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Conserved domains on  [gi|1010225905|ref|NP_001308463|]
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SUMO-specific isopeptidase USPL1 isoform 3 [Homo sapiens]

Protein Classification

Peptidase_C98 and DUF4650 domain-containing protein( domain architecture ID 11701092)

Peptidase_C98 and DUF4650 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF4650 pfam15509
Domain of unknown function (DUF4650); This family of vertebrate proteins lies to the ...
243-761 0e+00

Domain of unknown function (DUF4650); This family of vertebrate proteins lies to the C-terminus of Ubiquitin-specific peptidase-like protein family peptidase_C98, pfam15499. It might be acting as the exosite for the peptidase.


:

Pssm-ID: 464755 [Multi-domain]  Cd Length: 519  Bit Score: 778.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 243 LLSGPKGLVDN-ILPLTLEETiqktasvsQLNSEAFLLENKPVAENTGILKTNTLLSQESLMASSVSAPCNEKLIQDQFV 321
Cdd:pfam15509   1 LLSGLEGLVDDdILTLTLEEI--------QVDSEGFLLENKPVAENNGLVETNTLQSQESLLASSVSAPCEEKLTQDQFV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 322 DISFPSQVVNTNMQSVQLNTEDTVNTKSVNNTDATGLIQGVKSVEIEKDAQLKQFLTPKTEQLKPER-VTSQVSNLKKKE 400
Cdd:pfam15509  73 DLSFPSQNVSIDLQSVQLNTEDTVITVPVNDAHAADLVQGVKSVEIEKDAQLKQFLSPKTEKLKPEQnVTSQVSNLKKKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 401 TTADSQTTTSKSLQNQSLKENQKKPFVGSWVKGLISRGASFMPLCVSAHNRNTITDLQPSVKGVNNFGGFKTKGINQKAS 480
Cdd:pfam15509 153 TAADSQTVTASSLQNQSLKENQKKPFVGSWVKGLLSKGASFMPSCVSAHNRNKVTDLQPSVKGASNFGGFKTKGINQKAN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 481 HVSKKARKSASKPPPISKPPAGPPSSNGTAAHP--HAHAASEVLEKSGSTSCGAQLNHSSYGN--GISSANHEDLVEGQI 556
Cdd:pfam15509 233 QASKKARRSANKPPPLSNSPPSLLSSQNTAAHPhaTVNADSEVLKKSESLSQGASLNHNSHGNenGISSANHGDSVEDQT 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 557 HKLRLKLRKKLKAEKKKLAALMSSPQSRTVRSENLEQVPQDGSPNDCESIEDLLNELPYPIDIA-SESACTTVPGVSLYS 635
Cdd:pfam15509 313 HKLRLKLLKKLKAKKKKLAALMSSPQNGKLPSENLEHVSQCGSPNDCESLQDLLRELQYQIDIAdNKSGCTTVSGVSLYS 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 636 SQTHEEILAELLSPTPV-STELSENGEGDFRYLGMGDSHIPPPVPSEFNDVSQNTHLRQDHNYCSPTKKNPCEVQPDSLT 714
Cdd:pfam15509 393 SQTHEEILAELLSPTTVvSSELSENGEADFRYLEMGDNHIPAPVPSELNSVPQNTHLSQDHNYCSPVKKNQCEVQPDSLT 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1010225905 715 NNACVRTLNLESPMKTDIFDEFFSSSALNALANDTLDLPHFDEYLFE 761
Cdd:pfam15509 473 NNACVKTLNLESPMKTDIFDDFFSTSALNSLANDTLDLPHFDEYLFE 519
Peptidase_C98 super family cl21310
Ubiquitin-specific peptidase-like, SUMO isopeptidase; Peptidase_C98 is a small family of SUMO ...
1-169 9.77e-121

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.


The actual alignment was detected with superfamily member pfam15499:

Pssm-ID: 464750  Cd Length: 272  Bit Score: 363.17  E-value: 9.77e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905   1 MESPVFAFPLLLKLETHIEKLFLYSFSWDFECSQCGHQYQNRHMKSLVTFTNVIPEWHPLNAAHFGPCNNCNSKSQIRKM 80
Cdd:pfam15499 103 RESPVFALPLLLKLDPWAEKLFLHSFSWEFECSECGYKYQERVTKTLPTFTNVIPDWHPLNAVHLGPCNSCSAKNQRRKM 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905  81 VLEKVSPIFMLHFVEGLPQNDLQHYAFHFEGCLYQITSVIQYRAN-NHFITWILDADGSWLECDDLKGPCSERHKKFEVP 159
Cdd:pfam15499 183 VLERVPPVFMLHFVEGLPHNDLQAYSFTFQGSQYSVTAVIQYQTHlKHFVTWIRNSDGSWLECDDLKGPYCRRHKRLEVP 262
                         170
                  ....*....|
gi 1010225905 160 ASEIHIVIWE 169
Cdd:pfam15499 263 ASEIHIVFWE 272
 
Name Accession Description Interval E-value
DUF4650 pfam15509
Domain of unknown function (DUF4650); This family of vertebrate proteins lies to the ...
243-761 0e+00

Domain of unknown function (DUF4650); This family of vertebrate proteins lies to the C-terminus of Ubiquitin-specific peptidase-like protein family peptidase_C98, pfam15499. It might be acting as the exosite for the peptidase.


Pssm-ID: 464755 [Multi-domain]  Cd Length: 519  Bit Score: 778.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 243 LLSGPKGLVDN-ILPLTLEETiqktasvsQLNSEAFLLENKPVAENTGILKTNTLLSQESLMASSVSAPCNEKLIQDQFV 321
Cdd:pfam15509   1 LLSGLEGLVDDdILTLTLEEI--------QVDSEGFLLENKPVAENNGLVETNTLQSQESLLASSVSAPCEEKLTQDQFV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 322 DISFPSQVVNTNMQSVQLNTEDTVNTKSVNNTDATGLIQGVKSVEIEKDAQLKQFLTPKTEQLKPER-VTSQVSNLKKKE 400
Cdd:pfam15509  73 DLSFPSQNVSIDLQSVQLNTEDTVITVPVNDAHAADLVQGVKSVEIEKDAQLKQFLSPKTEKLKPEQnVTSQVSNLKKKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 401 TTADSQTTTSKSLQNQSLKENQKKPFVGSWVKGLISRGASFMPLCVSAHNRNTITDLQPSVKGVNNFGGFKTKGINQKAS 480
Cdd:pfam15509 153 TAADSQTVTASSLQNQSLKENQKKPFVGSWVKGLLSKGASFMPSCVSAHNRNKVTDLQPSVKGASNFGGFKTKGINQKAN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 481 HVSKKARKSASKPPPISKPPAGPPSSNGTAAHP--HAHAASEVLEKSGSTSCGAQLNHSSYGN--GISSANHEDLVEGQI 556
Cdd:pfam15509 233 QASKKARRSANKPPPLSNSPPSLLSSQNTAAHPhaTVNADSEVLKKSESLSQGASLNHNSHGNenGISSANHGDSVEDQT 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 557 HKLRLKLRKKLKAEKKKLAALMSSPQSRTVRSENLEQVPQDGSPNDCESIEDLLNELPYPIDIA-SESACTTVPGVSLYS 635
Cdd:pfam15509 313 HKLRLKLLKKLKAKKKKLAALMSSPQNGKLPSENLEHVSQCGSPNDCESLQDLLRELQYQIDIAdNKSGCTTVSGVSLYS 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 636 SQTHEEILAELLSPTPV-STELSENGEGDFRYLGMGDSHIPPPVPSEFNDVSQNTHLRQDHNYCSPTKKNPCEVQPDSLT 714
Cdd:pfam15509 393 SQTHEEILAELLSPTTVvSSELSENGEADFRYLEMGDNHIPAPVPSELNSVPQNTHLSQDHNYCSPVKKNQCEVQPDSLT 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1010225905 715 NNACVRTLNLESPMKTDIFDEFFSSSALNALANDTLDLPHFDEYLFE 761
Cdd:pfam15509 473 NNACVKTLNLESPMKTDIFDDFFSTSALNSLANDTLDLPHFDEYLFE 519
Peptidase_C98 pfam15499
Ubiquitin-specific peptidase-like, SUMO isopeptidase; Peptidase_C98 is a small family of SUMO ...
1-169 9.77e-121

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: 363.17  E-value: 9.77e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905   1 MESPVFAFPLLLKLETHIEKLFLYSFSWDFECSQCGHQYQNRHMKSLVTFTNVIPEWHPLNAAHFGPCNNCNSKSQIRKM 80
Cdd:pfam15499 103 RESPVFALPLLLKLDPWAEKLFLHSFSWEFECSECGYKYQERVTKTLPTFTNVIPDWHPLNAVHLGPCNSCSAKNQRRKM 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905  81 VLEKVSPIFMLHFVEGLPQNDLQHYAFHFEGCLYQITSVIQYRAN-NHFITWILDADGSWLECDDLKGPCSERHKKFEVP 159
Cdd:pfam15499 183 VLERVPPVFMLHFVEGLPHNDLQAYSFTFQGSQYSVTAVIQYQTHlKHFVTWIRNSDGSWLECDDLKGPYCRRHKRLEVP 262
                         170
                  ....*....|
gi 1010225905 160 ASEIHIVIWE 169
Cdd:pfam15499 263 ASEIHIVFWE 272
 
Name Accession Description Interval E-value
DUF4650 pfam15509
Domain of unknown function (DUF4650); This family of vertebrate proteins lies to the ...
243-761 0e+00

Domain of unknown function (DUF4650); This family of vertebrate proteins lies to the C-terminus of Ubiquitin-specific peptidase-like protein family peptidase_C98, pfam15499. It might be acting as the exosite for the peptidase.


Pssm-ID: 464755 [Multi-domain]  Cd Length: 519  Bit Score: 778.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 243 LLSGPKGLVDN-ILPLTLEETiqktasvsQLNSEAFLLENKPVAENTGILKTNTLLSQESLMASSVSAPCNEKLIQDQFV 321
Cdd:pfam15509   1 LLSGLEGLVDDdILTLTLEEI--------QVDSEGFLLENKPVAENNGLVETNTLQSQESLLASSVSAPCEEKLTQDQFV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 322 DISFPSQVVNTNMQSVQLNTEDTVNTKSVNNTDATGLIQGVKSVEIEKDAQLKQFLTPKTEQLKPER-VTSQVSNLKKKE 400
Cdd:pfam15509  73 DLSFPSQNVSIDLQSVQLNTEDTVITVPVNDAHAADLVQGVKSVEIEKDAQLKQFLSPKTEKLKPEQnVTSQVSNLKKKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 401 TTADSQTTTSKSLQNQSLKENQKKPFVGSWVKGLISRGASFMPLCVSAHNRNTITDLQPSVKGVNNFGGFKTKGINQKAS 480
Cdd:pfam15509 153 TAADSQTVTASSLQNQSLKENQKKPFVGSWVKGLLSKGASFMPSCVSAHNRNKVTDLQPSVKGASNFGGFKTKGINQKAN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 481 HVSKKARKSASKPPPISKPPAGPPSSNGTAAHP--HAHAASEVLEKSGSTSCGAQLNHSSYGN--GISSANHEDLVEGQI 556
Cdd:pfam15509 233 QASKKARRSANKPPPLSNSPPSLLSSQNTAAHPhaTVNADSEVLKKSESLSQGASLNHNSHGNenGISSANHGDSVEDQT 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 557 HKLRLKLRKKLKAEKKKLAALMSSPQSRTVRSENLEQVPQDGSPNDCESIEDLLNELPYPIDIA-SESACTTVPGVSLYS 635
Cdd:pfam15509 313 HKLRLKLLKKLKAKKKKLAALMSSPQNGKLPSENLEHVSQCGSPNDCESLQDLLRELQYQIDIAdNKSGCTTVSGVSLYS 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905 636 SQTHEEILAELLSPTPV-STELSENGEGDFRYLGMGDSHIPPPVPSEFNDVSQNTHLRQDHNYCSPTKKNPCEVQPDSLT 714
Cdd:pfam15509 393 SQTHEEILAELLSPTTVvSSELSENGEADFRYLEMGDNHIPAPVPSELNSVPQNTHLSQDHNYCSPVKKNQCEVQPDSLT 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1010225905 715 NNACVRTLNLESPMKTDIFDEFFSSSALNALANDTLDLPHFDEYLFE 761
Cdd:pfam15509 473 NNACVKTLNLESPMKTDIFDDFFSTSALNSLANDTLDLPHFDEYLFE 519
Peptidase_C98 pfam15499
Ubiquitin-specific peptidase-like, SUMO isopeptidase; Peptidase_C98 is a small family of SUMO ...
1-169 9.77e-121

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: 363.17  E-value: 9.77e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905   1 MESPVFAFPLLLKLETHIEKLFLYSFSWDFECSQCGHQYQNRHMKSLVTFTNVIPEWHPLNAAHFGPCNNCNSKSQIRKM 80
Cdd:pfam15499 103 RESPVFALPLLLKLDPWAEKLFLHSFSWEFECSECGYKYQERVTKTLPTFTNVIPDWHPLNAVHLGPCNSCSAKNQRRKM 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010225905  81 VLEKVSPIFMLHFVEGLPQNDLQHYAFHFEGCLYQITSVIQYRAN-NHFITWILDADGSWLECDDLKGPCSERHKKFEVP 159
Cdd:pfam15499 183 VLERVPPVFMLHFVEGLPHNDLQAYSFTFQGSQYSVTAVIQYQTHlKHFVTWIRNSDGSWLECDDLKGPYCRRHKRLEVP 262
                         170
                  ....*....|
gi 1010225905 160 ASEIHIVIWE 169
Cdd:pfam15499 263 ASEIHIVFWE 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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