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Conserved domains on  [gi|1993917542|ref|XP_039628759|]
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ubiquitin carboxyl-terminal hydrolase 8 isoform X2 [Polypterus senegalus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1069 9.40e-114

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: 351.20  E-value: 9.40e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNtprlaeyfnknyyqedinrsnilghkgevaeefgvimkalwsgqyrfisprdfkftigki 819
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  820 ndqfsgfDQQDSQELLLFLMDGLHedlnkadnrkrykeetndhlddykaadlawskhkmlneSIIVALFQGQFKSTVQCL 899
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  900 TCHKKSRTFEAFMYLSLPLASS----NKCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKR 975
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGsgdaPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  976 FSYDGRWKQKLQTSVDFPLENLDLSQYVIGP-KSNLKKYSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDHEVSDIS 1054
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1993917542 1055 TSSVKSSAAYILFYT 1069
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
736-923 1.32e-55

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 208.20  E-value: 1.32e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  736 AALTGLRNLGNTCYMNSILQCLCNTPRLAEYFNKNYYQEDINRSNILGHKGEVAEEFGVIMKALWSGQYRFISPRDFKFT 815
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  816 IGKINDQFSGFDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEETN----DHLDDYKAADLAWSKHKMLNESIIVALFQGQ 891
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKPDlspgDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1993917542  892 FKSTVQCLTCHKKSRTFEAFMYLSLPLASSNK 923
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 8-116 1.13e-31

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


:

Pssm-ID: 462647  Cd Length: 113  Bit Score: 119.71  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542    8 LKELYLSTSLGELNKKAEVKPD--KISTRSYVQSACKIFKAAEECRLDRDEEKAYVFYMKFLSVYDLIKKRPDFKQQQDY 85
Cdd:pfam08969    3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1993917542   86 VMSMLGPTSFKKAIEEAEKLSDSLKLRYEEA 116
Cdd:pfam08969   83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 202-311 3.48e-03

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


The actual alignment was detected with superfamily member pfam00581:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 92  Bit Score: 37.85  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  202 VIIMDARSQKDYQESQIqvptQKIISVPEDIIkpgitvnQIEANLPSESREQWKKRGLADYVVLLDWFSSAKDLklgtTL 281
Cdd:pfam00581    6 VVLIDVRPPEEYAKGHI----PGAVNVPLSSL-------SLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1993917542  282 QSLKDALFKwdsqtilrsEPLVLEGGYESW 311
Cdd:pfam00581   71 ALLKALGYK---------NVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1069 9.40e-114

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: 351.20  E-value: 9.40e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNtprlaeyfnknyyqedinrsnilghkgevaeefgvimkalwsgqyrfisprdfkftigki 819
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  820 ndqfsgfDQQDSQELLLFLMDGLHedlnkadnrkrykeetndhlddykaadlawskhkmlneSIIVALFQGQFKSTVQCL 899
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  900 TCHKKSRTFEAFMYLSLPLASS----NKCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKR 975
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGsgdaPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  976 FSYDGRWKQKLQTSVDFPLENLDLSQYVIGP-KSNLKKYSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDHEVSDIS 1054
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1993917542 1055 TSSVKSSAAYILFYT 1069
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
739-1068 3.24e-112

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 350.59  E-value: 3.24e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  739 TGLRNLGNTCYMNSILQCLCNTPRLAEYFNKNYYQEDINRSNILGHkgeVAEEFGVIMKALWSG-QYRFISPRDFKFTIG 817
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  818 KINDQFSGFDQQDSQELLLFLMDGLHEDLNkadnrkrykeetndhlddykaadlawSKHKMLNESIIVALFQGQFKSTVQ 897
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  898 CLTCHKKSRTFEAFMYLSLPLASSNKCS----LQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHL 973
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELktasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  974 KRFSYDGRWKQKLQTSVDFPLEnLDLSQYVIGPK----SNLKKYSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDHE 1049
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELkpktNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 1993917542 1050 VSDISTS-SVKSSAAYILFY 1068
Cdd:pfam00443  291 VTEVDEEtAVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
736-923 1.32e-55

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 208.20  E-value: 1.32e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  736 AALTGLRNLGNTCYMNSILQCLCNTPRLAEYFNKNYYQEDINRSNILGHKGEVAEEFGVIMKALWSGQYRFISPRDFKFT 815
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  816 IGKINDQFSGFDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEETN----DHLDDYKAADLAWSKHKMLNESIIVALFQGQ 891
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKPDlspgDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1993917542  892 FKSTVQCLTCHKKSRTFEAFMYLSLPLASSNK 923
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 8-116 1.13e-31

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


Pssm-ID: 462647  Cd Length: 113  Bit Score: 119.71  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542    8 LKELYLSTSLGELNKKAEVKPD--KISTRSYVQSACKIFKAAEECRLDRDEEKAYVFYMKFLSVYDLIKKRPDFKQQQDY 85
Cdd:pfam08969    3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1993917542   86 VMSMLGPTSFKKAIEEAEKLSDSLKLRYEEA 116
Cdd:pfam08969   83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
740-1068 1.94e-26

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 110.28  E-value: 1.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLC-NTPRLAEY-----FNKNYYQEDINRSnilgHKGEVAEEFGVIMKALWSGQyrfisprdfK 813
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKLDELlddlsKELKVLKNVIRKP----EPDLNQEEALKLFTALWSSK---------E 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  814 FTIGKINDQFSgfdQQDSQELLLFLMDGLHEDLNKADNRkRYKEETNDHLDDYKAadlAWSkhkmlneSIIVALFQGQF- 892
Cdd:COG5533     68 HKVGWIPPMGS---QEDAHELLGKLLDELKLDLVNSFTI-RIFKTTKDKKKTSTG---DWF-------DIIIELPDQTWv 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  893 --KSTVQCltchkksrTFEAFMYLslplaSSNKCSLQeclklfskeEKLTDNNKVLcshCKTRRDSTKKieiwKLPPILL 970
Cdd:COG5533    134 nnLKTLQE--------FIDNMEEL-----VDDETGVK---------AKENEELEVQ---AKQEYEVSFV----KLPKILT 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  971 VHLKRFSYDGRwKQKLQTSVDfplENLDLSqYVIGPKSNLKK---YSLYGVSNHYGGLDGGHYTAYCKnaIKQRWHKFDD 1047
Cdd:COG5533    185 IQLKRFANLGG-NQKIDTEVD---EKFELP-VKHDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKAND 257

                          330       340
                   ....*....|....*....|....
gi 1993917542 1048 HEVSDISTS---SVKSSAAYILFY 1068
Cdd:COG5533    258 SDVTPVSEEeaiNEKAKNAYLYFY 281
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 202-311 3.48e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 37.85  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  202 VIIMDARSQKDYQESQIqvptQKIISVPEDIIkpgitvnQIEANLPSESREQWKKRGLADYVVLLDWFSSAKDLklgtTL 281
Cdd:pfam00581    6 VVLIDVRPPEEYAKGHI----PGAVNVPLSSL-------SLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1993917542  282 QSLKDALFKwdsqtilrsEPLVLEGGYESW 311
Cdd:pfam00581   71 ALLKALGYK---------NVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1069 9.40e-114

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: 351.20  E-value: 9.40e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNtprlaeyfnknyyqedinrsnilghkgevaeefgvimkalwsgqyrfisprdfkftigki 819
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  820 ndqfsgfDQQDSQELLLFLMDGLHedlnkadnrkrykeetndhlddykaadlawskhkmlneSIIVALFQGQFKSTVQCL 899
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  900 TCHKKSRTFEAFMYLSLPLASS----NKCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKR 975
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGsgdaPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  976 FSYDGRWKQKLQTSVDFPLENLDLSQYVIGP-KSNLKKYSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDHEVSDIS 1054
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1993917542 1055 TSSVKSSAAYILFYT 1069
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
739-1068 3.24e-112

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 350.59  E-value: 3.24e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  739 TGLRNLGNTCYMNSILQCLCNTPRLAEYFNKNYYQEDINRSNILGHkgeVAEEFGVIMKALWSG-QYRFISPRDFKFTIG 817
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  818 KINDQFSGFDQQDSQELLLFLMDGLHEDLNkadnrkrykeetndhlddykaadlawSKHKMLNESIIVALFQGQFKSTVQ 897
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  898 CLTCHKKSRTFEAFMYLSLPLASSNKCS----LQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHL 973
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELktasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  974 KRFSYDGRWKQKLQTSVDFPLEnLDLSQYVIGPK----SNLKKYSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDHE 1049
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELkpktNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 1993917542 1050 VSDISTS-SVKSSAAYILFY 1068
Cdd:pfam00443  291 VTEVDEEtAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 740-1068 2.12e-74

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: 246.24  E-value: 2.12e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNtprlaeyfnknyyqedinrsnilghkgevaeefgvimkalwsgqyrfisprdfkftigki 819
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  820 ndqfsgfDQQDSQELLLFLMDGLHEDLNKADNRKRYKEEtndhlddykaadlawskhkmlNESIIVALFQGQFKSTVQCL 899
Cdd:cd02257     21 -------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSS---------------------LKSLIHDLFGGKLESTIVCL 72

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  900 TCHKKSRTFEAFMYLSLPL--ASSNKCSLQECLKLFSKEEKLTDNNKVLCSHCKtRRDSTKKIEIWKLPPILLVHLKRFS 977
Cdd:cd02257     73 ECGHESVSTEPELFLSLPLpvKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFS 151

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  978 YDGRW-KQKLQTSVDFPLEnLDLSQYVIGPKS------NLKKYSLYGVSNHYGGL-DGGHYTAYCKNAIKQRWHKFDDHE 1049
Cdd:cd02257    152 FNEDGtKEKLNTKVSFPLE-LDLSPYLSEGEKdsdsdnGSYKYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDK 230

                          330       340
                   ....*....|....*....|....
gi 1993917542 1050 VSDISTSSV-----KSSAAYILFY 1068
Cdd:cd02257    231 VTEVSEEEVlefgsLSSSAYILFY 254
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 739-1068 1.86e-69

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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 234.48  E-value: 1.86e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  739 TGLRNLGNTCYMNSILQCLCNTPRLAEYFNKNYYQEDINRsnilghkgevaEEFGV-------IMKALWSGQYrFISPRD 811
Cdd:cd02661      2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN-----------EGFCMmcaleahVERALASSGP-GSAPRI 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  812 FKFTIGKINDQFSGFDQQDSQELLLFLMDGLHedlnKADNRKRYKEETNDHLddykaadlawSKHKMLNESIivalFQGQ 891
Cdd:cd02661     70 FSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPS----------SQETTLVQQI----FGGY 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  892 FKSTVQCLTCHKKSRTFEAFMYLSLPLASSNkcSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLV 971
Cdd:cd02661    132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTI 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  972 HLKRFSYDGRwkQKLQTSVDFPlENLDLSQYVIGPKSNLKKYSLYGVSNHYGG-LDGGHYTAYCKNAIKqRWHKFDDHEV 1050
Cdd:cd02661    210 HLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNG-KWYNMDDSKV 285

                          330
                   ....*....|....*...
gi 1993917542 1051 SDISTSSVKSSAAYILFY 1068
Cdd:cd02661    286 SPVSIETVLSQKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1069 7.70e-64

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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 219.55  E-value: 7.70e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNTPRLAEYF--NKNYYQEDINRSN--ILGHKGEVAEEFgvimkaLWSGQYRFISPRDFKFT 815
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFlsDRHSCTCLSCSPNscLSCAMDEIFQEF------YYSGDRSPYGPINLLYL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  816 IGKINDQFSGFDQQDSQELLLFLMDGLHEDLnkadnrKRYKEETNDHLDdykaadlawskhkmlNESIIVALFQGQFKST 895
Cdd:cd02660     76 SWKHSRNLAGYSQQDAHEFFQFLLDQLHTHY------GGDKNEANDESH---------------CNCIIHQTFSGSLQSS 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  896 VQCLTCHKKSRTFEAFMYLSLPLASSNKCS-------------LQECLKLFSKEEKLTDNNkVLCSHCKTRRDSTKKIEI 962
Cdd:cd02660    135 VTCQRCGGVSTTVDPFLDLSLDIPNKSTPSwalgesgvsgtptLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSI 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  963 WKLPPILLVHLKRFSYD-GRWKQKLQTSVDFPLEnLDLSQYVIG---------PKSNLKKYSLYGVSNHYGGLDGGHYTA 1032
Cdd:cd02660    214 KKLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSsigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTA 292

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1993917542 1033 YCKNAIKQrWHKFDDHEVSDISTSSVKSSAAYILFYT 1069
Cdd:cd02660    293 YCRQGDGQ-WFKFDDAMITRVSEEEVLKSQAYLLFYH 328
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1068 1.54e-58

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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 203.00  E-value: 1.54e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNTPRLAEYFNKNyyqedinrsnilghkgevaeefgvimkalwsgqyrfisPRDFKFTIGKI 819
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  820 NDQFSGFDQQDSQELLLFLMDGLhedlnkadnrkrykeetndhlddykaadlawskhkmlnESIIVALFQGQFKSTVQCL 899
Cdd:cd02667     43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  900 TCHKKSRTFEAFMYLSLPLASSNK--CSLQECLKLFSKEEKLTDNNKVLCSHCKtrrDSTKKIEIWKLPPILLVHLKRFS 977
Cdd:cd02667     85 SCGTVSLVYEPFLDLSLPRSDEIKseCSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  978 YDGRWK-QKLQTSVDFPlENLDLSQYViGPKSNLK------KYSLYGVSNHYGGLDGGHYTAYCK--------------- 1035
Cdd:cd02667    162 QPRSANlRKVSRHVSFP-EILDLAPFC-DPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltksk 239

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1993917542 1036 ------NAIKQRWHKFDDHEVSDISTSSVKSSAAYILFY 1068
Cdd:cd02667    240 paadeaGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
736-923 1.32e-55

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 208.20  E-value: 1.32e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  736 AALTGLRNLGNTCYMNSILQCLCNTPRLAEYFNKNYYQEDINRSNILGHKGEVAEEFGVIMKALWSGQYRFISPRDFKFT 815
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  816 IGKINDQFSGFDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEETN----DHLDDYKAADLAWSKHKMLNESIIVALFQGQ 891
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKPDlspgDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1993917542  892 FKSTVQCLTCHKKSRTFEAFMYLSLPLASSNK 923
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1068 7.79e-48

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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 173.98  E-value: 7.79e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNTP--RLAEYFNKNYYQEDINRSNILghkgevaeEFGVIMKALWSGQYRFISPRDFKFTIG 817
Cdd:cd02659      4 GLKNQGATCYMNSLLQQLYMTPefRNAVYSIPPTEDDDDNKSVPL--------ALQRLFLFLQLSESPVKTTELTDKTRS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  818 KINDQFSGFDQQDSQELLLFLMDGLHEDLnkadnrkrykeetndhlddyKAADLawskhkmlnESIIVALFQGQFKSTVQ 897
Cdd:cd02659     76 FGWDSLNTFEQHDVQEFFRVLFDKLEEKL--------------------KGTGQ---------EGLIKNLFGGKLVNYII 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  898 CLTCHKKSRTFEAFmyLSLPLASSNKCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKRFS 977
Cdd:cd02659    127 CKECPHESEREEYF--LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFE 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  978 YDGR--WKQKLQTSVDFPLEnLDLSQYVI-----GPKSNLKK------YSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHK 1044
Cdd:cd02659    205 FDFEtmMRIKINDRFEFPLE-LDMEPYTEkglakKEGDSEKKdsesyiYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYK 283

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1993917542 1045 FDDHEVSDISTSSV----------------------KSSAAYILFY 1068
Cdd:cd02659    284 FNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFY 329
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1069 2.32e-47

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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 172.22  E-value: 2.32e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCL------------CNTPRLAEYFNKNyyqedinrSNILGHKGEVAEEFGVIMKALWSGQYRFI 807
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWfmnlefrkavyeCNSTEDAELKNMP--------PDKPHEPQTIIDQLQLIFAQLQFGNRSVV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  808 SPRDFKFTIGKINDQfsgfdQQDSQELLLFLMDGLHEDLNKADNRKrykeetndhlddykaadlawskhkmlNESIIVAL 887
Cdd:cd02668     73 DPSGFVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPD--------------------------LKNIVQDL 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  888 FQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASSNKcsLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPP 967
Cdd:cd02668    122 FRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT--LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPP 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  968 ILLVHLKRFSYD--GRWKQKLQTSVDFPlENLDLSQYVIGPKSNLKKYSLYGVSNHYG-GLDGGHYTAYCKNAIKQRWHK 1044
Cdd:cd02668    200 TLNFQLLRFVFDrkTGAKKKLNASISFP-EILDMGEYLAESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYK 278

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1993917542 1045 FDDHEVSDISTSSVK---------------------SSAAYILFYT 1069
Cdd:cd02668    279 FNDEDVEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1069 4.49e-47

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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 170.57  E-value: 4.49e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLcntprlaeYFNKNYYQedinrsnilghkgevaeeFGVIMKALWSGQYRF--ISPRDFKFTIG 817
Cdd:cd02663      1 GLENFGNTCYCNSVLQAL--------YFENLLTC------------------LKDLFESISEQKKRTgvISPKKFITRLK 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  818 KINDQFSGFDQQDSQELLLFLMDGLHEDLNKAdnRKRYKEETNDHLDDYKAADLAWskhkmlnesiIVALFQGQFKSTVQ 897
Cdd:cd02663     55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAE--RKAEKANRKLNNNNNAEPQPTW----------VHEIFQGILTNETR 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  898 CLTCHKKSRTFEAFMYLSLPLasSNKCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKRFS 977
Cdd:cd02663    123 CLTCETVSSRDETFLDLSIDV--EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFK 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  978 YDGRWKQ--KLQTSVDFPLEnLDLSQYVIGPKSNLKKYSLYGVSNHYG-GLDGGHYTAYCKnaIKQRWHKFDDHEVSDIS 1054
Cdd:cd02663    201 YDEQLNRyiKLFYRVVFPLE-LRLFNTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVK--SHGGWLLFDDETVEKID 277

                          330       340
                   ....*....|....*....|...
gi 1993917542 1055 TSSV-------KSSA-AYILFYT 1069
Cdd:cd02663    278 ENAVeeffgdsPNQAtAYVLFYQ 300
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1068 4.30e-33

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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 131.07  E-value: 4.30e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLcntprlaeyFNKNYYQEDINRSNILGHKGEVAEEFGVIM-KALWSGQYRFISPRDFKFTIGK 818
Cdd:cd02664      1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKLQLlQAHLMHTQRRAEAPPDYFLEAS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  819 INDQFSGFDQQDSQELLLFLMDGLHedlnkadnrkrykeetndhlddykaadlawskhkmlneSIIVALFQGQFKSTVQC 898
Cdd:cd02664     72 RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRC 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  899 LTCHKKSRTFEAFMYLSLPLassnkCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKRFSY 978
Cdd:cd02664    114 LNCNSTSARTERFRDLDLSF-----PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSY 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  979 D--GRWKQKLQTSVDFPlENLDLSQYVIGPKSNLKK-------------------YSLYGVSNHYG-GLDGGHYTAYCKN 1036
Cdd:cd02664    189 DqkTHVREKIMDNVSIN-EVLSLPVRVESKSSESPLekkeeesgddgelvtrqvhYRLYAVVVHSGySSESGHYFTYARD 267

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1993917542 1037 --------------------AIKQRWHKFDDHEVSDISTSSVK-------SSAAYILFY 1068
Cdd:cd02664    268 qtdadstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 8-116 1.13e-31

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


Pssm-ID: 462647  Cd Length: 113  Bit Score: 119.71  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542    8 LKELYLSTSLGELNKKAEVKPD--KISTRSYVQSACKIFKAAEECRLDRDEEKAYVFYMKFLSVYDLIKKRPDFKQQQDY 85
Cdd:pfam08969    3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1993917542   86 VMSMLGPTSFKKAIEEAEKLSDSLKLRYEEA 116
Cdd:pfam08969   83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1068 1.36e-31

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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 126.28  E-value: 1.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNTPRLAEYFN--KNYYQEDIN--RSNILGHKGEVAeefgvimKALWSGQYRF--------- 806
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDdlENKFPSDVVdpANDLNCQLIKLA-------DGLLSGRYSKpaslksend 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  807 -----ISPRDFKFTIGKINDQFSGFDQQDSQELLLFLMDglhedlnKADNRKRYKEETNdhlddykaadlawskhkmLNE 881
Cdd:cd02658     74 pyqvgIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLN------------------PND 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  882 siivaLFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASSNKC------------SLQECLKLFSKEEKLTDNnkvlCSH 949
Cdd:cd02658    129 -----LFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATekeegelvyepvPLEDCLKAYFAPETIEDF----CST 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  950 CKTRRDSTKKIEIWKLPPILLVHLKRFSYDGRWKQ-KLQTSVDFPlenldlsqYVIGPksnlKKYSLYGVSNHYG-GLDG 1027
Cdd:cd02658    200 CKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDVP--------EELGP----GKYELIAFISHKGtSVHS 267

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1993917542 1028 GHYTAYCKNAI--KQRWHKFDDHEVSDISTSSVKSSAAYILFY 1068
Cdd:cd02658    268 GHYVAHIKKEIdgEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1068 7.33e-31

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 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: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 123.98  E-value: 7.33e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNTPRLAEYFnKNYyqeDINRSNILGHKGEVAEEFGVIMKALWSGQYRfISPRDFKFTIGKI 819
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-KNY---NPARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLLRMA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  820 NDQFS------GFDQQDSQELLLFLMDGLHEDLNKADnrkrykeetndhlddykaadlawskhkmLNESIIVALFQGQFK 893
Cdd:cd02657     76 FPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAG----------------------------SKGSFIDQLFGIELE 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  894 STVQCL-TCHKKSRTFEAFMYLSLPLASSNKCS-LQECLKLFSKEEkLTDNNKVLcshcktRRDS--TKKIEIWKLPPIL 969
Cdd:cd02657    128 TKMKCTeSPDEEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEE-IEKHSPTL------GRDAiyTKTSRISRLPKYL 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  970 LVHLKRFSydgrWKQKLQT------SVDFPLEnLDLSQYVigpkSNLKKYSLYGVSNHYG-GLDGGHYTAYCKNAIKQRW 1042
Cdd:cd02657    201 TVQFVRFF----WKRDIQKkakilrKVKFPFE-LDLYELC----TPSGYYELVAVITHQGrSADSGHYVAWVRRKNDGKW 271

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1993917542 1043 HKFDDHEVSDISTSSVKSSA-------AYILFY 1068
Cdd:cd02657    272 IKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 719-1068 2.58e-28

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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 117.30  E-value: 2.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  719 PTATQIRNLNPvfgglgaaLTGLRNLGNTCYMNSILQCLCNTPrlaeyfnknYYQEDINRSNILGHKGEVAEEFGVIMKA 798
Cdd:cd02671     13 TSCEKRENLLP--------FVGLNNLGNTCYLNSVLQVLYFCP---------GFKHGLKHLVSLISSVEQLQSSFLLNPE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  799 LWSGQYRFISPRDFKFTIGKINDQFSGFDQQDSQELLLFLMDGLHEDLNKadnrkrykeetndhlddykaadlawskhkm 878
Cdd:cd02671     76 KYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK------------------------------ 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  879 lnesiivaLFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASSNKCSLQECLKL-----------------FSKEEKLTD 941
Cdd:cd02671    126 --------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEIspdpktemktlkwaisqFASVERIVG 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  942 NNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKRFSYDGRWK------QKLQTSVDFPLEnLDLSQYVIGPKSNLkkYSL 1015
Cdd:cd02671    198 EDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPLK-LSLEEWSTKPKNDV--YRL 274

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993917542 1016 YGVSNHYGG-LDGGHYTAYCknaikqRWHKFDDHEV---------SDISTSSVKSSAAYILFY 1068
Cdd:cd02671    275 FAVVMHSGAtISSGHYTAYV------RWLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1068 9.70e-27

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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 110.15  E-value: 9.70e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNTPRLAEYFNknyyqedinrsnilghkgevaeefgvimkalwsgqyRFISprdfkftigki 819
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEYLE------------------------------------EFLE----------- 33

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  820 ndqfsgfdQQDSQELLLFLMDGLhedlnkadnrkrykeetndhlddykaadlawskhkmlnESIIVALFQGQFKSTVQCL 899
Cdd:cd02662     34 --------QQDAHELFQVLLETL--------------------------------------EQLLKFPFDGLLASRIVCL 67

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  900 TCHKKSR-TFEAFMYLSLPL---ASSNKCSLQECLKLFSKEEKLTDnnkVLCSHCKTRrdstkkieIWKLPPILLVHLKR 975
Cdd:cd02662     68 QCGESSKvRYESFTMLSLPVpnqSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSR 136

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  976 FSYDGRWK-QKLQTSVDFPLEnldLSQYvigpksnlkKYSLYGVSNHYGGLDGGHYTAY--------------------C 1034
Cdd:cd02662    137 SVFDGRGTsTKNSCKVSFPER---LPKV---------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreG 204

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1993917542 1035 KNAIKQRWHKFDDHEVSDISTSSVK-SSAAYILFY 1068
Cdd:cd02662    205 PSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
740-1068 1.94e-26

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 110.28  E-value: 1.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLC-NTPRLAEY-----FNKNYYQEDINRSnilgHKGEVAEEFGVIMKALWSGQyrfisprdfK 813
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKLDELlddlsKELKVLKNVIRKP----EPDLNQEEALKLFTALWSSK---------E 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  814 FTIGKINDQFSgfdQQDSQELLLFLMDGLHEDLNKADNRkRYKEETNDHLDDYKAadlAWSkhkmlneSIIVALFQGQF- 892
Cdd:COG5533     68 HKVGWIPPMGS---QEDAHELLGKLLDELKLDLVNSFTI-RIFKTTKDKKKTSTG---DWF-------DIIIELPDQTWv 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  893 --KSTVQCltchkksrTFEAFMYLslplaSSNKCSLQeclklfskeEKLTDNNKVLcshCKTRRDSTKKieiwKLPPILL 970
Cdd:COG5533    134 nnLKTLQE--------FIDNMEEL-----VDDETGVK---------AKENEELEVQ---AKQEYEVSFV----KLPKILT 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  971 VHLKRFSYDGRwKQKLQTSVDfplENLDLSqYVIGPKSNLKK---YSLYGVSNHYGGLDGGHYTAYCKnaIKQRWHKFDD 1047
Cdd:COG5533    185 IQLKRFANLGG-NQKIDTEVD---EKFELP-VKHDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKAND 257

                          330       340
                   ....*....|....*....|....
gi 1993917542 1048 HEVSDISTS---SVKSSAAYILFY 1068
Cdd:COG5533    258 SDVTPVSEEeaiNEKAKNAYLYFY 281
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 740-1051 1.31e-24

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 111.50  E-value: 1.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNTprlaEYFNKNYYQ--EDINRSNilghkGEVAEefgVIMKALWSGQYRFISPRDFKFTIG 817
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFI----AKFRKDVYGipTDHPRGR-----DSVAL---ALQRLFYNLQTGEEPVDTTELTRS 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  818 KINDQFSGFDQQDSQELLLFLMDGLhedlnkaDNRKRYKEETNdhlddykaadlawskhkMLNEsiivaLFQGQFKSTVQ 897
Cdd:COG5077    263 FGWDSDDSFMQHDIQEFNRVLQDNL-------EKSMRGTVVEN-----------------ALNG-----IFVGKMKSYIK 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  898 CLTCHKKSRTFEAFMYLSLPLASSNkcSLQECLKLFSKEEKLTDNNKVLCSHcKTRRDSTKKIEIWKLPPILLVHLKRFS 977
Cdd:COG5077    314 CVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFE 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  978 YDGRWKQ--KLQTSVDFPLEnLDLSQYVigPKSNLKK------YSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDHE 1049
Cdd:COG5077    391 YDFERDMmvKINDRYEFPLE-IDLLPFL--DRDADKSensdavYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTR 467


                   ..
gi 1993917542 1050 VS 1051
Cdd:COG5077    468 VT 469
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 740-1068 8.78e-24

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: 105.86  E-value: 8.78e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  740 GLRNLGNTCYMNSILQCLCNTPRLAEYF--NKNYyqedinrSNILGHKGEVAEEFGVIMKALWS-----GQyrfISPRDF 812
Cdd:cd02669    121 GLNNIKNNDYANVIIQALSHVKPIRNFFllYENY-------ENIKDRKSELVKRLSELIRKIWNprnfkGH---VSPHEL 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  813 KFTIGKINDQFSGFDQQ-DSQELLLFLMDGLHEDLNKADNRkrykeetndhlddykaadlawskhkmlNESIIVALFQGQ 891
Cdd:cd02669    191 LQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGSKKP---------------------------NSSIIHDCFQGK 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  892 FKSTVQCLTCHK---------------KSRTFEAFMYLSLPL------ASSNKCSLQECLKLFskeEKLTDNNKVLCSHC 950
Cdd:cd02669    244 VQIETQKIKPHAeeegskdkffkdsrvKKTSVSPFLLLTLDLpppplfKDGNEENIIPQVPLK---QLLKKYDGKTETEL 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  951 KTRRdstKKIEIWKLPPILLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKSNLKKYSLYG-VSN--HYGG-LD 1026
Cdd:cd02669    321 KDSL---KRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNlVANivHEGTpQE 397

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1993917542 1027 GGHYTAYCKNAIKQRWHKFDDHEVSDISTSSVKSSAAYILFY 1068
Cdd:cd02669    398 DGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 815-1068 1.25e-12

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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 69.09  E-value: 1.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  815 TIGKINDQFSGFDQQDSQELLLFL---MDGLHEdlNKADNRKRYKEETNdHLDDYKAadlawskHKMLNESIIValfqgq 891
Cdd:cd02673     20 SIGKINTEFDNDDQQDAHEFLLTLleaIDDIMQ--VNRTNVPPSNIEIK-RLNPLEA-------FKYTIESSYV------ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  892 fkstvqCLTCHKKSRTFEAFMYLSLPLASSNKCSLQeclKLFSKEEKLTDNNKVlCSHCKTRRDSTKKiEIWKLPPILLV 971
Cdd:cd02673     84 ------CIGCSFEENVSDVGNFLDVSMIDNKLDIDE---LLISNFKTWSPIEKD-CSSCKCESAISSE-RIMTFPECLSI 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  972 HLKRFsydgrwkqKLQTSVdfpLENLDLSQYVIGP-KSNLKKYSLYGVSNHYG-GLDGGHYTAYCKNAIK-QRWHKFDDH 1048
Cdd:cd02673    153 NLKRY--------KLRIAT---SDYLKKNEEIMKKyCGTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDD 221

                          250       260
                   ....*....|....*....|...
gi 1993917542 1049 EVSDISTSSVK---SSAAYILFY 1068
Cdd:cd02673    222 EIRPVSKNDVStnaRSSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 828-1068 4.38e-11

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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 64.12  E-value: 4.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  828 QQDSQELLLFLMDGLHEDLNKADNRKRYKEEtndhlddykaadlawSKHKMlnesiiVALFQGQFkSTVQCLTcHKKSRT 907
Cdd:cd02665     22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEK---------------SKNPM------VQLFYGTF-LTEGVLE-GKPFCN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  908 FEafMYLSLPLASSNKCSLQECLK--LFSKEEKLTDNNKVLCSHckTRRDSTKkieiwkLPPILLVHLKRFSYDGRWKQK 985
Cdd:cd02665     79 CE--TFGQYPLQVNGYGNLHECLEaaMFEGEVELLPSDHSVKSG--QERWFTE------LPPVLTFELSRFEFNQGRPEK 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  986 LQTSVDFPLEnldLSQYvigpksnlkKYSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDHEVSDISTSSVKSSA--- 1062
Cdd:cd02665    149 IHDKLEFPQI---IQQV---------PYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgg 216

                          250
                   ....*....|.
gi 1993917542 1063 -----AYILFY 1068
Cdd:cd02665    217 grnpsAYCLMY 227
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
880-1047 1.03e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 54.97  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  880 NESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSL--------PLASSNKCSLQECLKLFSKEEKLTdnnKVLCSHCK 951
Cdd:pfam13423  124 AESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLiyprkpssNNKKPPNQTFSSILKSSLERETTT---KAWCEKCK 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  952 TRRDSTKKIEIWKLPPILLVHLKRFSYDgrWKQKLQTSVDFPLE-NLDLSQYVIGPkSNLKKYSLYG-VSNHYGGLDGGH 1029
Cdd:pfam13423  201 RYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPEiGLTLSDDLQGD-NEIVKYELRGvVVHIGDSGTSGH 277

                          170       180
                   ....*....|....*....|....*
gi 1993917542 1030 YTAYCKNAIK-------QRWHKFDD 1047
Cdd:pfam13423  278 LVSFVKVADSeledpteSQWYLFND 302
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 875-1069 2.27e-05

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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 47.51  E-value: 2.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  875 KHKMLNE-----SIIVALFQGQFKSTVQC-----LTCHKKSRTFEAFMY-LSLPLASSNKCSL---QECLKLFSKEEKlt 940
Cdd:cd02672     54 ESCLLCElgylfSTLIQNFTRFLLETISQdqlgtPFSCGTSRNSVSLLYtLSLPLGSTKTSKEstfLQLLKRSLDLEK-- 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  941 dNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKR-----------FSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKSN 1009
Cdd:cd02672    132 -VTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLVInlsvtngefddINVVLPSGKVMQNKVSPKAIDHDKLVKNRGQESI 210

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993917542 1010 lKKYSLYG-VSNHYGGLDGGHYTA----YCKNAIKQRWHKFDDHEVSDISTSsvkssaAYILFYT 1069
Cdd:cd02672    211 -YKYELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFNDFLVTPVSEL------AYILLYQ 268
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 964-1068 1.55e-04

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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 44.44  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  964 KLPPILLVHLKRFSYDGRWKQKLQTSVDFPLEnLDL----------------------SQYVIGPKSNLKKYSLYGVSNH 1021
Cdd:cd02670     97 KAPSCLIICLKRYGKTEGKAQKMFKKILIPDE-IDIpdfvaddpracskcqlecrvcyDDKDFSPTCGKFKLSLCSAVCH 175

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993917542 1022 YG-GLDGGHYTAYCK-----------NAIKQRWHKFDD-------HEVSDISTSSVKSSaAYILFY 1068
Cdd:cd02670    176 RGtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDDmadrdgvSNGFNIPAARLLED-PYMLFY 240
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 202-311 3.48e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 37.85  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917542  202 VIIMDARSQKDYQESQIqvptQKIISVPEDIIkpgitvnQIEANLPSESREQWKKRGLADYVVLLDWFSSAKDLklgtTL 281
Cdd:pfam00581    6 VVLIDVRPPEEYAKGHI----PGAVNVPLSSL-------SLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1993917542  282 QSLKDALFKwdsqtilrsEPLVLEGGYESW 311
Cdd:pfam00581   71 ALLKALGYK---------NVYVLDGGFEAW 91
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 739-755 5.46e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 40.17  E-value: 5.46e-03
                           10
                   ....*....|....*..
gi 1993917542  739 TGLRNLGNTCYMNSILQ 755
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQ 18
 
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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