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Conserved domains on  [gi|169646318|ref|NP_001013396|]
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SUMO-specific isopeptidase USPL1 isoform C [Mus musculus]

Protein Classification

Peptidase_C98 domain-containing protein( domain architecture ID 10634616)

Peptidase_C98 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C98 pfam15499
Ubiquitin-specific peptidase-like, SUMO isopeptidase; Peptidase_C98 is a small family of SUMO ...
 214-486 9.68e-174

Ubiquitin-specific peptidase-like, SUMO isopeptidase; Peptidase_C98 is a small family of SUMO - small ubiquitin-related modifier - isopeptidases found in eukaryotes. Reversible attachment of SUMO is an essential protein modification in all eukaryotic cells, The family neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase, and the invariant residues required for SUMO binding and cleavage, in UniProtKB:Q5W0Q7, are Cys-236, His-456 and Asp-472, all of which are fully conserved in the family. Member proteins are low-abundance proteins that colocalize with coilin in Cajal bodies. Peptidase_C98 depletion does not affect global sumoylation, but causes striking coilin mis-localization and impairs cell proliferation, functions that are not dependent on the catalytic activity. Thus, Peptidase_C98 represents a third type of SUMO protease, with essential functions in Cajal body biology.


:

Pssm-ID: 464750  Cd Length: 272  Bit Score: 490.29  E-value: 9.68e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646318  214 CVQWKNTQALCWLDCILSALVHLEVLRKTVLEACSREECVFGRLFEMYHQADELLHTHHLHGVtgEDCKKLTSEIFTEID 293
Cdd:pfam15499   1 CLQWKNSHNLCWLDSLLSALVHSKTLRKALPELNPQESSLVWRLFTKYDQACALLQTHQRTVK--DGVKKVPSDVLEKAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646318  294 TCLNKVRDEIFAKLQPKLRCTLGDMESPVFALPVLLKLEPHVESLFTYSFSWNFECSHCGHQYQNRCVKSLVTFTNIVPE 373
Cdd:pfam15499  79 ADLNELRMSVFNLLQPKLRCKLGQRESPVFALPLLLKLDPWAEKLFLHSFSWEFECSECGYKYQERVTKTLPTFTNVIPD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646318  374 WHPLNAAHFGPCNSCNSKSQIRKMVLERASPILMLHFVEGLPRRDLQHYAFHFEGSLYQVTSVIQYQAN-NHFITWFLDA 452
Cdd:pfam15499 159 WHPLNAVHLGPCNSCSAKNQRRKMVLERVPPVFMLHFVEGLPHNDLQAYSFTFQGSQYSVTAVIQYQTHlKHFVTWIRNS 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 169646318  453 DGSWLECDDLKGPCAKRHVTCEVPASETHIVIWE 486
Cdd:pfam15499 239 DGSWLECDDLKGPYCRRHKRLEVPASEIHIVFWE 272
 
Name Accession Description Interval E-value
Peptidase_C98 pfam15499
Ubiquitin-specific peptidase-like, SUMO isopeptidase; Peptidase_C98 is a small family of SUMO ...
 214-486 9.68e-174

Ubiquitin-specific peptidase-like, SUMO isopeptidase; Peptidase_C98 is a small family of SUMO - small ubiquitin-related modifier - isopeptidases found in eukaryotes. Reversible attachment of SUMO is an essential protein modification in all eukaryotic cells, The family neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase, and the invariant residues required for SUMO binding and cleavage, in UniProtKB:Q5W0Q7, are Cys-236, His-456 and Asp-472, all of which are fully conserved in the family. Member proteins are low-abundance proteins that colocalize with coilin in Cajal bodies. Peptidase_C98 depletion does not affect global sumoylation, but causes striking coilin mis-localization and impairs cell proliferation, functions that are not dependent on the catalytic activity. Thus, Peptidase_C98 represents a third type of SUMO protease, with essential functions in Cajal body biology.


Pssm-ID: 464750  Cd Length: 272  Bit Score: 490.29  E-value: 9.68e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646318  214 CVQWKNTQALCWLDCILSALVHLEVLRKTVLEACSREECVFGRLFEMYHQADELLHTHHLHGVtgEDCKKLTSEIFTEID 293
Cdd:pfam15499   1 CLQWKNSHNLCWLDSLLSALVHSKTLRKALPELNPQESSLVWRLFTKYDQACALLQTHQRTVK--DGVKKVPSDVLEKAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646318  294 TCLNKVRDEIFAKLQPKLRCTLGDMESPVFALPVLLKLEPHVESLFTYSFSWNFECSHCGHQYQNRCVKSLVTFTNIVPE 373
Cdd:pfam15499  79 ADLNELRMSVFNLLQPKLRCKLGQRESPVFALPLLLKLDPWAEKLFLHSFSWEFECSECGYKYQERVTKTLPTFTNVIPD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646318  374 WHPLNAAHFGPCNSCNSKSQIRKMVLERASPILMLHFVEGLPRRDLQHYAFHFEGSLYQVTSVIQYQAN-NHFITWFLDA 452
Cdd:pfam15499 159 WHPLNAVHLGPCNSCSAKNQRRKMVLERVPPVFMLHFVEGLPHNDLQAYSFTFQGSQYSVTAVIQYQTHlKHFVTWIRNS 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 169646318  453 DGSWLECDDLKGPCAKRHVTCEVPASETHIVIWE 486
Cdd:pfam15499 239 DGSWLECDDLKGPYCRRHKRLEVPASEIHIVFWE 272
 
Name Accession Description Interval E-value
Peptidase_C98 pfam15499
Ubiquitin-specific peptidase-like, SUMO isopeptidase; Peptidase_C98 is a small family of SUMO ...
 214-486 9.68e-174

Ubiquitin-specific peptidase-like, SUMO isopeptidase; Peptidase_C98 is a small family of SUMO - small ubiquitin-related modifier - isopeptidases found in eukaryotes. Reversible attachment of SUMO is an essential protein modification in all eukaryotic cells, The family neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase, and the invariant residues required for SUMO binding and cleavage, in UniProtKB:Q5W0Q7, are Cys-236, His-456 and Asp-472, all of which are fully conserved in the family. Member proteins are low-abundance proteins that colocalize with coilin in Cajal bodies. Peptidase_C98 depletion does not affect global sumoylation, but causes striking coilin mis-localization and impairs cell proliferation, functions that are not dependent on the catalytic activity. Thus, Peptidase_C98 represents a third type of SUMO protease, with essential functions in Cajal body biology.


Pssm-ID: 464750  Cd Length: 272  Bit Score: 490.29  E-value: 9.68e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646318  214 CVQWKNTQALCWLDCILSALVHLEVLRKTVLEACSREECVFGRLFEMYHQADELLHTHHLHGVtgEDCKKLTSEIFTEID 293
Cdd:pfam15499   1 CLQWKNSHNLCWLDSLLSALVHSKTLRKALPELNPQESSLVWRLFTKYDQACALLQTHQRTVK--DGVKKVPSDVLEKAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646318  294 TCLNKVRDEIFAKLQPKLRCTLGDMESPVFALPVLLKLEPHVESLFTYSFSWNFECSHCGHQYQNRCVKSLVTFTNIVPE 373
Cdd:pfam15499  79 ADLNELRMSVFNLLQPKLRCKLGQRESPVFALPLLLKLDPWAEKLFLHSFSWEFECSECGYKYQERVTKTLPTFTNVIPD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646318  374 WHPLNAAHFGPCNSCNSKSQIRKMVLERASPILMLHFVEGLPRRDLQHYAFHFEGSLYQVTSVIQYQAN-NHFITWFLDA 452
Cdd:pfam15499 159 WHPLNAVHLGPCNSCSAKNQRRKMVLERVPPVFMLHFVEGLPHNDLQAYSFTFQGSQYSVTAVIQYQTHlKHFVTWIRNS 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 169646318  453 DGSWLECDDLKGPCAKRHVTCEVPASETHIVIWE 486
Cdd:pfam15499 239 DGSWLECDDLKGPYCRRHKRLEVPASEIHIVFWE 272
 
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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