLS 71
Cdd:cd17061  12 SGQVITLAFTLGQTIGELKEHFSSELKIPPDVLQIMFDGKLVEDNTTLVDLGVRPNGTIQLE 73
RP_RTVL_H_like cd06095
Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family ...
 189-280 1.91e-03

Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family includes aspartate proteases from retroelements with LTR (long terminal repeats) including the RTVL_H family of human endogenous retrovirus-like elements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133159  Cd Length: 86  Bit Score: 36.93  E-value: 1.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68482077 189 IKVKINGVEQVALVDSGAAITTISEAIAEEVGLTrlidrRFQPQAVGI-GTQTVAGKIHSAPIEIGDSkiELPCSFHVVE 267
Cdd:cd06095   1 VTITVEGVPIVFLVDTGATHSVLKSDLGPKQELS-----TTSVLIRGVsGQSQQPVTTYRTLVDLGGH--TVSHSFLVVP 73

                        90
                ....*....|...
gi 68482077 268 TSVGILFGLDMLR 280
Cdd:cd06095  74 NCPDPLLGRDLLS 86
Ubl_BAG6 cd01809
ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins; ...
 18-63 7.79e-03

ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins; BAG6, also termed large proline-rich protein BAG6, or BAG family molecular chaperone regulator 6, or HLA-B-associated transcript 3 (Bat3), or protein Scythe, or protein G3, is a nucleo-cytoplasmic shuttling chaperone protein that is highly conserved in eukaryotes. It functions in two distinct biological pathways, ubiquitin-mediated protein degradation of defective polypeptides and tail-anchored transmembrane protein biogenesis in mammals. BAG6 is a component of the heterotrimeric BAG6 sortase complex composed of BAG6, transmembrane recognition complex 35 (TRC35) and ubiquitin-like protein 4A (UBL4A). The BAG6 complex together with the cochaperone small, glutamine-rich, tetratricopeptide repeat-containing, protein alpha (SGTA) plays a role in the biogenesis of tail-anchored membrane proteins and subsequently shown to regulate the ubiquitination and proteasomal degradation of mislocalized proteins. Moreover, BAG6 acts as an apoptotic regulator that binds reaper, a potent apoptotic inducer. BAG6/reaper is thought to signal apoptosis, in part through regulating the folding and activity of apoptotic signaling molecules. It is also likely a key regulator of the molecular chaperone Heat Shock Protein A2 (HSPA2) stability/function in human germ cells. Furthermore, aspartyl protease-mediated cleavage of BAG6 is necessary for autophagy and fungal resistance in plants. BAG6 contains a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which provides a platform for discriminating substrates with shorter hydrophobicity stretches as a signal for defective proteins.


Pssm-ID: 340507 [Multi-domain]  Cd Length: 71  Bit Score: 34.63  E-value: 7.79e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 68482077  18 VPDSLCLEDFKAYLSAETGLEASVQVLKFNGRELVGNATLSELQIH 63
Cdd:cd01809  17 VPEEITVKEFKEHIASSVNIPAEKQRLIFQGRVLQDDKKLKEYDVD 62
 
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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