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Conserved domains on  [gi|146262012|ref|NP_082218|]
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protein DDI1 homolog 1 [Mus musculus]

Protein Classification

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

DNA damage-inducible protein 1 (DDI1) is a probable aspartic protease that may be involved in the regulation of exocytosis

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 ...
 235-357 4.37e-78

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: 237.07  E-value: 4.37e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012 235 IAMEEAPESFGQVAMLYINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGVAKGVGTQRIMGRVHLAQIQ 314
Cdd:cd05479    2 NAMEHHPESFGKVPMLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQKILGRIHLAQVK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 146262012 315 IEGDFLQCSFSILEEQPMDILLGLDMLRRHQCSIDLKKNVLVI 357
Cdd:cd05479   82 IGNLFLPCSFTVLEDDDVDFLIGLDMLKRHQCVIDLKENVLRI 124
Ubl_Ddi1_like cd01796
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ...
 1-76 2.77e-24

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: 94.93  E-value: 2.77e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146262012   1 MLITVYCVRRDlteVTFSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLTDDHCSLGSYGLKDGDMVVLLQ 76
Cdd:cd01796    1 MKLTVTTEDDD---RLFSLEVSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDDKKTLEALGLKDGDLLLLRP 73
 
Name Accession Description Interval E-value
RP_DDI cd05479
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ...
 235-357 4.37e-78

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: 237.07  E-value: 4.37e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012 235 IAMEEAPESFGQVAMLYINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGVAKGVGTQRIMGRVHLAQIQ 314
Cdd:cd05479    2 NAMEHHPESFGKVPMLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQKILGRIHLAQVK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 146262012 315 IEGDFLQCSFSILEEQPMDILLGLDMLRRHQCSIDLKKNVLVI 357
Cdd:cd05479   82 IGNLFLPCSFTVLEDDDVDFLIGLDMLKRHQCVIDLKENVLRI 124
Asp_protease pfam09668
Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to ...
 226-349 1.00e-74

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: 228.39  E-value: 1.00e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012  226 QQNIEENMNIAMEEAPESFGQVAMLYINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGVAKGVGTQRIM 305
Cdd:pfam09668   1 QENIDENLEHAMEHHPEVFGRVTMLYINCEINGVPVKAFVDSGAQTSIMSPRCAERCGIMRLVDTRFAGIAKGVGTARIL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 146262012  306 GRVHLAQIQIEGDFLQCSFSILEEQPMDILLGLDMLRRHQCSID 349
Cdd:pfam09668  81 GRIHMADVKIGGLFLPCSFSVIEGQDMDLLLGLDMLKRHQCCID 124
Ubl_Ddi1_like cd01796
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ...
 1-76 2.77e-24

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: 94.93  E-value: 2.77e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146262012   1 MLITVYCVRRDlteVTFSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLTDDHCSLGSYGLKDGDMVVLLQ 76
Cdd:cd01796    1 MKLTVTTEDDD---RLFSLEVSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDDKKTLEALGLKDGDLLLLRP 73
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
251-357 8.89e-08

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 51.10  E-value: 8.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012 251 YINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGV--AKGVGTQRimgRVHLAQIQIeGDFL--QCSFSI 326
Cdd:COG3577   43 VVEGTINGQPVRFLVDTGASTVVLSESDARRLGLDPEDLGRPVRVqtANGVVRAA---RVRLDSVRI-GGITlrNVRAVV 118

                         90       100       110
                 ....*....|....*....|....*....|..
gi 146262012 327 LEEQPM-DILLGLDMLRRHQCSIDlkKNVLVI 357
Cdd:COG3577  119 LPGGELdDGLLGMSFLGRLDFEID--GDRLTL 148
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 16-77 1.53e-04

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: 39.85  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 146262012   16 TFSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLTDDHCsLGSYGLKDGDMVVLLQK 77
Cdd:pfam00240  10 KITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQT-LGEYGIEDGSTIHLVLR 70
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 1-77 1.65e-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: 39.55  E-value: 1.65e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 146262012     1 MLITVycvrRDLTEVTFSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLtDDHCSLGSYGLKDGDMVVLLQK 77
Cdd:smart00213   1 IELTV----KTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVL-EDDRTLADYGIQDGSTIHLVLR 72
 
Name Accession Description Interval E-value
RP_DDI cd05479
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ...
 235-357 4.37e-78

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: 237.07  E-value: 4.37e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012 235 IAMEEAPESFGQVAMLYINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGVAKGVGTQRIMGRVHLAQIQ 314
Cdd:cd05479    2 NAMEHHPESFGKVPMLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQKILGRIHLAQVK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 146262012 315 IEGDFLQCSFSILEEQPMDILLGLDMLRRHQCSIDLKKNVLVI 357
Cdd:cd05479   82 IGNLFLPCSFTVLEDDDVDFLIGLDMLKRHQCVIDLKENVLRI 124
Asp_protease pfam09668
Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to ...
 226-349 1.00e-74

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: 228.39  E-value: 1.00e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012  226 QQNIEENMNIAMEEAPESFGQVAMLYINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGVAKGVGTQRIM 305
Cdd:pfam09668   1 QENIDENLEHAMEHHPEVFGRVTMLYINCEINGVPVKAFVDSGAQTSIMSPRCAERCGIMRLVDTRFAGIAKGVGTARIL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 146262012  306 GRVHLAQIQIEGDFLQCSFSILEEQPMDILLGLDMLRRHQCSID 349
Cdd:pfam09668  81 GRIHMADVKIGGLFLPCSFSVIEGQDMDLLLGLDMLKRHQCCID 124
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 252-343 2.11e-30

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: 112.28  E-value: 2.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012  252 INCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGVAKGVGTQRImGRVHLAQIQIEGDFLQ-CSFSILEEQ 330
Cdd:pfam13975   1 VDVTINGRPVRFLVDTGASVTVISEALAERLGLDRLVDAYPVTVRTANGTVRA-ARVRLDSVKIGGIELRnVPAVVLPGD 79

                          90
                  ....*....|...
gi 146262012  331 PMDILLGLDMLRR 343
Cdd:pfam13975  80 LDDVLLGMDFLKR 92
Ubl_Ddi1_like cd01796
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ...
 1-76 2.77e-24

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: 94.93  E-value: 2.77e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146262012   1 MLITVYCVRRDlteVTFSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLTDDHCSLGSYGLKDGDMVVLLQ 76
Cdd:cd01796    1 MKLTVTTEDDD---RLFSLEVSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDDKKTLEALGLKDGDLLLLRP 73
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 252-342 1.08e-14

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: 69.29  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012 252 INCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGVaKGVGTQRIM--GRVHLAQIQIEGDFLQCSFSILEE 329
Cdd:cd00303    1 LKGKINGVPVRALVDSGASVNFISESLAKKLGLPPRLLPTPLKV-KGANGSSVKtlGVILPVTIGIGGKTFTVDFYVLDL 79

                         90
                 ....*....|...
gi 146262012 330 QPMDILLGLDMLR 342
Cdd:cd00303   80 LSYDVILGRPWLE 92
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 3-75 1.07e-09

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: 54.14  E-value: 1.07e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146262012   3 ITVycvrRDLTEVTFSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLTDDHcSLGSYGLKDGDMVVLL 75
Cdd:cd17039    1 ITV----KTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK-TLSDYGIKDGSTIHLV 68
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 252-339 5.71e-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: 53.06  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012  252 INCKVNGHPLKAFVDSGAQMTIMSQACAERCNImRLVDRRWGGVAKGVGTQRIMGRVHLAQIQIeGDFL--QCSFSILEE 329
Cdd:pfam13650   1 VPVTINGKPVRFLVDTGASGTVISPSLAERLGL-KVRGLAYTVRVSTAGGRVSAARVRLDSLRL-GGLTleNVPALVLDL 78

                          90
                  ....*....|.
gi 146262012  330 QPM-DILLGLD 339
Cdd:pfam13650  79 GDLiDGLLGMD 89
NRIP_C cd05480
NRIP_C; putative nuclear receptor interacting protein; Proteins in this family have been ...
 252-352 7.23e-08

NRIP_C; putative nuclear receptor interacting protein; Proteins in this family have been described as probable nuclear receptor interacting proteins. The C-terminal domain of this family is homologous to the retroviral aspartyl protease domain. The domain is structurally related to one lobe of the pepsin molecule. The conserved active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. 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: 133147  Cd Length: 103  Bit Score: 50.24  E-value: 7.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012 252 INCKVNGHPLKAFVDSGAQMTIMSQACAERCNIM-RLVDRRWGGVAKGVGTQ-RIMGRVHLAQIQIEGDFLQCSFSILEE 329
Cdd:cd05480    1 VSCQCAGKELRALVDTGCQYNLISAACLDRLGLKeRVLKAKAEEEAPSLPTSvKVIGQIERLVLQLGQLTVECSAQVVDD 80

                         90       100
                 ....*....|....*....|...
gi 146262012 330 QPMDILLGLDMLRRHQCSIDLKK 352
Cdd:cd05480   81 NEKNFSLGLQTLKSLKCVINLEK 103
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
251-357 8.89e-08

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 51.10  E-value: 8.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012 251 YINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGV--AKGVGTQRimgRVHLAQIQIeGDFL--QCSFSI 326
Cdd:COG3577   43 VVEGTINGQPVRFLVDTGASTVVLSESDARRLGLDPEDLGRPVRVqtANGVVRAA---RVRLDSVRI-GGITlrNVRAVV 118

                         90       100       110
                 ....*....|....*....|....*....|..
gi 146262012 327 LEEQPM-DILLGLDMLRRHQCSIDlkKNVLVI 357
Cdd:COG3577  119 LPGGELdDGLLGMSFLGRLDFEID--GDRLTL 148
Ubl2_FAT10 cd17053
ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 ...
 11-75 1.60e-06

ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 (FAT10) and similar proteins; FAT10, also termed ubiquitin D (UBD), or diubiquitin, is a cytokine-inducible ubiquitin-like (Ubl) modifer that is highly expressed in the thymus, and targets substrates covalently for 26S proteasomal degradation. It is also associated with cancer development, antigen processing and antimicrobial defense, chromosomal stability and cell cycle regulation. FAT10 is presented on immune cells and under the inflammatory conditions, is synergistically induced by interferon gamma (IFNgamma) and tumor necrosis factor (TNFalpha) in the non-immune (liver parenchymal) cells. FAT10 contains two Ubl domains. The family corresponds to the second Ubl domain of FAT10. Some family members contain only one Ubl domain.


Pssm-ID: 340573  Cd Length: 71  Bit Score: 45.42  E-value: 1.60e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 146262012  11 DLTEVTFSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLTDDHCSLGSYGLKDGDMVVLL 75
Cdd:cd17053    7 LLTGTVHTLQVSRSTTVAQVKAMIEDQSGVPPNEQILVYNGKRLEDGDKTLGEYGIKTGDTLYLL 71
retropepsin_like_bacteria cd05483
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ...
 249-342 1.95e-06

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: 45.70  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012 249 MLYINCKVNGHPLKAFVDSGAQMTIMSQACAERCNI-MRLVDRRWGGVAKGVGTQRimgRVHLAQIQIeGD--FLQCSFS 325
Cdd:cd05483    2 HFVVPVTINGQPVRFLLDTGASTTVISEELAERLGLpLTLGGKVTVQTANGRVRAA---RVRLDSLQI-GGitLRNVPAV 77

                         90
                 ....*....|....*....
gi 146262012 326 ILEEQPM--DILLGLDMLR 342
Cdd:cd05483   78 VLPGDALgvDGLLGMDFLR 96
Ubl_UBL4A_like cd01807
ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins; UBL4A, ...
 1-77 5.76e-05

ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins; UBL4A, also termed GdX, is a ubiquitously expressed ubiquitin-like (Ubl) protein that forms a complex with partner proteins and participates in the protein processing through endoplasmic reticulum (ER), acting as a chaperone. As a key component of the BCL2-associated athanogene 6 (BAG6) chaperone complex, UBL4A plays a role in mediating DNA damage signaling and cell death. UBL4A also regulates insulin-induced Akt plasma membrane translocation through promotion of Arp2/3-dependent actin branching. Moreover, UBL4A specifically stabilizes the TC45/STAT3 association and promotes dephosphorylation of STAT3 to repress tumorigenesis. UBL4B is testis-specific, and encoded by an X-derived retrogene Ubl4b, which is specifically expressed in post-meiotic germ cells in mammals. As a germ cell-specific cytoplasmic protein, UBL4B is not present in somatic cells. Moreover, UBL4B is present in elongated spermatids, but not in spermatocytes and round spermatids, suggesting its function is restricted to late spermiogenesis. The function of UBL4A may be compensated by either UBL4B or other Ubl proteins in normal conditions. Both UBL4A and UBL4B contain a conserved Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340505 [Multi-domain]  Cd Length: 72  Bit Score: 40.81  E-value: 5.76e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 146262012   1 MLITVycvrRDLTEVTFSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLTDDHCsLGSYGLKDGDMVVLLQK 77
Cdd:cd01807    1 MLITV----KILQGKECTIEVSPTESVLTVKQLVAEQLNVPVSQQRLVFKGKTLADEHS-LSDYSIGPGSKIHLVVK 72
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
 17-76 1.11e-04

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.


Pssm-ID: 340523 [Multi-domain]  Cd Length: 73  Bit Score: 40.31  E-value: 1.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012  17 FSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLTDDHcSLGSYGLKDGDMVVLLQ 76
Cdd:cd16106   13 FTVEVEPDATVLELKELIAEKSDIPAEQQRLIYKGKILKDEE-TLSSYKIQDGHTVHLVK 71
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 16-77 1.53e-04

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: 39.85  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 146262012   16 TFSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLTDDHCsLGSYGLKDGDMVVLLQK 77
Cdd:pfam00240  10 KITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQT-LGEYGIEDGSTIHLVLR 70
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 1-77 1.65e-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: 39.55  E-value: 1.65e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 146262012     1 MLITVycvrRDLTEVTFSLQVNPDFELSNFRVLCELESGVPAEEAQIVYMEQLLtDDHCSLGSYGLKDGDMVVLLQK 77
Cdd:smart00213   1 IELTV----KTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVL-EDDRTLADYGIQDGSTIHLVLR 72
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
 252-348 4.44e-03

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: 36.58  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262012  252 INCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGVAKGVGTQRI-MGRVHLaqiqIEGDF-LQCSFSILEE 329
Cdd:pfam00077   7 LTVKIGGKYFTALLDTGADDTVISQNDWPTNWPKQKATTNIQGIGGGINVRQSdQILILI----GEDKFrGTVSPLILPT 82

                          90
                  ....*....|....*....
gi 146262012  330 QPMDIlLGLDMLRRHQCSI 348
Cdd:pfam00077  83 CPVNI-IGRDLLQQLGGRL 100
 
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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