|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-418 |
0e+00 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 568.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYtkGDGIHGGKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQL 249
Cdd:cd02668 79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 250 TDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEPY-VE 328
Cdd:cd02668 159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 329 HKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDlepsKSQTRKPKCGKGTHC 408
Cdd:cd02668 239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSED----PAKPRKSEIKKGTHS 314
|
330
....*....|
gi 1039766797 409 SRNAYMLVYR 418
Cdd:cd02668 315 SRTAYMLVYK 324
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-417 |
1.05e-60 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 209.99 E-value: 1.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIHggkdyepqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------LLCALRDLFkALQKNSKSSSVSPKM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYE 238
Cdd:pfam00443 72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 239 LELNIQGHK------QLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 313 AYIGFSESLDMEPYV-----EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKmegkklqlgIE 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTE---------VD 295
|
330 340 350
....*....|....*....|....*....|
gi 1039766797 388 EDLEPSksqtrkpkcgkgthcSRNAYMLVY 417
Cdd:pfam00443 296 EETAVL---------------SSSAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-457 |
1.12e-45 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 179.30 E-value: 1.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 72 FHSIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDytkgdgihgGKDyepqTICEHLQYL 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPR---------GRD----SVALALQRL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNVVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077 244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 229 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 309 KKLNAYIGFSESLDMEPYVEH-----KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMegkklq 383
Cdd:COG5077 399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVTRA------ 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 384 lGIEEDLEPSKSQTR--KPKCGKGTHCSR--NAYMLVYRLQAQEkNHTM-----VQVPAFLQELVDRDNSKFEEWCVEMA 454
Cdd:COG5077 472 -TEKEVLEENFGGDHpyKDKIRDHSGIKRfmSAYMLVYLRKSML-DDLLnpvaaVDIPPHVEEVLSEEIDKTEVRCKEID 549
|
...
gi 1039766797 455 EMR 457
Cdd:COG5077 550 EIH 552
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
957-1052 |
3.17e-40 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.
Pssm-ID: 340493 [Multi-domain] Cd Length: 99 Bit Score: 143.58 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 957 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1033
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
|
90
....*....|....*....
gi 1039766797 1034 DVMQVCMPEEGFKGTGLLG 1052
Cdd:cd01795 81 DVSRARVPEEGFKGTALLG 99
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
483-553 |
9.05e-10 |
|
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: 56.22 E-value: 9.05e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766797 483 EPYEFVSLEWLQKWL----DESTPTKPIDNN--ACLCSHDKLHPDKISIMK--RISEYAANIFYSRYGGGPRLTVKALC 553
Cdd:pfam06337 2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
482-555 |
9.84e-06 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 45.04 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 482 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNNACLCSHD--KLHPDKI--SIMKRISEYAANIFYSRYGGGPR-LTVKA 551
Cdd:smart00695 5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84
|
....
gi 1039766797 552 LCKD 555
Cdd:smart00695 85 VCQG 88
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
962-1020 |
1.14e-05 |
|
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: 44.17 E-value: 1.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766797 962 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1020
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
967-1020 |
1.22e-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: 38.31 E-value: 1.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1039766797 967 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDcATLGTLGVIPESVILL 1020
Cdd:pfam00240 15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDD-QTLGEYGIEDGSTIHL 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-418 |
0e+00 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 568.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYtkGDGIHGGKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQL 249
Cdd:cd02668 79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 250 TDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEPY-VE 328
Cdd:cd02668 159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 329 HKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDlepsKSQTRKPKCGKGTHC 408
Cdd:cd02668 239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSED----PAKPRKSEIKKGTHS 314
|
330
....*....|
gi 1039766797 409 SRNAYMLVYR 418
Cdd:cd02668 315 SRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
88-418 |
1.75e-79 |
|
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: 262.96 E-value: 1.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 88 FVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdytkgdgihGGKDYEPQTICeHLQYLFALLQNSNRRYIDPSG 167
Cdd:cd02659 2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-----------EDDDDNKSVPL-ALQRLFLFLQLSESPVKTTEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELN 242
Cdd:cd02659 70 TDKTRSfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 243 IQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLD 322
Cdd:cd02659 147 VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 323 MEPYVEH------------KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKM---EGKKLQLGIE 387
Cdd:cd02659 227 MEPYTEKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGE 305
|
330 340 350
....*....|....*....|....*....|.
gi 1039766797 388 EDLEPSKSQTRKpkcGKGTHcsrNAYMLVYR 418
Cdd:cd02659 306 ETQKTYDSGPRA---FKRTT---NAYMLFYE 330
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-417 |
1.05e-60 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 209.99 E-value: 1.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIHggkdyepqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------LLCALRDLFkALQKNSKSSSVSPKM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYE 238
Cdd:pfam00443 72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 239 LELNIQGHK------QLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 313 AYIGFSESLDMEPYV-----EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKmegkklqlgIE 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTE---------VD 295
|
330 340 350
....*....|....*....|....*....|
gi 1039766797 388 EDLEPSksqtrkpkcgkgthcSRNAYMLVY 417
Cdd:pfam00443 296 EETAVL---------------SSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
90-418 |
6.21e-58 |
|
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: 200.02 E-value: 6.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNtflqvwflnlelrqalylcpSTcsdytkgdgihggkdyepqticehLQYLFAllqnsnrryidpsgfv 169
Cdd:cd02257 1 GLNNLGNTCYLN--------------------SV------------------------LQALFS---------------- 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 170 kalgldtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQ 244
Cdd:cd02257 21 --------EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 245 GHKQ----LTDCISEFLKEERLEGDNRYFCEnCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNAYIGFSES 320
Cdd:cd02257 93 VKGLpqvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 321 LDMEPYVEHKG-------GSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgiEEDLEps 393
Cdd:cd02257 171 LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVL-- 240
|
330 340
....*....|....*....|....*
gi 1039766797 394 ksqtrkpkcgKGTHCSRNAYMLVYR 418
Cdd:cd02257 241 ----------EFGSLSSSAYILFYE 255
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-457 |
1.12e-45 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 179.30 E-value: 1.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 72 FHSIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDytkgdgihgGKDyepqTICEHLQYL 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPR---------GRD----SVALALQRL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNVVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077 244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 229 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 309 KKLNAYIGFSESLDMEPYVEH-----KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMegkklq 383
Cdd:COG5077 399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVTRA------ 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 384 lGIEEDLEPSKSQTR--KPKCGKGTHCSR--NAYMLVYRLQAQEkNHTM-----VQVPAFLQELVDRDNSKFEEWCVEMA 454
Cdd:COG5077 472 -TEKEVLEENFGGDHpyKDKIRDHSGIKRfmSAYMLVYLRKSML-DDLLnpvaaVDIPPHVEEVLSEEIDKTEVRCKEID 549
|
...
gi 1039766797 455 EMR 457
Cdd:COG5077 550 EIH 552
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
178-418 |
4.30e-43 |
|
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: 156.68 E-value: 4.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 178 QQQDAQEFsklfMSLLEDTLskqknpdvRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNI-----QGHKQ-LTD 251
Cdd:cd02674 21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 252 CISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHKKKLNAYIGFS-ESLDMEPYV--E 328
Cdd:cd02674 89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPlNDLDLTPYVdtR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 329 HKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgieedlepsksqtrkpkcgKGTHC 408
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS-------------------------ESSVV 220
|
250
....*....|
gi 1039766797 409 SRNAYMLVYR 418
Cdd:cd02674 221 SSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-417 |
6.96e-43 |
|
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: 158.59 E-value: 6.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQVwflnleLRQALYL---CPStcSDYTKGDGIHGGKdyepqTICEHLQYLFALLQNSnRRYIDPS 166
Cdd:cd02661 3 GLQNLGNTCFLNSVLQC------LTHTPPLanyLLS--REHSKDCCNEGFC-----MMCALEAHVERALASS-GPGSAPR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 167 GFVKAL-----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NVVQQQFCGEYAYVTVCNQCGRESKLV 233
Cdd:cd02661 69 IFSSNLkqiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKHVSNTY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 234 SKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHkkKLNA 313
Cdd:cd02661 149 DPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 314 YIGFSESLDMEPYV-EHKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPqSGEWYKFNDEDIEKMEgkklqlgiEEDLep 392
Cdd:cd02661 225 QISFPETLDLSPYMsQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDDSKVSPVS--------IETV-- 293
|
330 340
....*....|....*....|....*
gi 1039766797 393 sksqtrkpkcgkgthCSRNAYMLVY 417
Cdd:cd02661 294 ---------------LSQKAYILFY 303
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
957-1052 |
3.17e-40 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.
Pssm-ID: 340493 [Multi-domain] Cd Length: 99 Bit Score: 143.58 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 957 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1033
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
|
90
....*....|....*....
gi 1039766797 1034 DVMQVCMPEEGFKGTGLLG 1052
Cdd:cd01795 81 DVSRARVPEEGFKGTALLG 99
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
4.03e-39 |
|
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: 148.41 E-value: 4.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdytkgdgIHGGKDYEPQTICEHLQYLFALLQNSNRRYIDP-SGF 168
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS-------------LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPpDYF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 169 VKAL---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrnvVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNIqg 245
Cdd:cd02664 68 LEASrppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 246 hKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEP 325
Cdd:cd02664 134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 326 YVEHKGGSFV--------------------YELSAVLIHRGVSAYSGHYIAHVKDPQSGE-------------------- 365
Cdd:cd02664 213 RVESKSSESPlekkeeesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQTDADstgqecpepkdaeendeskn 292
|
....*.
gi 1039766797 366 WYKFND 371
Cdd:cd02664 293 WYLFND 298
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-379 |
8.62e-36 |
|
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: 138.23 E-value: 8.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcSDYTkgdGIHGGKDYEPQTICEHLQYLFALLQNSNRRyIDPSGFV 169
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-------KNYN---PARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 170 KALGL---------DTGQ--QQDAQE-FSKLFMSLledTLSKQKNPDVRNVVQQQFCGEYAYVTVC-NQCGRESKLVSKF 236
Cdd:cd02657 70 QLLRMafpqfaekqNQGGyaQQDAEEcWSQLLSVL---SQKLPGAGSKGSFIDQLFGIELETKMKCtESPDEEEVSTESE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 237 YELELNIqGHKQLTDCISEFLKEeRLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIG 316
Cdd:cd02657 147 YKLQCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039766797 317 FSESLDMEPYVEHKGgsfVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFND--------EDIEKMEG 379
Cdd:cd02657 225 FPFELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-417 |
3.74e-35 |
|
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: 136.29 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQVWFLNlelrqALYLCpstcsdytkgdgihggkdyepqticehLQYLFALLQNSNRRY--IDPSG 167
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFE-----NLLTC---------------------------LKDLFESISEQKKRTgvISPKK 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNVVQQQFCGEYAYVTVCNQCGR 228
Cdd:cd02663 49 FITRLKrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCET 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 229 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:cd02663 129 VSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 309 KKLNAYIGFSESL------DMEPYVEHKggsfvYELSAVLIHRGVSAYSGHYIAHVKdpQSGEWYKFNDEDIEKMEGKKl 382
Cdd:cd02663 209 IKLFYRVVFPLELrlfnttDDAENPDRL-----YELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENA- 280
|
330 340 350
....*....|....*....|....*....|....*
gi 1039766797 383 qlgIEEDLEPSKSQTrkpkcgkgthcsrNAYMLVY 417
Cdd:cd02663 281 ---VEEFFGDSPNQA-------------TAYVLFY 299
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
3.79e-35 |
|
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: 137.12 E-value: 3.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQVwFLNLELRQALYLcpstcSDytkGDGIHGGKDYEPQTICEHLQYLFA-LLQNSNRRyidPSGF 168
Cdd:cd02660 2 GLINLGATCFMNVILQA-LLHNPLLRNYFL-----SD---RHSCTCLSCSPNSCLSCAMDEIFQeFYYSGDRS---PYGP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 169 VKAL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNVVQQQFCGEYAYVTVCNQCGRESKL 232
Cdd:cd02660 70 INLLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 233 VSKFYELELNIQGHKQ---------------LTDCISEFLKEERLeGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLM 297
Cdd:cd02660 147 VDPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 298 RFVFDrQTGHKKKLNAYIGFSESLDMEPYV----------EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDpQSGEWY 367
Cdd:cd02660 226 RFEHS-LNKTSRKIDTYVQFPLELNMTPYTsssigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQWF 302
|
....
gi 1039766797 368 KFND 371
Cdd:cd02660 303 KFDD 306
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-400 |
3.17e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 125.78 E-value: 3.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 78 PNCERRKKN--SFVGLTNLGATCYVNTFLQVwflnlelrqaLYLCPSTCSDYTKGDGIHGGKdyepqticEHLQYLFALL 155
Cdd:cd02671 12 ATSCEKRENllPFVGLNNLGNTCYLNSVLQV----------LYFCPGFKHGLKHLVSLISSV--------EQLQSSFLLN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 156 Q---NSNRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNVVQQQFCGEYAYVTVCNQCG 227
Cdd:cd02671 74 PekyNDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLECE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 228 ----------------RESKLVSKFYELELNIQGH---KQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSL 288
Cdd:cd02671 142 tfterredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 289 PCTLNLQLMRF----VFDRQTGHKKKLNAYIGFSESLDMEPYVEhKGGSFVYELSAVLIHRGVSAYSGHYIAHVKdpqsg 364
Cdd:cd02671 222 PEVITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR----- 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039766797 365 eWYKFNDEDIEKMEgkklQLGIEEDLEPSKSQTRKP 400
Cdd:cd02671 296 -WLLFDDSEVKVTE----EKDFLEALSPNTSSTSTP 326
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-372 |
9.16e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 120.89 E-value: 9.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQVWFlNLELRQALYLC-----------PSTC--SDYTK-GDGIHGGKDYEPQTICEHlqylfall 155
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLF-SIPSFQWRYDDlenkfpsdvvdPANDlnCQLIKlADGLLSGRYSKPASLKSE-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 156 QNSNRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNVVQQQFCgeyayvtvCNQC 226
Cdd:cd02658 72 NDPYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CLSC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 227 GRESKLVSKFYELELNIQGHKQ--------------LTDCISEFLKEERLEgdnrYFCENCQSKQNATRKIRLLSLPCTL 292
Cdd:cd02658 144 KKVKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 293 NLQLMRFVFDrQTGHKKKLNAYIGFSESLDMEPYvehkggsfvyELSAVLIHRGVSAYSGHYIAHVK--DPQSGEWYKFN 370
Cdd:cd02658 220 VINMKRFQLL-ENWVPKKLDVPIDVPEELGPGKY----------ELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFN 288
|
..
gi 1039766797 371 DE 372
Cdd:cd02658 289 DE 290
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-374 |
2.04e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 115.95 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdytkgdgihggkdyepqticehlqyLFALLQNSNRRYIDpsgfv 169
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE---------------------------LFSQVCRKAPQFKG----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 170 kalgldtGQQQDAQEfskLFMSLLEDtlskqknpdVRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELEL----NIQG 245
Cdd:cd02667 49 -------YQQQDSHE---LLRYLLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 246 HKQLTDCISEFLKEERLEGDNRYFCENCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNAYIGFSESLDMEP 325
Cdd:cd02667 110 ECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039766797 326 Y------VEHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQSGEWYKFNDEDI 374
Cdd:cd02667 186 FcdpkcnSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDV 260
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
89-371 |
1.93e-19 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 90.41 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCpsTCSDYTKgdgihggkdyEPQTICEhLQYLFALLQNSNRRYIDPSGF 168
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSH--LATECLK----------EHCLLCE-LGFLFDMLEKAKGKNCQASNF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 169 VKALG----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNVVQQQFCGEYAYVTVCNQCGR 228
Cdd:pfam13423 68 LRALSsipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 229 ESKLVSKFYELELN------IQGHKQLTDCISEFLKE--ERlEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFV 300
Cdd:pfam13423 148 ESVRESSTHVLDLIyprkpsSNNKKPPNQTFSSILKSslER-ETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 301 FD-RQTGHKKKlnayiGFSESLDMEPYVEHKG--GSFVYELSAVLIHRGVSAYSGHYIAHVK-------DPQSGEWYKFN 370
Cdd:pfam13423 227 EEwRQLWKTPG-----WLPPEIGLTLSDDLQGdnEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFN 301
|
.
gi 1039766797 371 D 371
Cdd:pfam13423 302 D 302
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-417 |
2.78e-19 |
|
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: 88.19 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQvwflnlelrqALYLCPStcsdytkgdgihggkdyepqtICEHLQylfallqnsnrRYIdpsgfv 169
Cdd:cd02662 1 GLVNLGNTCFMNSVLQ----------ALASLPS---------------------LIEYLE-----------EFL------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 170 kalgldtgQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnvvqqqFCGEYAYVTVCNQCGRESKL-VSKFYELELNIQGHKQ 248
Cdd:cd02662 33 --------EQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSS 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 249 -----LTDCISEFLKEERLEGdnrYFCENCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNAYIGFSESLDm 323
Cdd:cd02662 93 gsgttLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 324 epyvehkggSFVYELSAVLIHRGvSAYSGHYIAH------VKDPQSGE--------------WYKFNDEDIEKMEgkklq 383
Cdd:cd02662 160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKEVS----- 224
|
330 340 350
....*....|....*....|....*....|....
gi 1039766797 384 lgiEEDLEPSKSqtrkpkcgkgthcsrnAYMLVY 417
Cdd:cd02662 225 ---ESEVLEQKS----------------AYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
90-377 |
1.15e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 87.55 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKgDGIhgGKDYEPQTICEHLqYLFALLQNSNRRYIDPSGfv 169
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLK-NVI--RKPEPDLNQEEAL-KLFTALWSSKEHKVGWIP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 170 kalglDTGQQQDAQEFsklfMSLLEDTLskqKNPDVRnvvqqqfCGEYAYVTVCNQCGRESK------LVSKFYELELNI 243
Cdd:COG5533 75 -----PMGSQEDAHEL----LGKLLDEL---KLDLVN-------SFTIRIFKTTKDKKKTSTgdwfdiIIELPDQTWVNN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 244 QghKQLTDCIS---EFLKEERL--EGDNRYfcENCQSKQNATRKIRllSLPCTLNLQLMRFVFDrqtGHKKKLNAYIGfs 318
Cdd:COG5533 136 L--KTLQEFIDnmeELVDDETGvkAKENEE--LEVQAKQEYEVSFV--KLPKILTIQLKRFANL---GGNQKIDTEVD-- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039766797 319 ESLDMEPYVEHKGG---SFVYELSAVLIHRGvSAYSGHYIAHVKdpQSGEWYKFNDEDIEKM 377
Cdd:COG5533 205 EKFELPVKHDQILNivkETYYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
249-376 |
4.05e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 89.94 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 249 LTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNAYIGFS-ESLDMEPYV 327
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVE 754
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1039766797 328 EHKGGS-FVYELSAVLIHRGVSAySGHYIAHVKDPQSGEWYKFNDEDIEK 376
Cdd:COG5560 755 YMVDDPrLIYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLFDDSRITE 803
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-375 |
2.20e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 78.69 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKgDGIH----GGKDYEP------QTICEHLQYLFALLQNS 158
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELAS-DYPTerriGGREVSRselqrsNQFVYELRSLFNDLIHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 159 NRRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNVVQQQFCGEY----AYVTVCN 224
Cdd:cd02666 81 NTRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTkqqlVPESMGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 225 QCGRESK-------LV-SKFYELELNIQGHKQ-LTDCISEFLKEERLEGDNRYFCENCQSKQNATRKI---------RLL 286
Cdd:cd02666 158 QPSVRTKterflslLVdVGKKGREIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 287 SLPCTLNLQLMRFVFDRQTGHKKKLNAYigfseSLDMEPYVEHKGgSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEW 366
Cdd:cd02666 238 DDIDELIREAIQSESSLVRQAQNELAEL-----KHEIEKQFDDLK-SYGYRLHAVFIHRG-EASSGHYWVYIKDFEENVW 310
|
....*....
gi 1039766797 367 YKFNDEDIE 375
Cdd:cd02666 311 RKYNDETVT 319
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
178-417 |
2.27e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 70.66 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 178 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVrnvvqQQFCGEYAYVTVCNqcGRESKLVSKFYELELNIQGHK 247
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMV-----QLFYGTFLTEGVLE--GKPFCNCETFGQYPLQVNGYG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 248 QLTDCISEFLKEERLEGDnryfcENCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNAYIGFSESLDMEPYv 327
Cdd:cd02665 94 NLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVPY- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 328 ehkggsfvyELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKlqlgIEEDlepsksqtrkpkcGKGTH 407
Cdd:cd02665 165 ---------ELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEE----VERD-------------SFGGG 217
|
250
....*....|
gi 1039766797 408 CSRNAYMLVY 417
Cdd:cd02665 218 RNPSAYCLMY 227
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
173-374 |
3.41e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 61.78 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 173 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNVVQQQFCGEYAYVT----VCNQCGRESKLVSKFYELELNIQG 245
Cdd:cd02673 27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 246 HK--QLTDCISEFLKEERLEGDnryfCENCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIgfsesldM 323
Cdd:cd02673 107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039766797 324 EPYvEHKGGSfvYELSAVLIHRGVSAYSGHYIAHVKDPQSG-EWYKFNDEDI 374
Cdd:cd02673 175 KKY-CGTDAK--YSLVAVICHLGESPYDGHYIAYTKELYNGsSWLYCSDDEI 223
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
483-553 |
9.05e-10 |
|
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: 56.22 E-value: 9.05e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766797 483 EPYEFVSLEWLQKWL----DESTPTKPIDNN--ACLCSHDKLHPDKISIMK--RISEYAANIFYSRYGGGPRLTVKALC 553
Cdd:pfam06337 2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-378 |
2.22e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 54.63 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 86 NSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdytkgdgihgGKDYEPQ-TICEHLQYLFALLQ----NSN- 159
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL----------------YENYENIkDRKSELVKRLSELIrkiwNPRn 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 160 -RRYIDPSGFVKALGLDTGQ--QQDAQEFSKLFMSLLEDTLSKQ---KNPDVRNVVQQQFCGE-----YAYVTVCNQCGR 228
Cdd:cd02669 181 fKGHVSPHELLQAVSKVSKKkfSITEQSDPVEFLSWLLNTLHKDlggSKKPNSSIIHDCFQGKvqietQKIKPHAEEEGS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 229 ESKL----------VSKFYELELNIQG-----HKQLTDCISEFLKEERLegdNRYFCENCQSKQNATRKIRLLSLPCTLN 293
Cdd:cd02669 261 KDKFfkdsrvkktsVSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYLI 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 294 LQLMRFvfDRQTGHKKKLNAYIGFS-ESLDMEPYVE---HKGGSFV-YELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYK 368
Cdd:cd02669 338 FHIKRF--SKNNFFKEKNPTIVNFPiKNLDLSDYVHfdkPSLNLSTkYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFE 415
|
330
....*....|
gi 1039766797 369 FNDEDIEKME 378
Cdd:cd02669 416 IQDLNVKEVL 425
|
|
| Ubl_ubiquitin_like |
cd17039 |
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
967-1020 |
1.29e-06 |
|
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: 46.82 E-value: 1.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1039766797 967 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1020
Cdd:cd17039 15 VDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK-TLSDYGIKDGSTIHL 67
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
482-555 |
9.84e-06 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 45.04 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 482 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNNACLCSHD--KLHPDKI--SIMKRISEYAANIFYSRYGGGPR-LTVKA 551
Cdd:smart00695 5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84
|
....
gi 1039766797 552 LCKD 555
Cdd:smart00695 85 VCQG 88
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
962-1020 |
1.14e-05 |
|
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: 44.17 E-value: 1.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766797 962 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1020
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
75-371 |
6.84e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 45.97 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 75 IDDPNCERRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdytkgdgIHGGKDYEPQTICEhLQYLF-A 153
Cdd:cd02672 2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAI-------------ILVACPKESCLLCE-LGYLFsT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 154 LLQNSNRRYIDPSGFvKALGLDTGQQQDAQEFSKLF-MSLLEDTLSKQKNPDVRNVVQQQFCGEYAyvtvcNQCGRESKL 232
Cdd:cd02672 68 LIQNFTRFLLETISQ-DQLGTPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKV-----TKAWCDTCC 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766797 233 VSKFYELELNIQGhkqLTDCiseflkeerlegDNRYFCENCqSKQNATRKIRLLSLPCTLNLQlmrfvfdrqtghkkklN 312
Cdd:cd02672 142 KYQPLEQTTSIRH---LPDI------------LLLVLVINL-SVTNGEFDDINVVLPSGKVMQ----------------N 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039766797 313 AYIGFSESLDMEPYVEHKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQ----SGEWYKFND 371
Cdd:cd02672 190 KVSPKAIDHDKLVKNRGQESIYKYELVGYVCEINDSSRGQHNVVFVIKVNeestHGRWYLFND 252
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
967-1020 |
1.22e-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: 38.31 E-value: 1.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1039766797 967 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDcATLGTLGVIPESVILL 1020
Cdd:pfam00240 15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDD-QTLGEYGIEDGSTIHL 67
|
|
| Ubl_AtNPL4_like |
cd17055 |
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ... |
955-1012 |
6.03e-03 |
|
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins; The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2.
Pssm-ID: 340575 Cd Length: 73 Bit Score: 36.42 E-value: 6.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039766797 955 RHRKvrGEKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGK---ILNDDCATLGTLGV 1012
Cdd:cd17055 6 RSRD--GTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLSLDPGpdlLTAKSSATLSQLGL 64
|
|
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