|
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: 573.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMlgDGIQEEKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAEL--KNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQGHKQL 249
Cdd:cd02668 79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 250 TDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEPY-VE 328
Cdd:cd02668 159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 329 HKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDlepsKSQTRKPKCGKGTHC 408
Cdd:cd02668 239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSED----PAKPRKSEIKKGTHS 314
|
330
....*....|
gi 1174098913 409 SRNAYMLVYR 418
Cdd:cd02668 315 SRTAYMLVYK 324
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-417 |
4.12e-61 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 211.15 E-value: 4.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMLGDGIQeekdyepqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------LLCALRDLFkALQKNSKSSSVSPKM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYE 238
Cdd:pfam00443 72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 239 LELNIQGHK------QLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 313 TYIGFSEILDMEPYV-----EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKmegkklqlgIE 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTE---------VD 295
|
330 340 350
....*....|....*....|....*....|
gi 1174098913 388 EDLEPSksqtrkpkcgkgthcSRNAYMLVY 417
Cdd:pfam00443 296 EETAVL---------------SSSAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-457 |
2.43e-46 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 181.22 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 72 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYlcpstcsdymlgdGIQEEKDYEPQTICEHLQYL 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-------------GIPTDHPRGRDSVALALQRL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077 244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 309 KKLNTYIGFSEILDMEPYVEH-----KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMegkklq 383
Cdd:COG5077 399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVTRA------ 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 384 lGIEEDLEPSKSQTR--KPKCGKGTHCSR--NAYMLVYRLQTQE----KPNTTVQVPAFLQELVDRDNSKFEEWCIEMAE 455
Cdd:COG5077 472 -TEKEVLEENFGGDHpyKDKIRDHSGIKRfmSAYMLVYLRKSMLddllNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDE 550
|
..
gi 1174098913 456 MR 457
Cdd:COG5077 551 IH 552
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
938-1033 |
2.07e-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: 143.96 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 938 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1014
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
|
90
....*....|....*....
gi 1174098913 1015 DVMQVCMPEEGFKGTGLLG 1033
Cdd:cd01795 81 DVSRARVPEEGFKGTALLG 99
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
483-553 |
1.35e-09 |
|
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: 55.45 E-value: 1.35e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098913 483 EPYEFVSLEWLQKWL----DESTPTKPIDNH--ACLCSHDKLHPDKISIMK--RISEYAADIFYSRYGGGPRLTVKALC 553
Cdd:pfam06337 2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
482-555 |
9.19e-06 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 45.04 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 482 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNHACLCSHD--KLHPDKI--SIMKRISEYAADIFYSRYGGGPR-LTVKA 551
Cdd:smart00695 5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84
|
....
gi 1174098913 552 LCKE 555
Cdd:smart00695 85 VCQG 88
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
943-1001 |
3.08e-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: 43.02 E-value: 3.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098913 943 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCaTLGTLGVIPESVILL 1001
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
933-1001 |
9.20e-04 |
|
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: 38.69 E-value: 9.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098913 933 RSMRHRKVrgekALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDcATLGTLGVIPESVILL 1001
Cdd:pfam00240 4 KTLDGKKI----TLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDD-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: 573.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMlgDGIQEEKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAEL--KNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQGHKQL 249
Cdd:cd02668 79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 250 TDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEPY-VE 328
Cdd:cd02668 159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 329 HKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDlepsKSQTRKPKCGKGTHC 408
Cdd:cd02668 239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSED----PAKPRKSEIKKGTHS 314
|
330
....*....|
gi 1174098913 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 |
7.34e-81 |
|
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: 266.43 E-value: 7.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 88 FVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdymlgdgiqEEKDYEPQTICeHLQYLFALLQNSNRRYIDPSG 167
Cdd:cd02659 2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-----------EDDDDNKSVPL-ALQRLFLFLQLSESPVKTTEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELN 242
Cdd:cd02659 70 TDKTRSfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 243 IQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILD 322
Cdd:cd02659 147 VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 323 MEPYVEH------------KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKM---EGKKLQLGIE 387
Cdd:cd02659 227 MEPYTEKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGE 305
|
330 340 350
....*....|....*....|....*....|.
gi 1174098913 388 EDLEPSKSQTRKpkcGKGTHcsrNAYMLVYR 418
Cdd:cd02659 306 ETQKTYDSGPRA---FKRTT---NAYMLFYE 330
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-417 |
4.12e-61 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 211.15 E-value: 4.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMLGDGIQeekdyepqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------LLCALRDLFkALQKNSKSSSVSPKM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYE 238
Cdd:pfam00443 72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 239 LELNIQGHK------QLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 313 TYIGFSEILDMEPYV-----EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKmegkklqlgIE 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTE---------VD 295
|
330 340 350
....*....|....*....|....*....|
gi 1174098913 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 |
2.02e-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: 201.56 E-value: 2.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNtflqvwflnlelrqalylcpSTcsdymlgdgiqeekdyepqticehLQYLFAllqnsnrryidpsgfv 169
Cdd:cd02257 1 GLNNLGNTCYLN--------------------SV------------------------LQALFS---------------- 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 170 kalgldtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQ 244
Cdd:cd02257 21 --------EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 245 GHKQ----LTDCISEFLKEEKLEGDNRYFCEnCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSEI 320
Cdd:cd02257 93 VKGLpqvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 321 LDMEPYVEHKG-------GSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgiEEDLEps 393
Cdd:cd02257 171 LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVL-- 240
|
330 340
....*....|....*....|....*
gi 1174098913 394 ksqtrkpkcgKGTHCSRNAYMLVYR 418
Cdd:cd02257 241 ----------EFGSLSSSAYILFYE 255
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-457 |
2.43e-46 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 181.22 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 72 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYlcpstcsdymlgdGIQEEKDYEPQTICEHLQYL 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-------------GIPTDHPRGRDSVALALQRL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077 244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 309 KKLNTYIGFSEILDMEPYVEH-----KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMegkklq 383
Cdd:COG5077 399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVTRA------ 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 384 lGIEEDLEPSKSQTR--KPKCGKGTHCSR--NAYMLVYRLQTQE----KPNTTVQVPAFLQELVDRDNSKFEEWCIEMAE 455
Cdd:COG5077 472 -TEKEVLEENFGGDHpyKDKIRDHSGIKRfmSAYMLVYLRKSMLddllNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDE 550
|
..
gi 1174098913 456 MR 457
Cdd:COG5077 551 IH 552
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-417 |
3.57e-44 |
|
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: 162.45 E-value: 3.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQVwflnleLRQALYLcpstcSDYMLGDGIQEEKDYE-PQTICEHLQYLFALLQNSnRRYIDPSGF 168
Cdd:cd02661 3 GLQNLGNTCFLNSVLQC------LTHTPPL-----ANYLLSREHSKDCCNEgFCMMCALEAHVERALASS-GPGSAPRIF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 169 VKAL-----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NIVQQQFCGEYAYVTVCNQCGRESKLLSK 235
Cdd:cd02661 71 SSNLkqiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKHVSNTYDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 236 FYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHkkKLNTYI 315
Cdd:cd02661 151 FLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 316 GFSEILDMEPYV-EHKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPqSGEWYKFNDEDIEKMEgkklqlgiEEDLepsk 394
Cdd:cd02661 227 SFPETLDLSPYMsQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDDSKVSPVS--------IETV---- 293
|
330 340
....*....|....*....|...
gi 1174098913 395 sqtrkpkcgkgthCSRNAYMLVY 417
Cdd:cd02661 294 -------------LSQKAYILFY 303
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
178-418 |
8.81e-44 |
|
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: 158.60 E-value: 8.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 178 QQQDAQEFsklfMSLLEDTLskqknpdvRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNI-----QGHKQ-LTD 251
Cdd:cd02674 21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 252 CISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFS-EILDMEPYV--E 328
Cdd:cd02674 89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPlNDLDLTPYVdtR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 329 HKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgieedlepsksqtrkpkcgKGTHC 408
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS-------------------------ESSVV 220
|
250
....*....|
gi 1174098913 409 SRNAYMLVYR 418
Cdd:cd02674 221 SSSAYILFYE 230
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
938-1033 |
2.07e-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: 143.96 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 938 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1014
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
|
90
....*....|....*....
gi 1174098913 1015 DVMQVCMPEEGFKGTGLLG 1033
Cdd:cd01795 81 DVSRARVPEEGFKGTALLG 99
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
8.52e-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: 147.64 E-value: 8.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcsdymLGDGIQEEKDyePQTICEHLQYLFALLQNSNRRYIDP-SGF 168
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQV-----------LSLNLPRLGD--SQSVMKKLQLLQAHLMHTQRRAEAPpDYF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 169 VKAL---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrniVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIqg 245
Cdd:cd02664 68 LEASrppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 246 hKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEP 325
Cdd:cd02664 134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 326 YVEHKGGSYV--------------------YELSAVLIHRGVSAYSGHYIAHVKDPQSGE-------------------- 365
Cdd:cd02664 213 RVESKSSESPlekkeeesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQTDADstgqecpepkdaeendeskn 292
|
....*.
gi 1174098913 366 WYKFND 371
Cdd:cd02664 293 WYLFND 298
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
2.84e-37 |
|
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: 143.28 E-value: 2.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQVWFLNLELRqalylcpstcsDYMLGDGIQEEKDY--EPQTICEHLQYLFA-LLQNSNRRyidPS 166
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLR-----------NYFLSDRHSCTCLScsPNSCLSCAMDEIFQeFYYSGDRS---PY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 167 GFVKAL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRES 230
Cdd:cd02660 68 GPINLLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 231 KLLSKFYELELNIQGHKQ---------------LTDCISEFLKEEKLeGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQ 295
Cdd:cd02660 145 TTVDPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 296 LMRFVFDrQTGHKKKLNTYIGFSEILDMEPYV----------EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDpQSGE 365
Cdd:cd02660 224 LKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTsssigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQ 300
|
....*.
gi 1174098913 366 WYKFND 371
Cdd:cd02660 301 WFKFDD 306
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-417 |
4.60e-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: 135.90 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQVWFLNlelrqALYLCpstcsdymlgdgiqeekdyepqticehLQYLFALLQNSNRRY--IDPSG 167
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFE-----NLLTC---------------------------LKDLFESISEQKKRTgvISPKK 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:cd02663 49 FITRLKrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCET 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:cd02663 129 VSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 309 KKLNTYIGFSEIL------DMEPYVEHKggsyvYELSAVLIHRGVSAYSGHYIAHVKdpQSGEWYKFNDEDIEKMEGKKl 382
Cdd:cd02663 209 IKLFYRVVFPLELrlfnttDDAENPDRL-----YELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENA- 280
|
330 340 350
....*....|....*....|....*....|....*
gi 1174098913 383 qlgIEEDLEPSKSQTrkpkcgkgthcsrNAYMLVY 417
Cdd:cd02663 281 ---VEEFFGDSPNQA-------------TAYVLFY 299
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-379 |
7.33e-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 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: 135.54 E-value: 7.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcSDYMlgdGIQEEKDYEPQTICEHLQYLFALLQNSNRRyIDPSGFV 169
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-------KNYN---PARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 170 KALGL---------DTGQ--QQDAQE-FSKLFMSLLEDTLSKQKNPDVrniVQQQFCGEYAYVTVC-NQCGRESKLLSKF 236
Cdd:cd02657 70 QLLRMafpqfaekqNQGGyaQQDAEEcWSQLLSVLSQKLPGAGSKGSF---IDQLFGIELETKMKCtESPDEEEVSTESE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 237 YELELNIqGHKQLTDCISEFLKEeKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIG 316
Cdd:cd02657 147 YKLQCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1174098913 317 FSEILDMEPYVEHKGgsyVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFND--------EDIEKMEG 379
Cdd:cd02657 225 FPFELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-400 |
3.31e-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: 125.39 E-value: 3.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 78 PNCERRKK-NSFVGLTNLGATCYVNTFLQVwflnlelrqaLYLCPSTCSD--YMLGDGIQEEkdyEPQTICEHLQYLFal 154
Cdd:cd02671 13 TSCEKRENlLPFVGLNNLGNTCYLNSVLQV----------LYFCPGFKHGlkHLVSLISSVE---QLQSSFLLNPEKY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 155 lqNSNRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNIVQQQFCGEYAYVTVCNQCG-- 227
Cdd:cd02671 78 --NDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLECEtf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 228 --------------RESKLLSKFYELELNIQGH---KQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPC 290
Cdd:cd02671 144 terredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 291 TLNLQLMRF----VFDRQTGHKKKLNTYIGFSEILDMEPYVEhKGGSYVYELSAVLIHRGVSAYSGHYIAHVKdpqsgeW 366
Cdd:cd02671 224 VITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR------W 296
|
330 340 350
....*....|....*....|....*....|....
gi 1174098913 367 YKFNDEDIEKMEgkklQLGIEEDLEPSKSQTRKP 400
Cdd:cd02671 297 LLFDDSEVKVTE----EKDFLEALSPNTSSTSTP 326
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-372 |
4.40e-29 |
|
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: 118.58 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQVWF-------LNLELRQALYLCPS------TCSDYMLGDGIQEEKDYEPQTICEHlqylfallQ 156
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwRYDDLENKFPSDVVdpandlNCQLIKLADGLLSGRYSKPASLKSE--------N 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 157 NSNRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNIVQQQFCgeyayvtvCNQCG 227
Cdd:cd02658 73 DPYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CLSCK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 228 RESKLLSKFYELELNIQGHKQ--------------LTDCISEFLKEEKLEgdnrYFCENCQSKQNATRKIRLLSLPCTLN 293
Cdd:cd02658 145 KVKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 294 LQLMRFVFDrQTGHKKKLNTYIGFSEILDMEPYvehkggsyvyELSAVLIHRGVSAYSGHYIAHVK--DPQSGEWYKFND 371
Cdd:cd02658 221 INMKRFQLL-ENWVPKKLDVPIDVPEELGPGKY----------ELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFND 289
|
.
gi 1174098913 372 E 372
Cdd:cd02658 290 E 290
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-374 |
1.45e-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: 116.33 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTflqvwflnleLRQALYLCPstcsdyMLGDGIQEEkdyePQTicehlqyLFALLQNSNRRYIDpsgfv 169
Cdd:cd02667 1 GLSNLGNTCFFNA----------VMQNLSQTP------ALRELLSET----PKE-------LFSQVCRKAPQFKG----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 170 kalgldtGQQQDAQEfskLFMSLLEDtlskqknpdVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELEL----NIQG 245
Cdd:cd02667 49 -------YQQQDSHE---LLRYLLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 246 HKQLTDCISEFLKEEKLEGDNRYFCENCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNTYIGFSEILDMEP 325
Cdd:cd02667 110 ECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174098913 326 Y------VEHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQSGEWYKFNDEDI 374
Cdd:cd02667 186 FcdpkcnSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDV 260
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-417 |
8.77e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 89.73 E-value: 8.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQvwflnlelrqALYLCPStcsdymlgdgiqeekdyepqtICEHLQylfallqnsnrRYIdpsgfv 169
Cdd:cd02662 1 GLVNLGNTCFMNSVLQ----------ALASLPS---------------------LIEYLE-----------EFL------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 170 kalgldtgQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnivqqqFCGEYAYVTVCNQCGRESKL-LSKFYELELNIQGHKQ 248
Cdd:cd02662 33 --------EQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSS 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 249 -----LTDCISEFLKEEKLEGdnrYFCENCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSEILDm 323
Cdd:cd02662 93 gsgttLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 324 epyvehkggSYVYELSAVLIHRGvSAYSGHYIAH------VKDPQSGE--------------WYKFNDEDIEKMEgkklq 383
Cdd:cd02662 160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKEVS----- 224
|
330 340 350
....*....|....*....|....*....|....
gi 1174098913 384 lgiEEDLEPSKSqtrkpkcgkgthcsrnAYMLVY 417
Cdd:cd02662 225 ---ESEVLEQKS----------------AYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
90-377 |
9.97e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 90.63 E-value: 9.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMlgdgIQE-EKDYEPQTICEHLqYLFALLQNSNRRYIDPSGf 168
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVL----KNViRKPEPDLNQEEAL-KLFTALWSSKEHKVGWIP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 169 vkalglDTGQQQDAQEFSKLFMSLLEDTLSKQ--------KNPDVRNIVQQQFcgeyaYVTVCNQCGRESKLLSKFyele 240
Cdd:COG5533 75 ------PMGSQEDAHELLGKLLDELKLDLVNSftirifktTKDKKKTSTGDWF-----DIIIELPDQTWVNNLKTL---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 241 lniqghKQLTDCISEFLKEEKL--EGDNRYfcENCQSKQNATRKIRllSLPCTLNLQLMRFVFDrqtGHKKKLNTYIGfs 318
Cdd:COG5533 140 ------QEFIDNMEELVDDETGvkAKENEE--LEVQAKQEYEVSFV--KLPKILTIQLKRFANL---GGNQKIDTEVD-- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1174098913 319 EILDMEPYVEHKGG---SYVYELSAVLIHRGvSAYSGHYIAHVKdpQSGEWYKFNDEDIEKM 377
Cdd:COG5533 205 EKFELPVKHDQILNivkETYYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
89-371 |
1.27e-18 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 87.71 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCpstcsdymlgdgIQEEKDYEPQTICEhLQYLFALLQNSNRRYIDPSGF 168
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSH------------LATECLKEHCLLCE-LGFLFDMLEKAKGKNCQASNF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 169 VKALG----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:pfam13423 68 LRALSsipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 229 ESKLLSKFYELELN------IQGHKQLTDCISEFLKEE-KLEGDNRYFCENCQSKQNATRKIRLLSLPC--TLNLQLMRF 299
Cdd:pfam13423 148 ESVRESSTHVLDLIyprkpsSNNKKPPNQTFSSILKSSlERETTTKAWCEKCKRYQPLESRRTVRNLPPvlSLNAALTNE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098913 300 VFDRQTGHKKKLNTYIGfseiLDMEPYVEHKGGSYVYELSAVLIHRGVSAYSGHYIAHVK-------DPQSGEWYKFND 371
Cdd:pfam13423 228 EWRQLWKTPGWLPPEIG----LTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
220-376 |
7.47e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 89.17 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 220 VTVCNQCGRESKLLSKFYE-----LELNIQGHKQ---LTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCT 291
Cdd:COG5560 640 DAVVISCEWEEKRYLSLFSydplwTIREIGAAERtitLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 292 LNLQLMRFVFDRQTghKKKLNTYIGFS-EILDMEPYVEHKGGSYV-YELSAVLIHRGVSAySGHYIAHVKDPQSGEWYKF 369
Cdd:COG5560 720 LIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVEYMVDDPRLiYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLF 796
|
....*..
gi 1174098913 370 NDEDIEK 376
Cdd:COG5560 797 DDSRITE 803
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-375 |
7.36e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 80.23 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 89 VGLTNLGATCYVNTFLQVWFLNLELRQA--------LYLCPSTCSDYMLGDGIQEEKDYE-PQTICEHLQYLFALLQNSN 159
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnfdeskAELASDYPTERRIGGREVSRSELQrSNQFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 160 RRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNIVQQQFCGEY----AYVTVCNQ 225
Cdd:cd02666 82 TRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTkqqlVPESMGNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 226 CGRESK---LLSKFYEL-----ELNIQGHKQ-LTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKI---------RLLS 287
Cdd:cd02666 159 PSVRTKterFLSLLVDVgkkgrEIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 288 LPCTLNLQLMRFVFDRQTGHKKKLNTYIGfseilDMEPYVEHKGgSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWY 367
Cdd:cd02666 239 DIDELIREAIQSESSLVRQAQNELAELKH-----EIEKQFDDLK-SYGYRLHAVFIHRG-EASSGHYWVYIKDFEENVWR 311
|
....*...
gi 1174098913 368 KFNDEDIE 375
Cdd:cd02666 312 KYNDETVT 319
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
178-417 |
4.96e-14 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 72.59 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 178 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVrnivqQQFCGEYAYVTVcnqcgRESKLLSK---FYELELNIQ 244
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMV-----QLFYGTFLTEGV-----LEGKPFCNcetFGQYPLQVN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 245 GHKQLTDCISEFLKEEKLEGDnryfcENCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFSEILDME 324
Cdd:cd02665 91 GYGNLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 325 PYvehkggsyvyELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKlqlgIEEDlepsksqtrkpkcGK 404
Cdd:cd02665 163 PY----------ELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEE----VERD-------------SF 214
|
250
....*....|...
gi 1174098913 405 GTHCSRNAYMLVY 417
Cdd:cd02665 215 GGGRNPSAYCLMY 227
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-378 |
6.36e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 65.80 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 86 NSFVGLTNLGATCYVNTFLQvwflnlelrqALYLCPSTCSDYMLGDGIQEEKDYEPQTIcEHLQYLFALLQNSN--RRYI 163
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQ----------ALSHVKPIRNFFLLYENYENIKDRKSELV-KRLSELIRKIWNPRnfKGHV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 164 DPSGFVKALGLDTGQ--QQDAQEFSKLFMSLLEDTLSKQ---KNPDVRNIVQQQFCGEY-----AYVTVCNQCGRESKLL 233
Cdd:cd02669 186 SPHELLQAVSKVSKKkfSITEQSDPVEFLSWLLNTLHKDlggSKKPNSSIIHDCFQGKVqietqKIKPHAEEEGSKDKFF 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 234 ----------SKFYELELNIQG-----HKQLTDCISEFLKEEKLegdNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMR 298
Cdd:cd02669 266 kdsrvkktsvSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYLIFHIKR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 299 FvfDRQTGHKKKLNTYIGFS-EILDMEPYVE---HKGGSYV-YELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDED 373
Cdd:cd02669 343 F--SKNNFFKEKNPTIVNFPiKNLDLSDYVHfdkPSLNLSTkYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLN 420
|
....*
gi 1174098913 374 IEKME 378
Cdd:cd02669 421 VKEVL 425
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
173-374 |
3.40e-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: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 173 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNIVQQQFCGEYAYVT----VCNQCGRESKLLSKFYELELNIQG 245
Cdd:cd02673 27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 246 HK--QLTDCISEFLKEEKLEGDnryfCENCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIgfseildM 323
Cdd:cd02673 107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1174098913 324 EPYvEHKGGSYvyELSAVLIHRGVSAYSGHYIAHVKDPQSG-EWYKFNDEDI 374
Cdd:cd02673 175 KKY-CGTDAKY--SLVAVICHLGESPYDGHYIAYTKELYNGsSWLYCSDDEI 223
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
483-553 |
1.35e-09 |
|
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: 55.45 E-value: 1.35e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098913 483 EPYEFVSLEWLQKWL----DESTPTKPIDNH--ACLCSHDKLHPDKISIMK--RISEYAADIFYSRYGGGPRLTVKALC 553
Cdd:pfam06337 2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
75-371 |
1.96e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 50.59 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 75 IDDPNCERRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdymlgdgIQEEKDYEPQTICEhLQYLFAL 154
Cdd:cd02672 2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAI-------------ILVACPKESCLLCE-LGYLFST 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 155 LqnsnrryidpsgfvkalgldtgqqqdAQEFSKLFmslLEDTLSKQKNPDvrnivqqqfcgeyayvtvcNQCGRESKLLS 234
Cdd:cd02672 68 L--------------------------IQNFTRFL---LETISQDQLGTP-------------------FSCGTSRNSVS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 235 KFYELELNIQGHKQLTD-----CISEFLKEEKlegDNRYFCENCQSKQNATRKIRLLSLPCTLNLQL---MRFV------ 300
Cdd:cd02672 100 LLYTLSLPLGSTKTSKEstflqLLKRSLDLEK---VTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLvinLSVTngefdd 176
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174098913 301 FDRQTGHKKKLNTYIGFSEILDMEPYVEHKG-GSYVYELSAVLIHRGVSAYSGHYIAHVKDPQS----GEWYKFND 371
Cdd:cd02672 177 INVVLPSGKVMQNKVSPKAIDHDKLVKNRGQeSIYKYELVGYVCEINDSSRGQHNVVFVIKVNEesthGRWYLFND 252
|
|
| Ubl_ubiquitin_like |
cd17039 |
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
948-1001 |
3.76e-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: 45.28 E-value: 3.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1174098913 948 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCaTLGTLGVIPESVILL 1001
Cdd:cd17039 15 VDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK-TLSDYGIKDGSTIHL 67
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
482-555 |
9.19e-06 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 45.04 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 482 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNHACLCSHD--KLHPDKI--SIMKRISEYAADIFYSRYGGGPR-LTVKA 551
Cdd:smart00695 5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84
|
....
gi 1174098913 552 LCKE 555
Cdd:smart00695 85 VCQG 88
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
943-1001 |
3.08e-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: 43.02 E-value: 3.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098913 943 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCaTLGTLGVIPESVILL 1001
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
90-243 |
5.13e-05 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 47.19 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 90 GLTNLGATCYVNTFLQVWFLNLELRqalylcpstcsDYMLGDGIQEEKDYE-PQTICEHLQYLFA-LLQ---NSNRRYID 164
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELR-----------DYFLSDEYEESINEEnPLGMHGSVASAYAdLIKqlyDGNLHAFT 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098913 165 PSGFVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSK--QK----NPDV-----------------------RNIVQ 210
Cdd:COG5560 336 PSGFKKTIGsfneeFSGYDQQDSQEFIAFLLDGLHEDLNRiiKKpytsKPDLspgddvvvkkkakecwwehlkrnDSIIT 415
|
170 180 190
....*....|....*....|....*....|...
gi 1174098913 211 QQFCGEYAYVTVCNQCGRESKLLSKFYELELNI 243
Cdd:COG5560 416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
933-1001 |
9.20e-04 |
|
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: 38.69 E-value: 9.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098913 933 RSMRHRKVrgekALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDcATLGTLGVIPESVILL 1001
Cdd:pfam00240 4 KTLDGKKI----TLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDD-QTLGEYGIEDGSTIHL 67
|
|
| Ubl_AtNPL4_like |
cd17055 |
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ... |
930-993 |
3.48e-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: 37.19 E-value: 3.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1174098913 930 VIRrsMRHRKvrGEKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGK---ILSDDCATLGTLGV 993
Cdd:cd17055 2 LLR--VRSRD--GTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLSLDPGpdlLTAKSSATLSQLGL 64
|
|
| |
