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Conserved domains on  [gi|327269841|ref|XP_003219701|]
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ubiquitin carboxyl-terminal hydrolase 14 [Anolis carolinensis]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 13005984)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins; similar to human ubiquitin carboxyl-terminal hydrolase 14 (USP14) and Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 6 (UBP6)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-482 2.74e-175

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: 494.54  E-value: 2.74e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 185
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 186 FAEKGDQGQYLQQDANECWVQMMRVLQQKLEGiegdtvmetdpgasgaaaaPPKKKSLIDQFFSIEFETTMKCTEAE-EE 264
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG-------------------AGSKGSFIDQLFGIELETKMKCTESPdEE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 265 EVTKGRENQLQLSCFINQEVKYLFTGLKLRLQEEITKLSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKV 344
Cdd:cd02657  140 EVSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKI 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 345 LKDVKFPLMLDVYELCTPelqesmvpyrskfkdledkkvnqqtknsskgdgaqkevkyeafsfpddigsnnCGYYELQAV 424
Cdd:cd02657  220 LRKVKFPFELDLYELCTP-----------------------------------------------------SGYYELVAV 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 327269841 425 LTHQGRSSSSGHYVSWVKRKE-DEWIKFDDDKVSTVTPEDILRLSGGGDWHIAYVLLYG 482
Cdd:cd02657  247 ITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-76 3.96e-44

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain.


:

Pssm-ID: 340521  Cd Length: 75  Bit Score: 149.69  E-value: 3.96e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327269841   4 FTVNVKWGKEKFDGVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTVKDDDWGN-IKIKNGMTLLMMGSAE 76
Cdd:cd16104    2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKDGQTLMLMGSAE 75
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-482 2.74e-175

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: 494.54  E-value: 2.74e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 185
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 186 FAEKGDQGQYLQQDANECWVQMMRVLQQKLEGiegdtvmetdpgasgaaaaPPKKKSLIDQFFSIEFETTMKCTEAE-EE 264
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG-------------------AGSKGSFIDQLFGIELETKMKCTESPdEE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 265 EVTKGRENQLQLSCFINQEVKYLFTGLKLRLQEEITKLSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKV 344
Cdd:cd02657  140 EVSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKI 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 345 LKDVKFPLMLDVYELCTPelqesmvpyrskfkdledkkvnqqtknsskgdgaqkevkyeafsfpddigsnnCGYYELQAV 424
Cdd:cd02657  220 LRKVKFPFELDLYELCTP-----------------------------------------------------SGYYELVAV 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 327269841 425 LTHQGRSSSSGHYVSWVKRKE-DEWIKFDDDKVSTVTPEDILRLSGGGDWHIAYVLLYG 482
Cdd:cd02657  247 ITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
105-481 1.04e-75

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 240.42  E-value: 1.04e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841  105 CGLTNLGNTCYMNATVQCIRSVPELKEALKRYAGALRASGEMASAQyITAALRDLFDSMDK--TSSSIPPIILLQFLHMA 182
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKnsKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841  183 FPQFAekgdqgQYLQQDANECWVQMMRVLQQKLEGiegdtvmetdpgasgaaAAPPKKKSLIDQFFSIEFETTMKCTEAE 262
Cdd:pfam00443  80 NPDFS------GYKQQDAQEFLLFLLDGLHEDLNG-----------------NHSTENESLITDLFRGQLKSRLKCLSCG 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841  263 EEEVTKGRENQLQLSCFINQEVK--------YLFTGLKLRLQEEITKLSPTLQRNALYIKSSKISRLPAYLTIQMVRFFY 334
Cdd:pfam00443 137 EVSETFEPFSDLSLPIPGDSAELktaslqicFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841  335 keKESVNAKVLKDVKFPLMLDVYELCTPELQESMVPYRSkfkdledkkvnqqtknsskgdgaqkevkyeafsfpddigsn 414
Cdd:pfam00443 217 --NRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD----------------------------------------- 253
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327269841  415 ncgyYELQAVLTHQGrSSSSGHYVSWVKRKED-EWIKFDDDKVSTVTPEDILRLsgggdwHIAYVLLY 481
Cdd:pfam00443 254 ----YRLVAVVVHSG-SLSSGHYIAYIKAYENnRWYKFDDEKVTEVDEETAVLS------SSAYILFY 310
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-76 3.96e-44

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain.


Pssm-ID: 340521  Cd Length: 75  Bit Score: 149.69  E-value: 3.96e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327269841   4 FTVNVKWGKEKFDGVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTVKDDDWGN-IKIKNGMTLLMMGSAE 76
Cdd:cd16104    2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKDGQTLMLMGSAE 75
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
106-464 2.54e-21

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 93.71  E-value: 2.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIR-SVPELKEALKRYAGALRA-------SGEMASAQYITAALRDLFDSMDKTSSSIPPiillq 177
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEHKVGWIPP----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 178 flhmafpqfaekgdqgQYLQQDANECWVQMMRVLQQKLEGIEGDTVMETdpgasgaaaAPPKKKSLIDQFFSIEFETTMK 257
Cdd:COG5533   76 ----------------MGSQEDAHELLGKLLDELKLDLVNSFTIRIFKT---------TKDKKKTSTGDWFDIIIELPDQ 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 258 cteaeeeevtKGRENQLQLSCFINQeVKYLF---TGLKLRLQEEItklspTLQRNALYIKSskISRLPAYLTIQMVRFFY 334
Cdd:COG5533  131 ----------TWVNNLKTLQEFIDN-MEELVddeTGVKAKENEEL-----EVQAKQEYEVS--FVKLPKILTIQLKRFAN 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 335 kekESVNAKVLKDVkfplmldvyelctpelqesmvpyrskfkdleDKKVNQQTKnsskgdgaqkevkyeafsfPDDIGSN 414
Cdd:COG5533  193 ---LGGNQKIDTEV-------------------------------DEKFELPVK-------------------HDQILNI 219
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 327269841 415 N-CGYYELQAVLTHQGrSSSSGHYVSWVKRKEDeWIKFDDDKVSTVTPEDI 464
Cdd:COG5533  220 VkETYYDLVGFVLHQG-SLEGGHYIAYVKKGGK-WEKANDSDVTPVSEEEA 268
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
4-74 4.42e-10

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 55.73  E-value: 4.42e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327269841     4 FTVNVKWGKEKFDGVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTVKDDD-WGNIKIKNGMTLLMMGS 74
Cdd:smart00213   1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRtLADYGIQDGSTIHLVLR 72
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
6-74 6.09e-03

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 35.61  E-value: 6.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327269841    6 VNVK-WGKEKFDgVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTVKDDD-WGNIKIKNGMTLLMMGS 74
Cdd:pfam00240   1 ITVKtLDGKKIT-LEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQtLGEYGIEDGSTIHLVLR 70
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-482 2.74e-175

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: 494.54  E-value: 2.74e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 185
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 186 FAEKGDQGQYLQQDANECWVQMMRVLQQKLEGiegdtvmetdpgasgaaaaPPKKKSLIDQFFSIEFETTMKCTEAE-EE 264
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG-------------------AGSKGSFIDQLFGIELETKMKCTESPdEE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 265 EVTKGRENQLQLSCFINQEVKYLFTGLKLRLQEEITKLSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKV 344
Cdd:cd02657  140 EVSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKI 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 345 LKDVKFPLMLDVYELCTPelqesmvpyrskfkdledkkvnqqtknsskgdgaqkevkyeafsfpddigsnnCGYYELQAV 424
Cdd:cd02657  220 LRKVKFPFELDLYELCTP-----------------------------------------------------SGYYELVAV 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 327269841 425 LTHQGRSSSSGHYVSWVKRKE-DEWIKFDDDKVSTVTPEDILRLSGGGDWHIAYVLLYG 482
Cdd:cd02657  247 ITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
105-481 1.04e-75

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 240.42  E-value: 1.04e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841  105 CGLTNLGNTCYMNATVQCIRSVPELKEALKRYAGALRASGEMASAQyITAALRDLFDSMDK--TSSSIPPIILLQFLHMA 182
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKnsKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841  183 FPQFAekgdqgQYLQQDANECWVQMMRVLQQKLEGiegdtvmetdpgasgaaAAPPKKKSLIDQFFSIEFETTMKCTEAE 262
Cdd:pfam00443  80 NPDFS------GYKQQDAQEFLLFLLDGLHEDLNG-----------------NHSTENESLITDLFRGQLKSRLKCLSCG 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841  263 EEEVTKGRENQLQLSCFINQEVK--------YLFTGLKLRLQEEITKLSPTLQRNALYIKSSKISRLPAYLTIQMVRFFY 334
Cdd:pfam00443 137 EVSETFEPFSDLSLPIPGDSAELktaslqicFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841  335 keKESVNAKVLKDVKFPLMLDVYELCTPELQESMVPYRSkfkdledkkvnqqtknsskgdgaqkevkyeafsfpddigsn 414
Cdd:pfam00443 217 --NRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD----------------------------------------- 253
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327269841  415 ncgyYELQAVLTHQGrSSSSGHYVSWVKRKED-EWIKFDDDKVSTVTPEDILRLsgggdwHIAYVLLY 481
Cdd:pfam00443 254 ----YRLVAVVVHSG-SLSSGHYIAYIKAYENnRWYKFDDEKVTEVDEETAVLS------SSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
106-481 3.77e-53

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: 179.99  E-value: 3.77e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIRSVpelkealkryagalrasgemasaqyitaalrdlfdsmdktsssippiillqflhmafpq 185
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 186 faekgdqgqylQQDANECWVQMMRVLQQKLEGIEGDTVMETdpgasgaaaappKKKSLIDQFFSIEFETTMKCTEAEEEE 265
Cdd:cd02257   22 -----------QQDAHEFLLFLLDKLHEELKKSSKRTSDSS------------SLKSLIHDLFGGKLESTIVCLECGHES 78
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 266 VTKGRENQLQLSCFI-NQEVKYLFTGLKLRLQEEIT----KLSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKeSV 340
Cdd:cd02257   79 VSTEPELFLSLPLPVkGLPQVSLEDCLEKFFKEEILegdnCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GT 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 341 NAKVLKDVKFPLMLDVYELCTPElqesmvpyrskfkdledkkvnqqtknsskgdgaqkevkyeafsFPDDIGSNNCGYYE 420
Cdd:cd02257  158 KEKLNTKVSFPLELDLSPYLSEG-------------------------------------------EKDSDSDNGSYKYE 194
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327269841 421 LQAVLTHQGRSSSSGHYVSWVK-RKEDEWIKFDDDKVSTVTPEDILRLsgGGDWHIAYVLLY 481
Cdd:cd02257  195 LVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLEF--GSLSSSAYILFY 254
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-76 3.96e-44

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain.


Pssm-ID: 340521  Cd Length: 75  Bit Score: 149.69  E-value: 3.96e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327269841   4 FTVNVKWGKEKFDGVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTVKDDDWGN-IKIKNGMTLLMMGSAE 76
Cdd:cd16104    2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKDGQTLMLMGSAE 75
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-481 5.58e-23

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: 99.64  E-value: 5.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 105 CGLTNLGNTCYMNATVQCIRSVPELKEALKRYAGA---------------LRASGEMASAQYITAALRDLFDSMDKTSSS 169
Cdd:cd02659    3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTeddddnksvplalqrLFLFLQLSESPVKTTELTDKTRSFGWDSLN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 170 IppiillqflhmafpqfaekgdqgqYLQQDANEcwvqMMRVLQQKLEgiegdTVMEtdpgasgaaaaPPKKKSLIDQFFS 249
Cdd:cd02659   83 T------------------------FEQHDVQE----FFRVLFDKLE-----EKLK-----------GTGQEGLIKNLFG 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 250 IEFETTMKCTEAEEEevTKGRENQLQLSCFInQEVKYLFTGLKLRLQEEitklspTLQRNALY-----------IKSSKI 318
Cdd:cd02659  119 GKLVNYIICKECPHE--SEREEYFLDLQVAV-KGKKNLEESLDAYVQGE------TLEGDNKYfcekcgkkvdaEKGVCF 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 319 SRLPAYLTIQMVRFFYK----EKESVNAKVlkdvKFPLMLDvyelctpelqesMVPYRSKFkdledkkvnqqtknsskgd 394
Cdd:cd02659  190 KKLPPVLTLQLKRFEFDfetmMRIKINDRF----EFPLELD------------MEPYTEKG------------------- 234
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 395 gaqkEVKYEAFSFPDDIGSNNcgyYELQAVLTHQGrSSSSGHYVSWVK-RKEDEWIKFDDDKVSTVTPEDILRLSGGGD- 472
Cdd:cd02659  235 ----LAKKEGDSEKKDSESYI---YELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECFGGEe 306
                        410       420
                 ....*....|....*....|...
gi 327269841 473 --------------WHIAYVLLY 481
Cdd:cd02659  307 tqktydsgprafkrTTNAYMLFY 329
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-481 2.09e-22

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: 97.83  E-value: 2.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIRSVPELKEAL---KRYAGALRASgemaSAQYITAALRDLFDSMDKTSSSIP--PIILLQFLH 180
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFlsdRHSCTCLSCS----PNSCLSCAMDEIFQEFYYSGDRSPygPINLLYLSW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 181 MAFPQFAekgdqgQYLQQDANECWVQMMRVLQQKLEGIEGDTVMETDPgasgaaaappkkKSLIDQFFSIEFETTMKCTE 260
Cdd:cd02660   78 KHSRNLA------GYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHC------------NCIIHQTFSGSLQSSVTCQR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 261 AEEeeVTKGRENQLQLSCFInQEVKYLFTGLKLRLQEEITKLSPTLQR--------NALY-----------IKSSKISRL 321
Cdd:cd02660  140 CGG--VSTTVDPFLDLSLDI-PNKSTPSWALGESGVSGTPTLSDCLDRftrpeklgDFAYkcsgcgstqeaTKQLSIKKL 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 322 PAYLTIQMVRFFYKEKESvNAKVLKDVKFPLMLDvyelctpelqesMVPYRSkfkdledkkvnqqtknSSKGDGAQKEVK 401
Cdd:cd02660  217 PPVLCFQLKRFEHSLNKT-SRKIDTYVQFPLELN------------MTPYTS----------------SSIGDTQDSNSL 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 402 YEAFSfpddigsnncgyYELQAVLTHQGrSSSSGHYVSWVKRKEDEWIKFDDDKVSTVTPEDILRLSgggdwhiAYVLLY 481
Cdd:cd02660  268 DPDYT------------YDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQ-------AYLLFY 327
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
106-464 2.54e-21

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 93.71  E-value: 2.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIR-SVPELKEALKRYAGALRA-------SGEMASAQYITAALRDLFDSMDKTSSSIPPiillq 177
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEHKVGWIPP----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 178 flhmafpqfaekgdqgQYLQQDANECWVQMMRVLQQKLEGIEGDTVMETdpgasgaaaAPPKKKSLIDQFFSIEFETTMK 257
Cdd:COG5533   76 ----------------MGSQEDAHELLGKLLDELKLDLVNSFTIRIFKT---------TKDKKKTSTGDWFDIIIELPDQ 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 258 cteaeeeevtKGRENQLQLSCFINQeVKYLF---TGLKLRLQEEItklspTLQRNALYIKSskISRLPAYLTIQMVRFFY 334
Cdd:COG5533  131 ----------TWVNNLKTLQEFIDN-MEELVddeTGVKAKENEEL-----EVQAKQEYEVS--FVKLPKILTIQLKRFAN 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 335 kekESVNAKVLKDVkfplmldvyelctpelqesmvpyrskfkdleDKKVNQQTKnsskgdgaqkevkyeafsfPDDIGSN 414
Cdd:COG5533  193 ---LGGNQKIDTEV-------------------------------DEKFELPVK-------------------HDQILNI 219
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 327269841 415 N-CGYYELQAVLTHQGrSSSSGHYVSWVKRKEDeWIKFDDDKVSTVTPEDI 464
Cdd:COG5533  220 VkETYYDLVGFVLHQG-SLEGGHYIAYVKKGGK-WEKANDSDVTPVSEEEA 268
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
104-481 1.07e-20

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: 92.34  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 104 PCGLTNLGNTCYMNATVQCIRSVPELKEALKRYAGALRASGEMASA-----QYITAALRDlfdsmdkTSSSIPPIILLQF 178
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMmcaleAHVERALAS-------SGPGSAPRIFSSN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 179 LHMAFPQFaekgdqGQYLQQDANEcwvqMMRVLQQKLEGIEGDTvmetdPGASGAAAAPPKKKSLIDQFFSIEFETTMKC 258
Cdd:cd02661   74 LKQISKHF------RIGRQEDAHE----FLRYLLDAMQKACLDR-----FKKLKAVDPSSQETTLVQQIFGGYLRSQVKC 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 259 TEAEEEEVTkgRENQLQLSCFINQeVKYLFTGLKLRLQEEITKLSPTLQ--RNALYIKSSK---ISRLPAYLTIQMVRF- 332
Cdd:cd02661  139 LNCKHVSNT--YDPFLDLSLDIKG-ADSLEDALEQFTKPEQLDGENKYKceRCKKKVKASKqltIHRAPNVLTIHLKRFs 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 333 -FYKEKESvnakvlKDVKFPLMLDvyelctpelqesMVPYRSkfkdledkkvnqqtknsSKGDGAQKevkyeafsfpddi 411
Cdd:cd02661  216 nFRGGKIN------KQISFPETLD------------LSPYMS-----------------QPNDGPLK------------- 247
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 412 gsnncgyYELQAVLTHQGRSSSSGHYVSWVKRKEDEWIKFDDDKVSTVTPEDILRLSgggdwhiAYVLLY 481
Cdd:cd02661  248 -------YKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQK-------AYILFY 303
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-461 1.32e-20

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: 92.48  E-value: 1.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIRSVPELKEALkrYAGALRASGEMASAQyitaalrdlfdsMDKTSSSIPPIILLQFLhMAFPQ 185
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAV--YECNSTEDAELKNMP------------PDKPHEPQTIIDQLQLI-FAQLQ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 186 FAEKG-------------DQGQylQQDANECWVQMMRVLQQKLEgiegdtvmetdpgasgaAAAPPKKKSLIDQFFSIEF 252
Cdd:cd02668   66 FGNRSvvdpsgfvkalglDTGQ--QQDAQEFSKLFLSLLEAKLS-----------------KSKNPDLKNIVQDLFRGEY 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 253 ETTMKCTEAEEEEVTKGRENQLQLSCFINQEVKYLFTGLklrLQEEITK-----LSPTLQRNALYIKSSKISRLPAYLTI 327
Cdd:cd02668  127 SYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEF---LKEEQLTgdnqyFCESCNSKTDATRRIRLTTLPPTLNF 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 328 QMVRFFYKEKESVNAKVLKDVKFPLMLDVYELCTPelqesmvpyrskfkdledkkvnqqtknsskgdgaQKEVKYEafsf 407
Cdd:cd02668  204 QLLRFVFDRKTGAKKKLNASISFPEILDMGEYLAE----------------------------------SDEGSYV---- 245
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 327269841 408 pddigsnncgyYELQAVLTHQGRSSSSGHYVSWVK-RKEDEWIKFDDDKVSTVTP 461
Cdd:cd02668  246 -----------YELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMPG 289
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-481 1.37e-17

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: 83.70  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQcirsvpelkealkryagALrasgemASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 185
Cdd:cd02664    1 GLINLGNTCYMNSVLQ-----------------AL------FMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQ 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 186 FAEKGDQGQYL------------QQDANEcwvqMMRVLQQKLEgiegdtvmetdpgasgaaaappkkkSLIDQFFSIEFE 253
Cdd:cd02664   58 RRAEAPPDYFLeasrppwftpgsQQDCSE----YLRYLLDRLH-------------------------TLIEKMFGGKLS 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 254 TTMKCTEAEEEEVTKGRENQLQLS-CFINQEVKYLFTGLKLrlQEEITKLSPTLQRNALYIKSSKISRLPAYLTIQMVRF 332
Cdd:cd02664  109 TTIRCLNCNSTSARTERFRDLDLSfPSVQDLLNYFLSPEKL--TGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRF 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 333 FYKEKESVNAKVLKDVKFPLMLDVyelctpelqesmvPYRSKFKDLEDKKVNQQTKNSSKGDGAQKEVkyeafsfpddig 412
Cdd:cd02664  187 SYDQKTHVREKIMDNVSINEVLSL-------------PVRVESKSSESPLEKKEEESGDDGELVTRQV------------ 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 413 snncgYYELQAVLTHQGRSSSSGHYVSWV---------------------KRKEDEWIKFDDDKVSTVTPEDILRLSGGG 471
Cdd:cd02664  242 -----HYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYLFNDSRVTFSSFESVQNVTSRF 316
                        410
                 ....*....|
gi 327269841 472 DWHIAYVLLY 481
Cdd:cd02664  317 PKDTPYILFY 326
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-481 5.03e-17

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: 80.02  E-value: 5.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIrsvpelkealkryagalrasgemasaqyitaalrdlfdsmdktsssippiillqfLHMafpq 185
Cdd:cd02674    1 GLRNLGNTCYMNSILQCL-------------------------------------------------------SAD---- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 186 faekgdqgqylQQDANEcwvqmmrVLQQKLEGIEgdtvmetdpgasgaaaappkkkSLIDQFFSIEFETTMKCTEAEEEE 265
Cdd:cd02674   22 -----------QQDAQE-------FLLFLLDGLH----------------------SIIVDLFQGQLKSRLTCLTCGKTS 61
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 266 VT--------------KGRENQLQL-SCFInqevkyLFTGlKLRLQEEITKLSPTLQRNALYIKSSKISRLPAYLTIQMV 330
Cdd:cd02674   62 TTfepftylslpipsgSGDAPKVTLeDCLR------LFTK-EETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLK 134
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 331 RFFYKEKESVnaKVLKDVKFPLmldvyelctpelqesmvpyrskfKDLEDKKvnqqtknsskgdgaqkevkyeafsFPDD 410
Cdd:cd02674  135 RFSFSRGSTR--KLTTPVTFPL-----------------------NDLDLTP------------------------YVDT 165
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327269841 411 IGSNNCGYYELQAVLTHQGrSSSSGHYVSWVKRKE-DEWIKFDDDKVSTVTPEDILRLSgggdwhiAYVLLY 481
Cdd:cd02674  166 RSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNEtNDWYKFDDSRVTKVSESSVVSSS-------AYILFY 229
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-481 2.44e-16

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: 79.66  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIrsvpelkealkrYAGALRASgemasaqyitaaLRDLFDSM---DKTSSSIPPIILLQFLHMA 182
Cdd:cd02663    1 GLENFGNTCYCNSVLQAL------------YFENLLTC------------LKDLFESIseqKKRTGVISPKKFITRLKRE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 183 FPQFaekgdqGQYLQQDANECwvqMMRVLQQKLEGIEGDTVMETDPGASGAAAAPPKKKSLIDQFFSIEFETTMKCTEAE 262
Cdd:cd02663   57 NELF------DNYMHQDAHEF---LNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCE 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 263 EeeVTKGRENQLQLSCFINQEVKyLFTGLKLRLQEEItkLSptlQRNALYI----------KSSKISRLPAYLTIQMVRF 332
Cdd:cd02663  128 T--VSSRDETFLDLSIDVEQNTS-ITSCLRQFSATET--LC---GRNKFYCdeccslqeaeKRMKIKKLPKILALHLKRF 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 333 FYKEKESVNAKVLKDVKFPLMLDVyelctpelqesmvpyrskfkdledkkvnqqtKNSSkgdgaqkevkyeafsfpdDIG 412
Cdd:cd02663  200 KYDEQLNRYIKLFYRVVFPLELRL-------------------------------FNTT------------------DDA 230
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 413 SNNCGYYELQAVLTHQGRSSSSGHYVSWVKRKeDEWIKFDDDKVSTVTPEDILRLSGGGDWHI-AYVLLY 481
Cdd:cd02663  231 ENPDRLYELVAVVVHIGGGPNHGHYVSIVKSH-GGWLLFDDETVEKIDENAVEEFFGDSPNQAtAYVLFY 299
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-442 6.30e-15

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: 75.12  E-value: 6.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRyagalrasgemasaqyitaALRDLFDSMDKTSssippiillqflhmafPQ 185
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------TPKELFSQVCRKA----------------PQ 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 186 FaeKGdqgqYLQQDANEcwvqmmrVLQQKLEGIEgdtvmetdpgasgaaaappkkkSLIDQFFSIEFETTMKCTEAEEee 265
Cdd:cd02667   46 F--KG----YQQQDSHE-------LLRYLLDGLR----------------------TFIDSIFGGELTSTIMCESCGT-- 88
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 266 VTKGRENQLQLSC----FINQEV-----KYLFTGlklrlQEEITKLSPTLQRNALY-IKSSKISRLPAYLTIQMVRFFyK 335
Cdd:cd02667   89 VSLVYEPFLDLSLprsdEIKSECsiescLKQFTE-----VEILEGNNKFACENCTKaKKQYLISKLPPVLVIHLKRFQ-Q 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 336 EKESVNAKVLKDVKFPLMLDVYELCTPELQESmvpyRSKFKDLedkkvnqqtknsskgdgaqkevkyeafsfpddigsnn 415
Cdd:cd02667  163 PRSANLRKVSRHVSFPEILDLAPFCDPKCNSS----EDKSSVL------------------------------------- 201
                        330       340
                 ....*....|....*....|....*..
gi 327269841 416 cgyYELQAVLTHQGrSSSSGHYVSWVK 442
Cdd:cd02667  202 ---YRLYGVVEHSG-TMRSGHYVAYVK 224
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-481 7.00e-15

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: 75.44  E-value: 7.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYAGALR-----------------ASGeMASAQYITaaLRDLFDSMDKTSS 168
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPsdvvdpandlncqliklADG-LLSGRYSK--PASLKSENDPYQV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 169 SIPPIILLQFLHMAFPQFAEKGdqgqylQQDANECWVQMMRVLQQKLEGIEGD---TVME--TDPGASGAAAAPPKKKSL 243
Cdd:cd02658   78 GIKPSMFKALIGKGHPEFSTMR------QQDALEFLLHLIDKLDRESFKNLGLnpnDLFKfmIEDRLECLSCKKVKYTSE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 244 IDQFFSIEFEttmKCTEAEEEEVTKGRENQLQLSCFINqevkyLFTGlklrlqEEITKLSPTLQRNALYIKSSKISRLPA 323
Cdd:cd02658  152 LSEILSLPVP---KDEATEKEEGELVYEPVPLEDCLKA-----YFAP------ETIEDFCSTCKEKTTATKTTGFKTFPD 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 324 YLTIQMVRFFYKEKESVnakvlkdVKFPLMLDVyelctpelqesmvpyrskfkdledkkvnqqtknsskgdgaqkevkye 403
Cdd:cd02658  218 YLVINMKRFQLLENWVP-------KKLDVPIDV----------------------------------------------- 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 404 afsfPDDIGSnncGYYELQAVLTHQGRSSSSGHYVSWVKRK---EDEWIKFDDDKV-STVTPEDILRLsgggdwhiAYVL 479
Cdd:cd02658  244 ----PEELGP---GKYELIAFISHKGTSVHSGHYVAHIKKEidgEGKWVLFNDEKVvASQDPPEMKKL--------GYIY 308

                 ..
gi 327269841 480 LY 481
Cdd:cd02658  309 FY 310
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-467 1.98e-14

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: 74.16  E-value: 1.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYAGALrasGEMASAQYITAALRDLFDSMDKTSssiPPIILLQFLHMAFPQ 185
Cdd:cd02671   26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI---SSVEQLQSSFLLNPEKYNDELANQ---APRRLLNALREVNPM 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 186 FaekgdQGqYLQQDANE---CWVQMMRVLQQKLegIEGDTVMETdpGASGAAAAPPKKKSLIDQFFSIEFETTMKCTEAE 262
Cdd:cd02671  100 Y-----EG-YLQHDAQEvlqCILGNIQELVEKD--FQGQLVLRT--RCLECETFTERREDFQDISVPVQESELSKSEESS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 263 E---EEVTKGRENQLQLSCFINQEvkylftglklRLQEEITKLSPTLQRNALYIKSSKISRLPAYLTIQMVRF------- 332
Cdd:cd02671  170 EispDPKTEMKTLKWAISQFASVE----------RIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFaangsef 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 333 -FYKEKESVNAKVLKdvkfPLMLDVYELCTpelqesmvpyrskfkdledkkvnQQTKNSskgdgaqkevkyeafsfpddi 411
Cdd:cd02671  240 dCYGGLSKVNTPLLT----PLKLSLEEWST-----------------------KPKNDV--------------------- 271
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 327269841 412 gsnncgyYELQAVLTHQGRSSSSGHYVSWVKrkedeWIKFDDDKVSTVTPEDILRL 467
Cdd:cd02671  272 -------YRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEA 315
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
104-478 1.02e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 69.06  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 104 PCGLTNLGNTCYMNATVQCIRSVPELKEALKRYAGALRAS-----------------GEMASAQYITAALRDLFDSMDKT 166
Cdd:cd02666    1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELasdypterriggrevsrSELQRSNQFVYELRSLFNDLIHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 167 -SSSIPPIILLQFLHMAfpqfaekgdqgqylQQDANECwvqMMRVLQQklegIEGDTVMETDPGASGAAAAPPKKKSLID 245
Cdd:cd02666   81 nTRSVTPSKELAYLALR--------------QQDVTEC---IDNVLFQ----LEVALEPISNAFAGPDTEDDKEQSDLIK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 246 QFFSIEF-ETTMKCTEAEEEEVTKGRENQLQLScfinqeVKYLFTGLKLRLQEEITKLSPTLQRnalYIKSSKISRLPAY 324
Cdd:cd02666  140 RLFSGKTkQQLVPESMGNQPSVRTKTERFLSLL------VDVGKKGREIVVLLEPKDLYDALDR---YFDYDSLTKLPQR 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 325 LTIQMVRFFYKEKE---SVNAKVLKDVKfplmlDVYELCTPELQESMVPYRSKFKDLEDKKvnqqTKNSSKGDGaqkevk 401
Cdd:cd02666  211 SQVQAQLAQPLQRElisMDRYELPSSID-----DIDELIREAIQSESSLVRQAQNELAELK----HEIEKQFDD------ 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 402 YEAFSfpddigsnncgyYELQAVLTHQGrSSSSGHYVSWVK-RKEDEWIKFDDDKVSTVTPEDI-LRLSGGGD--WHIAY 477
Cdd:cd02666  276 LKSYG------------YRLHAVFIHRG-EASSGHYWVYIKdFEENVWRKYNDETVTVVPASEVfLFTLGNTAtpYFLVY 342

                 .
gi 327269841 478 V 478
Cdd:cd02666  343 V 343
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
4-74 4.42e-10

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 55.73  E-value: 4.42e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327269841     4 FTVNVKWGKEKFDGVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTVKDDD-WGNIKIKNGMTLLMMGS 74
Cdd:smart00213   1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRtLADYGIQDGSTIHLVLR 72
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
89-267 1.46e-08

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 57.20  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841  89 VEDMTEEQLASAMEL--PCGLTNLGNTCYMNATVQCIRSVPELKEAL--KRYAGALRASGEMASAQYITAALRDLFDSM- 163
Cdd:COG5560  248 VDSIVDDHNRSINKEagTCGLRNLGNTCYMNSALQCLMHTWELRDYFlsDEYEESINEENPLGMHGSVASAYADLIKQLy 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 164 DKTSSSIPPI----ILLQFLHMAfpqfaeKGdqgqYLQQDANECWVQMMRVLQQKLEGIEGDTVMETDPGASGAAAAPPK 239
Cdd:COG5560  328 DGNLHAFTPSgfkkTIGSFNEEF------SG----YDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKK 397
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 327269841 240 K------------KSLIDQFFSIEFETTMKCTEAEEEEVT 267
Cdd:COG5560  398 KakecwwehlkrnDSIITDLFQGMYKSTLTCPGCGSVSIT 437
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
8-74 2.10e-08

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins; UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator.


Pssm-ID: 340567  Cd Length: 70  Bit Score: 50.71  E-value: 2.10e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327269841   8 VKWGKEKFDgVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTVKDDDWGNIKIKNGMTLLMMGS 74
Cdd:cd17047    5 VIWNKEKYD-VKFPLDSTIAELKEHIETLTGVPPAMQKLMYKGLLKDDKTLRELKVTKGAKVMVVGS 70
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
5-74 4.90e-08

ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) and similar proteins; UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. It is localized in the nucleus and it contains conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which directly interacts with the proteasome. Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear proteasome activity. UBLCP1 may also play a role in the regulation of phosphorylation state of RNA polymerase II C-terminal domain, a key event during mRNA metabolism.


Pssm-ID: 340511  Cd Length: 74  Bit Score: 49.88  E-value: 4.90e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327269841   5 TVNVKWGKEKFDgVELNTDEPPMVFKAQLFALTGVQPDRQKV--MVKGGTVKDDD--WGNIKIKNGMTLLMMGS 74
Cdd:cd01813    2 TLIVKWSGKEYP-VTVLSSDTVLDLKQRIFELTGVLPKRQKLlgLKVKGKPADDDvkLSSLKLKPNTKIMMMGT 74
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
6-72 3.23e-07

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 47.59  E-value: 3.23e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327269841   6 VNVKWGKEKFDGVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTVKDDDW-GNIKIKNGMTLLMM 72
Cdd:cd17039    1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTlSDYGIKDGSTIHLV 68
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
405-481 3.49e-07

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: 51.02  E-value: 3.49e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327269841 405 FSFPDDIGSNNcgyYELQAVLTHQGRsSSSGHYVSWV-KRKEDEWIKFDDDKVSTVTPEDILRLS-GGGDWHIAYVLLY 481
Cdd:cd02665  153 LEFPQIIQQVP---YELHAVLVHEGQ-ANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDSfGGGRNPSAYCLMY 227
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
419-481 2.96e-06

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 49.88  E-value: 2.96e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327269841 419 YELQAVLTHQGrSSSSGHYVSWVKRKEDE-WIKFDDDKVSTVTPEDILRLSgggdwhiAYVLLY 481
Cdd:COG5560  764 YDLYAVDNHYG-GLSGGHYTAYARNFANNgWYLFDDSRITEVDPEDSVTSS-------AYVLFY 819
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
399-472 4.14e-06

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 49.48  E-value: 4.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327269841  399 EVKYEAFSFPDDIGSNNCGY-YELQAVLTHQGrSSSSGHYVSWVK-RKEDEWIKFDDDKVSTVTPEDILRLSGGGD 472
Cdd:COG5077   410 EIDLLPFLDRDADKSENSDAvYVLYGVLVHSG-DLHEGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEENFGGD 484
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
419-470 1.60e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 43.29  E-value: 1.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 327269841 419 YELQAVLTHQGRSSSSGHYVSWVKR--KEDEWIKFDDDKVSTVTPEDIL---RLSGG 470
Cdd:cd02673  184 YSLVAVICHLGESPYDGHYIAYTKElyNGSSWLYCSDDEIRPVSKNDVStnaRSSGY 240
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
401-453 4.09e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 42.26  E-value: 4.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327269841  401 KYEAFSFPDDIGSNNCGYYELQAVLTHQGRSSSSGHYVSWVK--------RKEDEWIKFDD 453
Cdd:pfam13423 242 EIGLTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseledPTESQWYLFND 302
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-136 4.62e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 41.97  E-value: 4.62e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 327269841 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRY 136
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF 31
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
401-481 6.40e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 41.20  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327269841 401 KYEAFSFPDDIGSNncgYYELQAVLTHQGrSSSSGHYVSW------VKRKE---------------DEWIKFDDDKVSTV 459
Cdd:cd02662  148 NSCKVSFPERLPKV---LYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEpgsfvrmregpsstsHPWWRISDTTVKEV 223
                         90       100
                 ....*....|....*....|..
gi 327269841 460 TPEDILrLSGGgdwhiAYVLLY 481
Cdd:cd02662  224 SESEVL-EQKS-----AYMLFY 239
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
6-74 6.09e-03

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 35.61  E-value: 6.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327269841    6 VNVK-WGKEKFDgVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTVKDDD-WGNIKIKNGMTLLMMGS 74
Cdd:pfam00240   1 ITVKtLDGKKIT-LEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQtLGEYGIEDGSTIHLVLR 70
Ubl2_FAT10 cd17053
ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 ...
29-72 9.04e-03

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


Pssm-ID: 340573  Cd Length: 71  Bit Score: 35.02  E-value: 9.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 327269841  29 FKAQLFALTGVQPDRQKVMVKGGTVKDDD--WGNIKIKNGMTLLMM 72
Cdd:cd17053   26 VKAMIEDQSGVPPNEQILVYNGKRLEDGDktLGEYGIKTGDTLYLL 71
Ubl_BAG1 cd01812
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ...
4-74 9.34e-03

ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain.


Pssm-ID: 340510 [Multi-domain]  Cd Length: 77  Bit Score: 35.33  E-value: 9.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327269841   4 FTVNVKWGKEKFD-GVELNTDEPPMV--FKAQLFALTGVQPDRQKVMVKGGTVKDDD--WGNIKIKNGMTLLMMGS 74
Cdd:cd01812    1 LTVTVIHGSNKHTiELPSQDEDEPTLqdLAEAIEEVTGVPVENQKLIFKGKSLKDPEqpLSALGVKNGSKIMLIGK 76
 
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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