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Conserved domains on  [gi|299788311|gb|AAS54496|]
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AGR007Cp [Eremothecium gossypii ATCC 10895]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 10119323)

ubiquitin carboxyl-terminal hydrolase family protein is a C19 family peptidase that may deubiquitinate polyubiquitinated target proteins

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0004843
MEROPS:  C19
PubMed:  7845226|11517925
SCOP:  4003158

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
65-493 0e+00

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


:

Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 560.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311  65 LLQTIEKKRLDFYSEKVCSVTLSTIDVYSCLTCGKYLQGRNEGSPAFKHSIEDLHRLFMHMRTFKTYILPENRPFrNAEV 144
Cdd:cd02669    2 YLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEI-IDSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 145 LDQIRYGFKPTYGRLQVADFPQDCE---DLNGQPYLNGFVGLHNISNNGSSNVILLMLAHIKPVRD---LFLLNDDLLER 218
Cdd:cd02669   81 LDDIKYVLNPTYTKEQISDLDRDPKlsrDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNfflLYENYENIKDR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 219 ADPFINKLALLIRHIWSPNLFRRHVSPHEFLQYVATHLAQPSSMKAYSDPRNFMLFVINRMLKSSCG---EVRKTLTDNI 295
Cdd:cd02669  161 KSELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGskkPNSSIIHDCF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 296 QGTVTIRTTKIVPVPNDDGSAIKFVLDTRTAKSTDVMFWMLSLDLPPRPLFKDGKSANSLPQVKLEELMGKFDGTVEQHL 375
Cdd:cd02669  241 QGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGKTETEL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 376 KESVKLNKVSRCPRYLVLHLKRFEPGKFpVQERNQTVVEFGQELE-------------FRSVKFRLLMNVVHEATKPakn 442
Cdd:cd02669  321 KDSLKRYLISRLPKYLIFHIKRFSKNNF-FKEKNPTIVNFPIKNLdlsdyvhfdkpslNLSTKYNLVANIVHEGTPQ--- 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 299788311 443 qevpildEISNWKIQIRNDKDDTWFELDEGNVRKREKELLFLNETYLQVWE 493
Cdd:cd02669  397 -------EDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
 
Name Accession Description Interval E-value
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
65-493 0e+00

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 560.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311  65 LLQTIEKKRLDFYSEKVCSVTLSTIDVYSCLTCGKYLQGRNEGSPAFKHSIEDLHRLFMHMRTFKTYILPENRPFrNAEV 144
Cdd:cd02669    2 YLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEI-IDSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 145 LDQIRYGFKPTYGRLQVADFPQDCE---DLNGQPYLNGFVGLHNISNNGSSNVILLMLAHIKPVRD---LFLLNDDLLER 218
Cdd:cd02669   81 LDDIKYVLNPTYTKEQISDLDRDPKlsrDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNfflLYENYENIKDR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 219 ADPFINKLALLIRHIWSPNLFRRHVSPHEFLQYVATHLAQPSSMKAYSDPRNFMLFVINRMLKSSCG---EVRKTLTDNI 295
Cdd:cd02669  161 KSELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGskkPNSSIIHDCF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 296 QGTVTIRTTKIVPVPNDDGSAIKFVLDTRTAKSTDVMFWMLSLDLPPRPLFKDGKSANSLPQVKLEELMGKFDGTVEQHL 375
Cdd:cd02669  241 QGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGKTETEL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 376 KESVKLNKVSRCPRYLVLHLKRFEPGKFpVQERNQTVVEFGQELE-------------FRSVKFRLLMNVVHEATKPakn 442
Cdd:cd02669  321 KDSLKRYLISRLPKYLIFHIKRFSKNNF-FKEKNPTIVNFPIKNLdlsdyvhfdkpslNLSTKYNLVANIVHEGTPQ--- 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 299788311 443 qevpildEISNWKIQIRNDKDDTWFELDEGNVRKREKELLFLNETYLQVWE 493
Cdd:cd02669  397 -------EDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
82-136 2.85e-12

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 61.51  E-value: 2.85e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 299788311   82 CSVTLSTIDVYSCLTCGKYLQGRNEGSPAFKHSIEDLHRLFMHMRTFKTYILPEN 136
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCD 55
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
82-127 4.21e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 52.37  E-value: 4.21e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 299788311    82 CSVTLSTIDVYSCLTCGKYLQGRNEGSPAFKHSIEDLHRLFMHMRT 127
Cdd:smart00290   2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGT 47
 
Name Accession Description Interval E-value
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
65-493 0e+00

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 560.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311  65 LLQTIEKKRLDFYSEKVCSVTLSTIDVYSCLTCGKYLQGRNEGSPAFKHSIEDLHRLFMHMRTFKTYILPENRPFrNAEV 144
Cdd:cd02669    2 YLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEI-IDSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 145 LDQIRYGFKPTYGRLQVADFPQDCE---DLNGQPYLNGFVGLHNISNNGSSNVILLMLAHIKPVRD---LFLLNDDLLER 218
Cdd:cd02669   81 LDDIKYVLNPTYTKEQISDLDRDPKlsrDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNfflLYENYENIKDR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 219 ADPFINKLALLIRHIWSPNLFRRHVSPHEFLQYVATHLAQPSSMKAYSDPRNFMLFVINRMLKSSCG---EVRKTLTDNI 295
Cdd:cd02669  161 KSELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGskkPNSSIIHDCF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 296 QGTVTIRTTKIVPVPNDDGSAIKFVLDTRTAKSTDVMFWMLSLDLPPRPLFKDGKSANSLPQVKLEELMGKFDGTVEQHL 375
Cdd:cd02669  241 QGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGKTETEL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 376 KESVKLNKVSRCPRYLVLHLKRFEPGKFpVQERNQTVVEFGQELE-------------FRSVKFRLLMNVVHEATKPakn 442
Cdd:cd02669  321 KDSLKRYLISRLPKYLIFHIKRFSKNNF-FKEKNPTIVNFPIKNLdlsdyvhfdkpslNLSTKYNLVANIVHEGTPQ--- 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 299788311 443 qevpildEISNWKIQIRNDKDDTWFELDEGNVRKREKELLFLNETYLQVWE 493
Cdd:cd02669  397 -------EDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
267-493 8.08e-14

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 71.36  E-value: 8.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 267 DPRNFMLFVINRMLKSSCGEVRKT---------LTDNIQGTVTIRTTKivpvpnddgsaikfvLDTRTAKSTDVMFWMLS 337
Cdd:cd02257   24 DAHEFLLFLLDKLHEELKKSSKRTsdssslkslIHDLFGGKLESTIVC---------------LECGHESVSTEPELFLS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 338 LDLPPRPLfkdgksanslPQVKLEELMGKFDGTVE-----------QHLKESVKLNKVSRCPRYLVLHLKRFEPGKFPVQ 406
Cdd:cd02257   89 LPLPVKGL----------PQVSLEDCLEKFFKEEIlegdncykcekKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 407 ERNQTVVEFGQEL---------------EFRSVKFRLLMNVVHEATkpaknqevpiLDEISNWKIQIRNDKDDTWFELDE 471
Cdd:cd02257  159 EKLNTKVSFPLELdlspylsegekdsdsDNGSYKYELVAVVVHSGT----------SADSGHYVAYVKDPSDGKWYKFND 228
                        250       260
                 ....*....|....*....|....*..
gi 299788311 472 GNVRKREKELLFL-----NETYLQVWE 493
Cdd:cd02257  229 DKVTEVSEEEVLEfgslsSSAYILFYE 255
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
82-136 2.85e-12

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 61.51  E-value: 2.85e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 299788311   82 CSVTLSTIDVYSCLTCGKYLQGRNEGSPAFKHSIEDLHRLFMHMRTFKTYILPEN 136
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCD 55
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
181-419 1.17e-10

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 62.46  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311  181 VGLHNISNNGSSNVILLMLAHIKPVRD--LFLLNDDLLERADPFINK---LALLIRHIWSPNLfRRHVSPHEFLQyVATH 255
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDylLRISPLSEDSRYNKDINLlcaLRDLFKALQKNSK-SSSVSPKMFKK-SLGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311  256 LAQPSSMKAYSDPRNFMLFVINR----MLKSSCGEVRKTLTDNIQGTVTIRTTkivpvpnddgsaikfVLDTRTAKSTDV 331
Cdd:pfam00443  79 LNPDFSGYKQQDAQEFLLFLLDGlhedLNGNHSTENESLITDLFRGQLKSRLK---------------CLSCGEVSETFE 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311  332 MFWMLSLDLPP--RPLFKDGKSANSLPQVKLEELMGKFDGTVEQ--HLKESVKLNKVSRCPRYLVLHLKRFEPGKFpVQE 407
Cdd:pfam00443 144 PFSDLSLPIPGdsAELKTASLQICFLQFSKLEELDDEEKYYCDKcgCKQDAIKQLKISRLPPVLIIHLKRFSYNRS-TWE 222
                         250
                  ....*....|..
gi 299788311  408 RNQTVVEFGQEL 419
Cdd:pfam00443 223 KLNTEVEFPLEL 234
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
82-127 4.21e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 52.37  E-value: 4.21e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 299788311    82 CSVTLSTIDVYSCLTCGKYLQGRNEGSPAFKHSIEDLHRLFMHMRT 127
Cdd:smart00290   2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGT 47
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
317-415 3.13e-03

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 39.19  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788311 317 IKFVLDTRTAKSTDVM---FWMLSLDLPprplfkdgKSANSLPQVKLEELMGKFdgTVEQHL--------------KESV 379
Cdd:cd02674   48 LKSRLTCLTCGKTSTTfepFTYLSLPIP--------SGSGDAPKVTLEDCLRLF--TKEETLdgdnawkcpkckkkRKAT 117
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 299788311 380 KLNKVSRCPRYLVLHLKRFEPgKFPVQERNQTVVEF 415
Cdd:cd02674  118 KKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTF 152
 
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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