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Conserved domains on  [gi|808377460|ref|XP_012193494|]
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ubiquitin carboxyl-terminal hydrolase 2 [Pseudozyma hubeiensis SY62]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 1000871)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0046872|GO:0003723

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
240-1318 2.09e-146

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: 466.67  E-value: 2.09e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  240 GDTWYLISRKWYRRWdaacserrdSDPAEKVDVPIGTIDNSDLLDPDSTPALPRLRpginEHIDYEMLPEEGWSLLVQWY 319
Cdd:COG5560    44 CEYAVIFAYAWYEGM---------FDRASCDGGSPGPIVQGPIVDFEPESLKKSLR----EGIDYSIISGAVWQLLVRWY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  320 GSSGPVFARNVIDGLNAGQESVEFYPPVIRLLKLVHDVSV---QGSGVASFSLSVSASVAELKAKAKSALNLGSiaDvDI 396
Cdd:COG5560   111 GLAGLITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSlinLGHDPVPHSASSHGTLRDLSERVMNAFVDPS--D-DF 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  397 RLYFLPEPTDQeLQNGLVSSARVTEegvdivdaGEDKPDSYQPNTTLKSVGIEEIEiNLVVETRQSGRWQTDpaptdnaa 476
Cdd:COG5560   188 RLWDVVPEIMG-LRLGLDSFFRRYR--------VLASDGRVLHPLTRLELFEDRSV-LLLSKITRNPDWLVD-------- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  477 sssvkgifaqqgdffSNLQQNNatagasaasgtaaeaqgrvtrsqtavdRTMGRSRGLRGLNNLGNTCFMNSALQCLSNT 556
Cdd:COG5560   250 ---------------SIVDDHN---------------------------RSINKEAGTCGLRNLGNTCYMNSALQCLMHT 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  557 YELQQYFVSGAYKEELNTDNPLGMGGAIADAFGNLITNIWNGQGGSFWPREFKFALSRFAPQFSGYAQHDSQELLAFLLD 636
Cdd:COG5560   288 WELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLD 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  637 GLHEDLNRILKKPYIEAPDWEGGDEKDLVAFAKRQWDIYKARNDSVIVDLFQGQYRSTLVCPECSKVSIKFDPFMYLTLP 716
Cdd:COG5560   368 GLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLP 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  717 IPNKKMWKGQIYFVPldASQPMHKFQVQLPAGTTVGKLRQKVAAQFGIE--TKRLVCgEVWHHRVYKWFD--DYEPLVDI 792
Cdd:COG5560   448 LPVSMVWKHTIVVFP--ESGRRQPLKIELDASSTIRGLKKLVDAEYGKLgcFEIKVM-CIYYGGNYNMLEpaDKVLLQDI 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  793 KDGDFVYFWevaapprlskqrqfryhrsvEDAEDALDIPeqeyaVLPVFTNvasdtSGPSSSQAFvsrrarseaiGIPFF 872
Cdd:COG5560   525 PQTDFVYLY--------------------ETNDNGIEVP-----VVHLRIE-----KGYKSKRLF----------GDPFL 564
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  873 isvpKADVNDADAIREHVLQGFsrfagvpEELRQAVEHDRTaaapsalppstsqisdwemvddsaagnddaiqvvapsqm 952
Cdd:COG5560   565 ----QLNVLIKASIYDKLVKEF-------EELLVLVEMKKT--------------------------------------- 594
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  953 adsdlvteiredgeavvvpdvstvDADVSSPSVAPLNEFKAPtpsspalrirfsiaelGQGLPKGSESNaDNLSEDLEER 1032
Cdd:COG5560   595 ------------------------DVDLVSEQVRLLREESSP----------------SSWLKLETEID-TKREEQVEEE 633
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1033 HARlakrsasaasslggEEPMKVEadeleaedeskttstdkavplvytggaIVCTWShsvkARGLLVDSDSAQLWgdyee 1112
Cdd:COG5560   634 GQM--------------NFNDAVV---------------------------ISCEWE----EKRYLSLFSYDPLW----- 663
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1113 tvdeAIRQRENAGParpkTLSIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAGRHSRD 1192
Cdd:COG5560   664 ----TIREIGAAER----TITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD 735
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1193 KLNMLVDFPLEGLDLtdrvegtqalrrvqeeakesgeelsesmlgSGILRPLEDNddavavdRPIYDLYAVDNHFGGLGG 1272
Cdd:COG5560   736 KIDDLVEYPIDDLDL------------------------------SGVEYMVDDP-------RLIYDLYAVDNHYGGLSG 778
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*.
gi 808377460 1273 GHYTAFAKSPADGKWYEFDDSSVRPVANSEAVKsSSAYLLFYRRRT 1318
Cdd:COG5560   779 GHYTAYARNFANNGWYLFDDSRITEVDPEDSVT-SSAYVLFYRRKS 823
MTBP_C super family cl20806
MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its ...
52-153 5.84e-04

MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its interaction with p53, plays an important role in the regulation of the G1 checkpoint of the cell cycle. MTBP promotes MDM2-mediated ubiquitination and degradation of p53 and also MDM2 stabilization in an MDM2 RING finger-dependent manner. MTBP differentially regulates the E3 ubiquitin ligase activity of MDM2 towards two of its most critical targets (itself and p53) and in doing so significantly contributes to MDM2-dependent p53 homeostasis in unstressed cells. MTBP inhibits cancer cell migration by interacting with a protein involved in cell motility. This motility protein is alpha-actinin-4 (ACTN4). It is unclear which regions of MTBP interact with which binding-partner. See PF14918, PF14919.


The actual alignment was detected with superfamily member pfam14920:

Pssm-ID: 464376  Cd Length: 257  Bit Score: 43.17  E-value: 5.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460    52 VTARRPAPSPAQSPEPASIS---RFSGSLATAAAELKRSS-----AYKRARTvspiidenssdVENESRSSPFSQPSSES 123
Cdd:pfam14920   64 PFALSPLPSPAVLSEPGSVPdgeALQSELRTEVSRLKRRSrdldgLYPRKRL-----------AKSESSDSLLSQASGSS 132
                           90       100       110
                   ....*....|....*....|....*....|.
gi 808377460   124 G-EPDnteVTSTQPTPLRQSISSADILHPPH 153
Cdd:pfam14920  133 GhHPA---VESLRRQPERSVSVTSPSLPPPG 160
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
240-1318 2.09e-146

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 466.67  E-value: 2.09e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  240 GDTWYLISRKWYRRWdaacserrdSDPAEKVDVPIGTIDNSDLLDPDSTPALPRLRpginEHIDYEMLPEEGWSLLVQWY 319
Cdd:COG5560    44 CEYAVIFAYAWYEGM---------FDRASCDGGSPGPIVQGPIVDFEPESLKKSLR----EGIDYSIISGAVWQLLVRWY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  320 GSSGPVFARNVIDGLNAGQESVEFYPPVIRLLKLVHDVSV---QGSGVASFSLSVSASVAELKAKAKSALNLGSiaDvDI 396
Cdd:COG5560   111 GLAGLITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSlinLGHDPVPHSASSHGTLRDLSERVMNAFVDPS--D-DF 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  397 RLYFLPEPTDQeLQNGLVSSARVTEegvdivdaGEDKPDSYQPNTTLKSVGIEEIEiNLVVETRQSGRWQTDpaptdnaa 476
Cdd:COG5560   188 RLWDVVPEIMG-LRLGLDSFFRRYR--------VLASDGRVLHPLTRLELFEDRSV-LLLSKITRNPDWLVD-------- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  477 sssvkgifaqqgdffSNLQQNNatagasaasgtaaeaqgrvtrsqtavdRTMGRSRGLRGLNNLGNTCFMNSALQCLSNT 556
Cdd:COG5560   250 ---------------SIVDDHN---------------------------RSINKEAGTCGLRNLGNTCYMNSALQCLMHT 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  557 YELQQYFVSGAYKEELNTDNPLGMGGAIADAFGNLITNIWNGQGGSFWPREFKFALSRFAPQFSGYAQHDSQELLAFLLD 636
Cdd:COG5560   288 WELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLD 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  637 GLHEDLNRILKKPYIEAPDWEGGDEKDLVAFAKRQWDIYKARNDSVIVDLFQGQYRSTLVCPECSKVSIKFDPFMYLTLP 716
Cdd:COG5560   368 GLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLP 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  717 IPNKKMWKGQIYFVPldASQPMHKFQVQLPAGTTVGKLRQKVAAQFGIE--TKRLVCgEVWHHRVYKWFD--DYEPLVDI 792
Cdd:COG5560   448 LPVSMVWKHTIVVFP--ESGRRQPLKIELDASSTIRGLKKLVDAEYGKLgcFEIKVM-CIYYGGNYNMLEpaDKVLLQDI 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  793 KDGDFVYFWevaapprlskqrqfryhrsvEDAEDALDIPeqeyaVLPVFTNvasdtSGPSSSQAFvsrrarseaiGIPFF 872
Cdd:COG5560   525 PQTDFVYLY--------------------ETNDNGIEVP-----VVHLRIE-----KGYKSKRLF----------GDPFL 564
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  873 isvpKADVNDADAIREHVLQGFsrfagvpEELRQAVEHDRTaaapsalppstsqisdwemvddsaagnddaiqvvapsqm 952
Cdd:COG5560   565 ----QLNVLIKASIYDKLVKEF-------EELLVLVEMKKT--------------------------------------- 594
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  953 adsdlvteiredgeavvvpdvstvDADVSSPSVAPLNEFKAPtpsspalrirfsiaelGQGLPKGSESNaDNLSEDLEER 1032
Cdd:COG5560   595 ------------------------DVDLVSEQVRLLREESSP----------------SSWLKLETEID-TKREEQVEEE 633
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1033 HARlakrsasaasslggEEPMKVEadeleaedeskttstdkavplvytggaIVCTWShsvkARGLLVDSDSAQLWgdyee 1112
Cdd:COG5560   634 GQM--------------NFNDAVV---------------------------ISCEWE----EKRYLSLFSYDPLW----- 663
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1113 tvdeAIRQRENAGParpkTLSIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAGRHSRD 1192
Cdd:COG5560   664 ----TIREIGAAER----TITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD 735
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1193 KLNMLVDFPLEGLDLtdrvegtqalrrvqeeakesgeelsesmlgSGILRPLEDNddavavdRPIYDLYAVDNHFGGLGG 1272
Cdd:COG5560   736 KIDDLVEYPIDDLDL------------------------------SGVEYMVDDP-------RLIYDLYAVDNHYGGLSG 778
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*.
gi 808377460 1273 GHYTAFAKSPADGKWYEFDDSSVRPVANSEAVKsSSAYLLFYRRRT 1318
Cdd:COG5560   779 GHYTAYARNFANNGWYLFDDSRITEVDPEDSVT-SSAYVLFYRRKS 823
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1133-1315 1.45e-55

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: 192.89  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1133 SIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAGRHSRDKLNMLVDFPLEGLDLTDRVe 1212
Cdd:cd02674    85 TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV- 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1213 gtqalrrvqeeakesgeelsesmlgsgilrplednDDAVAVDRPIYDLYAVDNHFGGLGGGHYTAFAKSPADGKWYEFDD 1292
Cdd:cd02674   164 -----------------------------------DTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDD 208
                         170       180
                  ....*....|....*....|...
gi 808377460 1293 SSVRPVaNSEAVKSSSAYLLFYR 1315
Cdd:cd02674   209 SRVTKV-SESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
535-723 1.10e-47

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 173.40  E-value: 1.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460   535 RGLNNLGNTCFMNSALQCLSNTYELQQYFVSGaykEELNTDNPLGMGGAIADAFGNLITNIW-NGQGGSFWPREFKFALS 613
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI---SPLSEDSRYNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460   614 RFAPQFSGYAQHDSQELLAFLLDGLHEDLNRILKKpyieapdweggdekdlvafakrqwdiykaRNDSVIVDLFQGQYRS 693
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHST-----------------------------ENESLITDLFRGQLKS 128
                          170       180       190
                   ....*....|....*....|....*....|
gi 808377460   694 TLVCPECSKVSIKFDPFMYLTLPIPNKKMW 723
Cdd:pfam00443  129 RLKCLSCGEVSETFEPFSDLSLPIPGDSAE 158
DUSP smart00695
Domain in ubiquitin-specific proteases;
236-332 6.88e-17

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 77.01  E-value: 6.88e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460    236 PLHAGDTWYLISRKWYRRWdaaCSERRDSDPaekvdVPIGTIDNSDLLDPDSTPalpRLRPGINEHIDYEMLPEEGWSLL 315
Cdd:smart00695    1 PLEEGLTWYLISTRWYRQW---ADFVEGKDG-----KDPGPIDNSGILCSHGGP---RLKEHLVEGEDYVLIPEELWNKL 69
                            90
                    ....*....|....*..
gi 808377460    316 VQWYGSSGPVFARNVID 332
Cdd:smart00695   70 VRWYGGGPGPIPRKVVC 86
MTBP_C pfam14920
MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its ...
52-153 5.84e-04

MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its interaction with p53, plays an important role in the regulation of the G1 checkpoint of the cell cycle. MTBP promotes MDM2-mediated ubiquitination and degradation of p53 and also MDM2 stabilization in an MDM2 RING finger-dependent manner. MTBP differentially regulates the E3 ubiquitin ligase activity of MDM2 towards two of its most critical targets (itself and p53) and in doing so significantly contributes to MDM2-dependent p53 homeostasis in unstressed cells. MTBP inhibits cancer cell migration by interacting with a protein involved in cell motility. This motility protein is alpha-actinin-4 (ACTN4). It is unclear which regions of MTBP interact with which binding-partner. See PF14918, PF14919.


Pssm-ID: 464376  Cd Length: 257  Bit Score: 43.17  E-value: 5.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460    52 VTARRPAPSPAQSPEPASIS---RFSGSLATAAAELKRSS-----AYKRARTvspiidenssdVENESRSSPFSQPSSES 123
Cdd:pfam14920   64 PFALSPLPSPAVLSEPGSVPdgeALQSELRTEVSRLKRRSrdldgLYPRKRL-----------AKSESSDSLLSQASGSS 132
                           90       100       110
                   ....*....|....*....|....*....|.
gi 808377460   124 G-EPDnteVTSTQPTPLRQSISSADILHPPH 153
Cdd:pfam14920  133 GhHPA---VESLRRQPERSVSVTSPSLPPPG 160
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
240-1318 2.09e-146

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 466.67  E-value: 2.09e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  240 GDTWYLISRKWYRRWdaacserrdSDPAEKVDVPIGTIDNSDLLDPDSTPALPRLRpginEHIDYEMLPEEGWSLLVQWY 319
Cdd:COG5560    44 CEYAVIFAYAWYEGM---------FDRASCDGGSPGPIVQGPIVDFEPESLKKSLR----EGIDYSIISGAVWQLLVRWY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  320 GSSGPVFARNVIDGLNAGQESVEFYPPVIRLLKLVHDVSV---QGSGVASFSLSVSASVAELKAKAKSALNLGSiaDvDI 396
Cdd:COG5560   111 GLAGLITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSlinLGHDPVPHSASSHGTLRDLSERVMNAFVDPS--D-DF 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  397 RLYFLPEPTDQeLQNGLVSSARVTEegvdivdaGEDKPDSYQPNTTLKSVGIEEIEiNLVVETRQSGRWQTDpaptdnaa 476
Cdd:COG5560   188 RLWDVVPEIMG-LRLGLDSFFRRYR--------VLASDGRVLHPLTRLELFEDRSV-LLLSKITRNPDWLVD-------- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  477 sssvkgifaqqgdffSNLQQNNatagasaasgtaaeaqgrvtrsqtavdRTMGRSRGLRGLNNLGNTCFMNSALQCLSNT 556
Cdd:COG5560   250 ---------------SIVDDHN---------------------------RSINKEAGTCGLRNLGNTCYMNSALQCLMHT 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  557 YELQQYFVSGAYKEELNTDNPLGMGGAIADAFGNLITNIWNGQGGSFWPREFKFALSRFAPQFSGYAQHDSQELLAFLLD 636
Cdd:COG5560   288 WELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLD 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  637 GLHEDLNRILKKPYIEAPDWEGGDEKDLVAFAKRQWDIYKARNDSVIVDLFQGQYRSTLVCPECSKVSIKFDPFMYLTLP 716
Cdd:COG5560   368 GLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLP 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  717 IPNKKMWKGQIYFVPldASQPMHKFQVQLPAGTTVGKLRQKVAAQFGIE--TKRLVCgEVWHHRVYKWFD--DYEPLVDI 792
Cdd:COG5560   448 LPVSMVWKHTIVVFP--ESGRRQPLKIELDASSTIRGLKKLVDAEYGKLgcFEIKVM-CIYYGGNYNMLEpaDKVLLQDI 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  793 KDGDFVYFWevaapprlskqrqfryhrsvEDAEDALDIPeqeyaVLPVFTNvasdtSGPSSSQAFvsrrarseaiGIPFF 872
Cdd:COG5560   525 PQTDFVYLY--------------------ETNDNGIEVP-----VVHLRIE-----KGYKSKRLF----------GDPFL 564
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  873 isvpKADVNDADAIREHVLQGFsrfagvpEELRQAVEHDRTaaapsalppstsqisdwemvddsaagnddaiqvvapsqm 952
Cdd:COG5560   565 ----QLNVLIKASIYDKLVKEF-------EELLVLVEMKKT--------------------------------------- 594
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  953 adsdlvteiredgeavvvpdvstvDADVSSPSVAPLNEFKAPtpsspalrirfsiaelGQGLPKGSESNaDNLSEDLEER 1032
Cdd:COG5560   595 ------------------------DVDLVSEQVRLLREESSP----------------SSWLKLETEID-TKREEQVEEE 633
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1033 HARlakrsasaasslggEEPMKVEadeleaedeskttstdkavplvytggaIVCTWShsvkARGLLVDSDSAQLWgdyee 1112
Cdd:COG5560   634 GQM--------------NFNDAVV---------------------------ISCEWE----EKRYLSLFSYDPLW----- 663
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1113 tvdeAIRQRENAGParpkTLSIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAGRHSRD 1192
Cdd:COG5560   664 ----TIREIGAAER----TITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD 735
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1193 KLNMLVDFPLEGLDLtdrvegtqalrrvqeeakesgeelsesmlgSGILRPLEDNddavavdRPIYDLYAVDNHFGGLGG 1272
Cdd:COG5560   736 KIDDLVEYPIDDLDL------------------------------SGVEYMVDDP-------RLIYDLYAVDNHYGGLSG 778
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*.
gi 808377460 1273 GHYTAFAKSPADGKWYEFDDSSVRPVANSEAVKsSSAYLLFYRRRT 1318
Cdd:COG5560   779 GHYTAYARNFANNGWYLFDDSRITEVDPEDSVT-SSAYVLFYRRKS 823
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1133-1315 1.45e-55

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: 192.89  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1133 SIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAGRHSRDKLNMLVDFPLEGLDLTDRVe 1212
Cdd:cd02674    85 TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV- 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1213 gtqalrrvqeeakesgeelsesmlgsgilrplednDDAVAVDRPIYDLYAVDNHFGGLGGGHYTAFAKSPADGKWYEFDD 1292
Cdd:cd02674   164 -----------------------------------DTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDD 208
                         170       180
                  ....*....|....*....|...
gi 808377460 1293 SSVRPVaNSEAVKSSSAYLLFYR 1315
Cdd:cd02674   209 SRVTKV-SESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
535-723 1.10e-47

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 173.40  E-value: 1.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460   535 RGLNNLGNTCFMNSALQCLSNTYELQQYFVSGaykEELNTDNPLGMGGAIADAFGNLITNIW-NGQGGSFWPREFKFALS 613
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI---SPLSEDSRYNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460   614 RFAPQFSGYAQHDSQELLAFLLDGLHEDLNRILKKpyieapdweggdekdlvafakrqwdiykaRNDSVIVDLFQGQYRS 693
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHST-----------------------------ENESLITDLFRGQLKS 128
                          170       180       190
                   ....*....|....*....|....*....|
gi 808377460   694 TLVCPECSKVSIKFDPFMYLTLPIPNKKMW 723
Cdd:pfam00443  129 RLKCLSCGEVSETFEPFSDLSLPIPGDSAE 158
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1126-1314 1.11e-47

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 173.40  E-value: 1.11e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  1126 PARPKTLSIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAGRHSRDKLNMLVDFPLEgL 1205
Cdd:pfam00443  156 SAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-L 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  1206 DLTdrvegtqalrrvqeeakesgeelsesmlgsgilRPLEDNDDAVAVDRPIYDLYAVDNHFGGLGGGHYTAFAKSPADG 1285
Cdd:pfam00443  235 DLS---------------------------------RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENN 281
                          170       180
                   ....*....|....*....|....*....
gi 808377460  1286 KWYEFDDSSVRPVANSEAVKSSSAYLLFY 1314
Cdd:pfam00443  282 RWYKFDDEKVTEVDEETAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1130-1315 4.96e-37

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: 140.70  E-value: 4.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1130 KTLSIEDCMDEFTREEQLGEDDPWYCPpCKEFRQATKKFDLWKAPDILVVHLKRFSAGRHSR-DKLNMLVDFPLEgLDLT 1208
Cdd:cd02257    97 PQVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTkEKLNTKVSFPLE-LDLS 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1209 DRVEGtqalrrvqeeakesgeelsesmlgsgilrplEDNDDAVAVDRPIYDLYAVDNHFGGLG-GGHYTAFAKSPADGKW 1287
Cdd:cd02257   175 PYLSE-------------------------------GEKDSDSDNGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKW 223
                         170       180       190
                  ....*....|....*....|....*....|..
gi 808377460 1288 YEFDDSSVRPVANSEAVK----SSSAYLLFYR 1315
Cdd:cd02257   224 YKFNDDKVTEVSEEEVLEfgslSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1133-1314 2.85e-30

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: 122.38  E-value: 2.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1133 SIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAGRhsRDKLNMLVDFPLEgLDLTDRVE 1212
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GGKINKQISFPET-LDLSPYMS 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1213 GTQAlrrvqeeakesgeelsesmlGSgilrplednddavavdrPIYDLYAVDNHFGGLG-GGHYTAFAKSpADGKWYEFD 1291
Cdd:cd02661   240 QPND--------------------GP-----------------LKYKLYAVLVHSGFSPhSGHYYCYVKS-SNGKWYNMD 281
                         170       180
                  ....*....|....*....|...
gi 808377460 1292 DSSVRPVaNSEAVKSSSAYLLFY 1314
Cdd:cd02661   282 DSKVSPV-SIETVLSQKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1125-1314 2.47e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 117.47  E-value: 2.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1125 GPARPKTLSieDCMDEFTREEQLGEDDpWYCPPCKEFRQATKKFDLWKAPDILVVHLKRF--SAGRHSRdKLNMLVDFPL 1202
Cdd:cd02660   171 GVSGTPTLS--DCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFehSLNKTSR-KIDTYVQFPL 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1203 EgLDLTDRVegtqalrrvqeeAKESGEELSESmlgsgilrplEDNDDAvavdrpIYDLYAVDNHFGGLGGGHYTAFAKSp 1282
Cdd:cd02660   247 E-LNMTPYT------------SSSIGDTQDSN----------SLDPDY------TYDLFAVVVHKGTLDTGHYTAYCRQ- 296
                         170       180       190
                  ....*....|....*....|....*....|..
gi 808377460 1283 ADGKWYEFDDSSVRPVANSEAVKsSSAYLLFY 1314
Cdd:cd02660   297 GDGQWFKFDDAMITRVSEEEVLK-SQAYLLFY 327
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-721 1.80e-25

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: 106.22  E-value: 1.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLSNTyelqqyfvsgaykeelntdnplgmggaiadafgnlitniwngqggsfwprefkfalsrf 615
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  616 apqfsgyaQHDSQELLAFLLDGLHedlnrilkkpyieapdweggdekdlvafakrqwdiykarndSVIVDLFQGQYRSTL 695
Cdd:cd02674    22 --------QQDAQEFLLFLLDGLH-----------------------------------------SIIVDLFQGQLKSRL 52
                         170       180
                  ....*....|....*....|....*.
gi 808377460  696 VCPECSKVSIKFDPFMYLTLPIPNKK 721
Cdd:cd02674    53 TCLTCGKTSTTFEPFTYLSLPIPSGS 78
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1133-1315 2.17e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 104.78  E-value: 2.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1133 SIEDCMDEFTREEQLGEDDPWYCPPCKEfrqATKKFDLWKAPDILVVHLKRFSA-GRHSRDKLNMLVDFPlEGLDLTdrv 1211
Cdd:cd02667   112 SIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQpRSANLRKVSRHVSFP-EILDLA--- 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1212 EGTQALRRVQEEakesgeelsesmlgsgilrplednddavaVDRPIYDLYAVDNHFGGLGGGHYTAFAKS---------- 1281
Cdd:cd02667   185 PFCDPKCNSSED-----------------------------KSSVLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdl 235
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 808377460 1282 -----------PADGKWYEFDDSSVRPVANSEaVKSSSAYLLFYR 1315
Cdd:cd02667   236 tkskpaadeagPGSGQWYYISDSDVREVSLEE-VLKSEAYLLFYE 279
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
535-725 6.76e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 104.38  E-value: 6.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  535 RGLNNLGNTCFMNSALQCLSNTYELQQYFVSGAYKEELNTDNPLG-MGGAIADAFGNLITNiwnGQGGSFWPREFKFALS 613
Cdd:cd02660     1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNScLSCAMDEIFQEFYYS---GDRSPYGPINLLYLSW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  614 RFAPQFSGYAQHDSQELLAFLLDGLHEDLNRILKKPyieapdwegGDEKDLVAFAKRqwdiykarndsvivdLFQGQYRS 693
Cdd:cd02660    78 KHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------NDESHCNCIIHQ---------------TFSGSLQS 133
                         170       180       190
                  ....*....|....*....|....*....|..
gi 808377460  694 TLVCPECSKVSIKFDPFMYLTLPIPNKKMWKG 725
Cdd:cd02660   134 SVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSW 165
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
535-719 7.10e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 103.89  E-value: 7.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  535 RGLNNLGNTCFMNSALQCLSNTYELQQYFVSGAYKEELNTDNPlGMGGAIADafgNLITNIWNGqGGSFWPREFKFALSR 614
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGF-CMMCALEA---HVERALASS-GPGSAPRIFSSNLKQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  615 FAPQFSGYAQHDSQELLAFLLDGLHEDLNRILKKPYIEAPdweggdekdlvafakrqwdiyKARNDSVIVDLFQGQYRST 694
Cdd:cd02661    77 ISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDP---------------------SSQETTLVQQIFGGYLRSQ 135
                         170       180
                  ....*....|....*....|....*
gi 808377460  695 LVCPECSKVSIKFDPFMYLTLPIPN 719
Cdd:cd02661   136 VKCLNCKHVSNTYDPFLDLSLDIKG 160
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1133-1316 2.33e-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: 103.11  E-value: 2.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1133 SIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAG--RHSRDKLNMLVDFPLEgLDLTDR 1210
Cdd:cd02659   152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLE-LDMEPY 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1211 VEGTQALRRVQEEAKESGEElsesmlgsgilrplednddavavdrpIYDLYAVDNHFGGLGGGHYTAFAKSPADGKWYEF 1290
Cdd:cd02659   231 TEKGLAKKEGDSEKKDSESY--------------------------IYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKF 284
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 808377460 1291 DDSSVRPVANSEA---------------------VKSSSAYLLFYRR 1316
Cdd:cd02659   285 NDDVVTPFDPNDAeeecfggeetqktydsgprafKRTTNAYMLFYER 331
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
536-721 4.41e-22

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: 97.17  E-value: 4.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLSNTyelqqyfvsgaykeelntdnplgmggaiadafgnlitniwngqggsfwprefkfalsrf 615
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  616 apqfsgyaQHDSQELLAFLLDGLHEDLNRILKKpyieapdweggdekdlvafakrqwDIYKARNDSVIVDLFQGQYRSTL 695
Cdd:cd02257    22 --------QQDAHEFLLFLLDKLHEELKKSSKR------------------------TSDSSSLKSLIHDLFGGKLESTI 69
                         170       180
                  ....*....|....*....|....*.
gi 808377460  696 VCPECSKVSIKFDPFMYLTLPIPNKK 721
Cdd:cd02257    70 VCLECGHESVSTEPELFLSLPLPVKG 95
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1133-1314 3.41e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 92.76  E-value: 3.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1133 SIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRF----SAGRHSrdKLNMLVDFPLEgldlt 1208
Cdd:cd02663   148 SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkydeQLNRYI--KLFYRVVFPLE----- 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1209 drvegtqalrrvqeeakesgeelsesmlgsgiLRPLEDNDDAVAVDRpIYDLYAVDNHFGglGG---GHYTAFAKSpaDG 1285
Cdd:cd02663   221 --------------------------------LRLFNTTDDAENPDR-LYELVAVVVHIG--GGpnhGHYVSIVKS--HG 263
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 808377460 1286 KWYEFDDSSVRPVaNSEAVK--------SSSAYLLFY 1314
Cdd:cd02663   264 GWLLFDDETVEKI-DENAVEeffgdspnQATAYVLFY 299
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
240-331 8.45e-20

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 85.11  E-value: 8.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460   240 GDTWYLISRKWYRRWdaacserrdSDPAEKVDVPIGTIDNSDLLDPDSTPalpRLRPGINEHIDYEMLPEEGWSLLVQWY 319
Cdd:pfam06337    1 GDKVYLISSKWLNKW---------KSYVKEPNNEPGPIDNSDLLDDESNG---QLKPNLQEGVDYVIVPEEVWEFLVEWY 68
                           90
                   ....*....|..
gi 808377460   320 GsSGPVFARNVI 331
Cdd:pfam06337   69 G-GGPEIKRNVV 79
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-718 5.35e-18

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: 85.90  E-value: 5.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLSNTYELQQYFvsgayKEElntdnplgmggaiadafgnlitniwngqggsfwPREFKFALSRF 615
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELL-----SET---------------------------------PKELFSQVCRK 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  616 APQFSGYAQHDSQELLAFLLDGLhedlnrilkkpyieapdweggdekdlvafakrqwdiykarnDSVIVDLFQGQYRSTL 695
Cdd:cd02667    43 APQFKGYQQQDSHELLRYLLDGL-----------------------------------------RTFIDSIFGGELTSTI 81
                         170       180
                  ....*....|....*....|...
gi 808377460  696 VCPECSKVSIKFDPFMYLTLPIP 718
Cdd:cd02667    82 MCESCGTVSLVYEPFLDLSLPRS 104
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1131-1315 2.25e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 85.16  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1131 TLSIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAGRHS--RDKLNMLVDFPLEgLDLt 1208
Cdd:cd02668   155 HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTgaKKKLNASISFPEI-LDM- 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1209 drvegtqalrrvqeeakesGEELSESMLGSGilrplednddavavdrpIYDLYAVDNHFG-GLGGGHYTAFAKSPADGKW 1287
Cdd:cd02668   233 -------------------GEYLAESDEGSY-----------------VYELSGVLIHQGvSAYSGHYIAHIKDEQTGEW 276
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 808377460 1288 YEFDDSSVRPV-------ANSEAVK-------------SSSAYLLFYR 1315
Cdd:cd02668   277 YKFNDEDVEEMpgkplklGNSEDPAkprkseikkgthsSRTAYMLVYK 324
DUSP smart00695
Domain in ubiquitin-specific proteases;
236-332 6.88e-17

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 77.01  E-value: 6.88e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460    236 PLHAGDTWYLISRKWYRRWdaaCSERRDSDPaekvdVPIGTIDNSDLLDPDSTPalpRLRPGINEHIDYEMLPEEGWSLL 315
Cdd:smart00695    1 PLEEGLTWYLISTRWYRQW---ADFVEGKDG-----KDPGPIDNSGILCSHGGP---RLKEHLVEGEDYVLIPEELWNKL 69
                            90
                    ....*....|....*..
gi 808377460    316 VQWYGSSGPVFARNVID 332
Cdd:smart00695   70 VRWYGGGPGPIPRKVVC 86
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-717 4.13e-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 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: 74.67  E-value: 4.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLSNTYELQQ---YFVSGAYKEELNTDNPLgmgGAIADAFGNLitniwNGQGGSFWPREFKFAL 612
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGANQSSDNLT---NALRDLFDTM-----DKKQEPVPPIEFLQLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  613 SRFAPQFS------GYAQHDSQELLAFLLdglhEDLNRILKKPYIEapdweggdekdlvafakrqwdiykarnDSVIVDL 686
Cdd:cd02657    73 RMAFPQFAekqnqgGYAQQDAEECWSQLL----SVLSQKLPGAGSK---------------------------GSFIDQL 121
                         170       180       190
                  ....*....|....*....|....*....|..
gi 808377460  687 FQGQYRSTLVCPECSKV-SIKFDPFMYLTLPI 717
Cdd:cd02657   122 FGIELETKMKCTESPDEeEVSTESEYKLQCHI 153
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1257-1316 3.32e-13

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 71.76  E-value: 3.32e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808377460 1257 IYDLYAVDNHFGGLGGGHYTAFAKSpaDGKWYEFDDSSVRPVA--NSEAVKSSSAYLLFYRR 1316
Cdd:COG5533   224 YYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSDVTPVSeeEAINEKAKNAYLYFYER 283
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1133-1315 7.69e-13

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: 71.37  E-value: 7.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1133 SIEDCMDEFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFS--AGRHSRDKLNMLVDFPlEGLDLTDR 1210
Cdd:cd02664   135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIMDNVSIN-EVLSLPVR 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1211 VEGTQALRRVQEEAKESGEelsesmlgsgilrplednDDAVAVDRPIYDLYAVDNHFG-GLGGGHYTAFAKSPADGK--- 1286
Cdd:cd02664   214 VESKSSESPLEKKEEESGD------------------DGELVTRQVHYRLYAVVVHSGySSESGHYFTYARDQTDADstg 275
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 808377460 1287 -----------------WYEFDDSSV-----RPVANSEAVKSS-SAYLLFYR 1315
Cdd:cd02664   276 qecpepkdaeendesknWYLFNDSRVtfssfESVQNVTSRFPKdTPYILFYE 327
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1140-1315 8.83e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 64.91  E-value: 8.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1140 EFTREEQLGEDDPWYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAGRHSRD------KLNMLVDFPLegldltdrveg 1213
Cdd:cd02671   188 QFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDcygglsKVNTPLLTPL----------- 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1214 tqalrrvqeeaKESGEELSESMlgsgilrplednddavavDRPIYDLYAVDNHFGG-LGGGHYTAFAKspadgkWYEFDD 1292
Cdd:cd02671   257 -----------KLSLEEWSTKP------------------KNDVYRLFAVVMHSGAtISSGHYTAYVR------WLLFDD 301
                         170       180       190
                  ....*....|....*....|....*....|.
gi 808377460 1293 SSVRPVANSEAVKS--------SSAYLLFYR 1315
Cdd:cd02671   302 SEVKVTEEKDFLEAlspntsstSTPYLLFYK 332
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-718 1.12e-10

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: 64.65  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLSNTYELQQYFVSGAYKEELNTDNP---LGMGGA-IADAF--------GNLITNIWNGQGGsF 603
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPandLNCQLIkLADGLlsgryskpASLKSENDPYQVG-I 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  604 WPREFKFALSRFAPQFSGYAQHDSQELLAFLLDGLHEDLNRILKKPyieapdweggdekdlvafakrqwdiykarndsvI 683
Cdd:cd02658    80 KPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLN---------------------------------P 126
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 808377460  684 VDLFQGQYRSTLVCPECSKVSIKFDPFMYLTLPIP 718
Cdd:cd02658   127 NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVP 161
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-719 7.62e-10

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: 61.94  E-value: 7.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLsntyelqqyfvsgaYKEELNTdnplgmggAIADAFGNLITNiwNGQGGSFWPREFKFALSRF 615
Cdd:cd02663     1 GLENFGNTCYCNSVLQAL--------------YFENLLT--------CLKDLFESISEQ--KKRTGVISPKKFITRLKRE 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  616 APQFSGYAQHDSQELLAFLLDGLHEDL---NRILKKPYIEAPDWEGGDEKDLVAfakrqwdiykarndsvivDLFQGQYR 692
Cdd:cd02663    57 NELFDNYMHQDAHEFLNFLLNEIAEILdaeRKAEKANRKLNNNNNAEPQPTWVH------------------EIFQGILT 118
                         170       180
                  ....*....|....*....|....*..
gi 808377460  693 STLVCPECSKVSIKFDPFMYLTLPIPN 719
Cdd:cd02663   119 NETRCLTCETVSSRDETFLDLSIDVEQ 145
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-718 2.39e-09

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: 60.58  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLSNTYELQQYFVSgaYKEELNTDNPLGMGGAIADAFGNLITniwngQGGSFWPREFKFALSRf 615
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS--LNLPRLGDSQSVMKKLQLLQAHLMHT-----QRRAEAPPDYFLEASR- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  616 APQFSGYAQHDSQELLAFLLDGLHedlnrilkkpyieapdweggdekdlvafakrqwdiykarndSVIVDLFQGQYRSTL 695
Cdd:cd02664    73 PPWFTPGSQQDCSEYLRYLLDRLH-----------------------------------------TLIEKMFGGKLSTTI 111
                         170       180
                  ....*....|....*....|...
gi 808377460  696 VCPECSKVSIKFDPFMYLTLPIP 718
Cdd:cd02664   112 RCLNCNSTSARTERFRDLDLSFP 134
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1174-1315 3.43e-09

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: 60.04  E-value: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1174 PDILVVHLKRFSAGRHSRDKLNML--VDFPLEgLDLTDRVEGtqalrrvqeeakesgeelsesmlgSGIlrplednddav 1251
Cdd:cd02657   197 PKYLTVQFVRFFWKRDIQKKAKILrkVKFPFE-LDLYELCTP------------------------SGY----------- 240
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808377460 1252 avdrpiYDLYAVDNHFG-GLGGGHYTAFAKSPADGKWYEFDDSSVRPVANSEAVKSS------SAYLLFYR 1315
Cdd:cd02657   241 ------YELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhIAYILLYK 305
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1131-1314 1.01e-08

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: 57.76  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1131 TLSIEDCMDEFTREEQLgeDDPwYCPPCKEFrqatkkfdLWKAPDILVVHLKRFSAGRH---SRDKLNmlVDFPlegldl 1207
Cdd:cd02662    95 GTTLEHCLDDFLSTEII--DDY-KCDRCQTV--------IVRLPQILCIHLSRSVFDGRgtsTKNSCK--VSFP------ 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1208 tdrvegtqalrrvqeeakesgEELSesmlgsgilrplednddavavdRPIYDLYAVDNHFGGLGGGHYTAFAKSPA---- 1283
Cdd:cd02662   156 ---------------------ERLP----------------------KVLYRLRAVVVHYGSHSSGHYVCYRRKPLfskd 192
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 808377460 1284 ----------------DGKWYEFDDSSVRPVANSEAVKSSSAYLLFY 1314
Cdd:cd02662   193 kepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQKSAYMLFY 239
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-640 3.43e-08

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: 57.21  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLsntyelqqYFVSGaYKEelNTDNPLGMGGAIADAFGNLITN--IWNGQGGSFWPREFKFALS 613
Cdd:cd02671    26 GLNNLGNTCYLNSVLQVL--------YFCPG-FKH--GLKHLVSLISSVEQLQSSFLLNpeKYNDELANQAPRRLLNALR 94
                          90       100
                  ....*....|....*....|....*..
gi 808377460  614 RFAPQFSGYAQHDSQELLAFLLDGLHE 640
Cdd:cd02671    95 EVNPMYEGYLQHDAQEVLQCILGNIQE 121
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1132-1315 4.11e-08

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: 56.56  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1132 LSIEDCMDEFTREEQLgEDdpwYCPPCKEFRQATKKFDLWKAPDILVVHLKRFSAGRHSRD-KLNMLVDFPLegldltdr 1210
Cdd:cd02658   178 VPLEDCLKAYFAPETI-ED---FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDVPE-------- 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1211 vegtqalrrvqeeakesgeelsesMLGSGilrplednddavavdrpIYDLYAVDNHFG-GLGGGHYTAFAKSPAD--GKW 1287
Cdd:cd02658   246 ------------------------ELGPG-----------------KYELIAFISHKGtSVHSGHYVAHIKKEIDgeGKW 284
                         170       180
                  ....*....|....*....|....*...
gi 808377460 1288 YEFDDSSVRPVANSEAVKsSSAYLLFYR 1315
Cdd:cd02658   285 VLFNDEKVVASQDPPEMK-KLGYIYFYQ 311
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
533-727 5.06e-08

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: 56.94  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  533 GLRGLNNLGNTCFMNSALQCLSNTYELQQYFvsgaykeeLNTDNPLGMG---GAIADAFGNLITNIWNgqggsfwPREFK 609
Cdd:cd02669   118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFF--------LLYENYENIKdrkSELVKRLSELIRKIWN-------PRNFK 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  610 falSRFAPQ-------------FSGYAQHDSQELLAFLLDGLHEDLNRilkkpyieapdweggdekdlvafakrqwdiYK 676
Cdd:cd02669   183 ---GHVSPHellqavskvskkkFSITEQSDPVEFLSWLLNTLHKDLGG------------------------------SK 229
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808377460  677 ARNDSVIVDLFQG--QYRSTLVCPECSKVSIKFD-------------PFMYLTLPIPNKKMWKGQI 727
Cdd:cd02669   230 KPNSSIIHDCFQGkvQIETQKIKPHAEEEGSKDKffkdsrvkktsvsPFLLLTLDLPPPPLFKDGN 295
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
536-642 1.31e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 54.81  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLS------NTYELQQYFVSGAYKEELNTDNP-LGMGGAIAdafgnLITNIWNgqggsfwprEF 608
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlylpklDELLDDLSKELKVLKNVIRKPEPdLNQEEALK-----LFTALWS---------SK 66
                          90       100       110
                  ....*....|....*....|....*....|....
gi 808377460  609 KFALSRFAPQfsgYAQHDSQELLAFLLDGLHEDL 642
Cdd:COG5533    67 EHKVGWIPPM---GSQEDAHELLGKLLDELKLDL 97
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1133-1317 1.40e-07

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 56.42  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1133 SIEDCMDEFTREEQLGEDDPWYCPPcKEFRQATKKFDLWKAPDILVVHLKRFSAGrHSRD---KLNMLVDFPLEgLDLtd 1209
Cdd:COG5077   339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYD-FERDmmvKINDRYEFPLE-IDL-- 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1210 rvegtqaLRRVQEEAKESgeelsesmlgsgilrpleDNDDAVavdrpiYDLYAVDNHFGGLGGGHYTAFAKSPADGKWYE 1289
Cdd:COG5077   414 -------LPFLDRDADKS------------------ENSDAV------YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYK 462
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 808377460 1290 FDDSSVRPVANSEAV---------------------KSSSAYLLFYRRR 1317
Cdd:COG5077   463 FDDTRVTRATEKEVLeenfggdhpykdkirdhsgikRFMSAYMLVYLRK 511
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-717 7.46e-06

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: 49.73  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLSNTYELQQYFV-----SGAYKEELNTDNPLGMGGAIaDAFGNLITNIWNGQGGSFWPREFKF 610
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnstEDAELKNMPPDKPHEPQTII-DQLQLIFAQLQFGNRSVVDPSGFVK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  611 ALSrfapqFSGYAQHDSQELLAFLLDGLHEDLNRILKKpyieapdweggdekdlvafakrqwdiyKARNdsVIVDLFQGQ 690
Cdd:cd02668    80 ALG-----LDTGQQQDAQEFSKLFLSLLEAKLSKSKNP---------------------------DLKN--IVQDLFRGE 125
                         170       180
                  ....*....|....*....|....*..
gi 808377460  691 YRSTLVCPECSKVSIKFDPFMYLTLPI 717
Cdd:cd02668   126 YSYVTQCSKCGRESSLPSKFYELELQL 152
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1158-1315 7.85e-06

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: 50.01  E-value: 7.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1158 CKEFRQATKKFDLWKAPDILVVHLKRFSAGRHSRDKLNMLVDFPLEGLDLTDRVegtqalrrvqeeakesgeelsesmlg 1237
Cdd:cd02669   317 ETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYV-------------------------- 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1238 sgilrpledNDDAVAVDRPI-YDLYAVDNHFGGLGG-GHYTAFAKSPADGKWYEFDDSSVRPVaNSEAVKSSSAYLLFYR 1315
Cdd:cd02669   371 ---------HFDKPSLNLSTkYNLVANIVHEGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEV-LPQLIFLSESYIQIWE 440
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1169-1315 1.42e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 48.29  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1169 DLWKAPDILVVHLKRFSAGRHSRDKLNMLVDFPLEgLDLTDRVEGT-QALRRVQEEAKESGEElsesmlgsgilrpleDN 1247
Cdd:cd02670    94 VFAKAPSCLIICLKRYGKTEGKAQKMFKKILIPDE-IDIPDFVADDpRACSKCQLECRVCYDD---------------KD 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460 1248 DDAVAVDRPIYDLYAVDNHFGGLGGGHYTAFAKS-----------PADGKWYEFDDSSVRPVANSE-----AVKSSSAYL 1311
Cdd:cd02670   158 FSPTCGKFKLSLCSAVCHRGTSLETGHYVAFVRYgsysltetdneAYNAQWVFFDDMADRDGVSNGfnipaARLLEDPYM 237

                  ....
gi 808377460 1312 LFYR 1315
Cdd:cd02670   238 LFYQ 241
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1256-1314 5.16e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 46.37  E-value: 5.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808377460 1256 PIYDLYAVDNHFG-GLGGGHYTAFAKSPADG-KWYEFDDSSVRPVANSEAVKS--SSAYLLFY 1314
Cdd:cd02673   182 AKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDVSTNarSSGYLIFY 244
MTBP_C pfam14920
MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its ...
52-153 5.84e-04

MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its interaction with p53, plays an important role in the regulation of the G1 checkpoint of the cell cycle. MTBP promotes MDM2-mediated ubiquitination and degradation of p53 and also MDM2 stabilization in an MDM2 RING finger-dependent manner. MTBP differentially regulates the E3 ubiquitin ligase activity of MDM2 towards two of its most critical targets (itself and p53) and in doing so significantly contributes to MDM2-dependent p53 homeostasis in unstressed cells. MTBP inhibits cancer cell migration by interacting with a protein involved in cell motility. This motility protein is alpha-actinin-4 (ACTN4). It is unclear which regions of MTBP interact with which binding-partner. See PF14918, PF14919.


Pssm-ID: 464376  Cd Length: 257  Bit Score: 43.17  E-value: 5.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460    52 VTARRPAPSPAQSPEPASIS---RFSGSLATAAAELKRSS-----AYKRARTvspiidenssdVENESRSSPFSQPSSES 123
Cdd:pfam14920   64 PFALSPLPSPAVLSEPGSVPdgeALQSELRTEVSRLKRRSrdldgLYPRKRL-----------AKSESSDSLLSQASGSS 132
                           90       100       110
                   ....*....|....*....|....*....|.
gi 808377460   124 G-EPDnteVTSTQPTPLRQSISSADILHPPH 153
Cdd:pfam14920  133 GhHPA---VESLRRQPERSVSVTSPSLPPPG 160
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-726 1.42e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 41.97  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  536 GLNNLGNTCFMNSALQCLSNTyelqQYFVSgaYKEELNtdnplgmggaiadafgnlitniwngqggsfwprefkfalsrf 615
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASL----PSLIE--YLEEFL------------------------------------------ 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808377460  616 apqfsgyAQHDSQELLAFLLDGLHedlnrilkkpyieapdweggdekDLVAFakrqwdiykarndsvivdLFQGQYRSTL 695
Cdd:cd02662    33 -------EQQDAHELFQVLLETLE-----------------------QLLKF------------------PFDGLLASRI 64
                         170       180       190
                  ....*....|....*....|....*....|..
gi 808377460  696 VCPECSKVS-IKFDPFMYLTLPIPNKKMWKGQ 726
Cdd:cd02662    65 VCLQCGESSkVRYESFTMLSLPVPNQSSGSGT 96
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1258-1314 4.56e-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: 40.94  E-value: 4.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808377460 1258 YDLYAVDNHFGGLGGGHYTAFAKSPADGKWYEFDDSSVRPVANSEAVK---SSSA--YLLFY 1314
Cdd:cd02666   281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVFLftlGNTAtpYFLVY 342
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1258-1314 7.52e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 39.85  E-value: 7.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808377460 1258 YDLYAVDNHFGGLGGGHYTAFAKSPADGKWYEFDDSSVRPVANSEAVKSS-------SAYLLFY 1314
Cdd:cd02665   164 YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgggrnpSAYCLMY 227
 
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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