|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-398 |
1.07e-116 |
|
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: 361.35 E-value: 1.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNTTFRNGVFS------AEMELVRND------PVLHQLARLFAQLHSGTKSSVDSAAFATT 148
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstedAELKNMPPDkphepqTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 149 LELDNAVQQDGQEFLKLLLTLLERVLAQSRVPEARDVVQNLFRGTFSYVTKCSSCGKESGASDqfvDFYELEVNVKGFSS 228
Cdd:cd02668 81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPS---KFYELELQLKGHKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 229 LEESLDDYLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLKTSTKKKVTSKFMFPKVLDMERRVs 308
Cdd:cd02668 158 LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 309 pvtsDGSPGEPAHYDLFAILMHKGNMASSGHYVVHIRDERTGQWWQFDDEEVTMLGSNPLGEPTSKlDKVSPDRDD---N 385
Cdd:cd02668 237 ----AESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSE-DPAKPRKSEikkG 311
|
330
....*....|...
gi 300172100 386 LLMSPDAYMLMFS 398
Cdd:cd02668 312 THSSRTAYMLVYK 324
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
80-397 |
1.27e-60 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 209.61 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 80 AGLTNLGATCYVNSVLQCLFMNTTFRNGVFSAEMELVRNDP-----VLHQLARLFAQLHSGTKSS-VDSAAFATTLELDN 153
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYnkdinLLCALRDLFKALQKNSKSSsVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 154 AV-----QQDGQEFLKLLLTLLERVLAQSRVPEARDVVQNLFRGTFSYVTKCSSCGKESGASDQFVDF---YELEVNVKG 225
Cdd:pfam00443 81 PDfsgykQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpIPGDSAELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 226 FSSLEESLDDYLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLktSTKKKVTSKFMFPKVLDMER 305
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNR--STWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 306 RVSPvTSDGSPGEPAHYDLFAILMHKGNmASSGHYVVHIRDERTGQWWQFDDEEVTmlgsnplgeptskldKVSPDRDdn 385
Cdd:pfam00443 239 YLAE-ELKPKTNNLQDYRLVAVVVHSGS-LSSGHYIAYIKAYENNRWYKFDDEKVT---------------EVDEETA-- 299
|
330
....*....|..
gi 300172100 386 lLMSPDAYMLMF 397
Cdd:pfam00443 300 -VLSSSAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
81-425 |
4.37e-49 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 189.70 E-value: 4.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNTTFRNGVFSAEMELVR-NDPVLHQLARLFAQLHSGtKSSVDSAAFATTLELDNAV---Q 156
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRgRDSVALALQRLFYNLQTG-EEPVDTTELTRSFGWDSDDsfmQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 157 QDGQEFLKLLLTLLERVLAQSRVpeaRDVVQNLFRGTFSYVTKCSSCGKESGASDqfvDFYELEVNVKGFSSLEESLDDY 236
Cdd:COG5077 274 HDIQEFNRVLQDNLEKSMRGTVV---ENALNGIFVGKMKSYIKCVNVNYESARVE---DFWDIQLNVKGMKNLQESFRRY 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 237 LNEEKLSGENQYFCEYcKARVDATHSTKLRLLPPVLNFQLKRFVFNLKTSTKKKVTSKFMFPKVLDMERRVSPvTSDGSP 316
Cdd:COG5077 348 IQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDR-DADKSE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 317 GEPAHYDLFAILMHKGNMaSSGHYVVHIRDERTGQWWQFDDEEVT------MLGSNPLGEPTSKlDKVSPDRDDNLLMSp 390
Cdd:COG5077 426 NSDAVYVLYGVLVHSGDL-HEGHYYALLKPEKDGRWYKFDDTRVTratekeVLEENFGGDHPYK-DKIRDHSGIKRFMS- 502
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 300172100 391 dAYMLMFSRRTS-----TPRVAEEpvrsIPEFLKAEVDEQ 425
Cdd:COG5077 503 -AYMLVYLRKSMlddllNPVAAVD----IPPHVEEVLSEE 537
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
889-996 |
1.55e-27 |
|
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: 107.37 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 889 RRTVATgnkQVKLTVSGTTTVYQLKMLIWEWLGVVKENQEVHFGKVELTDESTTLADVGVLPNSQLWVSDSGLHEHRDIA 968
Cdd:cd01795 1 RRVRGE---RKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDA 77
|
90 100
....*....|....*....|....*...
gi 300172100 969 GkpmlslFIYVSLIASLWFSQTSSRLHS 996
Cdd:cd01795 78 D------EADVSRARVPEEGFKGTALLG 99
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
467-531 |
6.20e-11 |
|
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: 59.30 E-value: 6.20e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300172100 467 KGFWISAEWLRNWTDSLKP----PSAIDNSILLCEHERVSPKSIQLMK----CISDAAWQSLHSKYGGQPVVT 531
Cdd:pfam06337 3 KVYLISSKWLNKWKSYVKEpnnePGPIDNSDLLDDESNGQLKPNLQEGvdyvIVPEEVWEFLVEWYGGGPEIK 75
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
469-528 |
1.17e-06 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 47.35 E-value: 1.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300172100 469 FWISAEWLRNWTDSL-----KPPSAIDNSILLCEHERVSPKSI----QLMKCISDAAWQSLHSKYGGQP 528
Cdd:smart00695 9 YLISTRWYRQWADFVegkdgKDPGPIDNSGILCSHGGPRLKEHlvegEDYVLIPEELWNKLVRWYGGGP 77
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
895-954 |
1.44e-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: 41.00 E-value: 1.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 895 GNKQVKLTVSGTTTVYQLKMLIWEWLGVVKENQEVHFGKVELTDEStTLADVGVLPNSQL 954
Cdd:pfam00240 7 DGKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQ-TLGEYGIEDGSTI 65
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
895-956 |
1.13e-03 |
|
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: 38.39 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300172100 895 GNKQVKLTVSGTTTVYQLKMLIWEWLGVVKENQEV-HFGKVeLTDEsTTLADVGVLPNSQLWV 956
Cdd:smart00213 9 DGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLiYKGKV-LEDD-RTLADYGIQDGSTIHL 69
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-398 |
1.07e-116 |
|
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: 361.35 E-value: 1.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNTTFRNGVFS------AEMELVRND------PVLHQLARLFAQLHSGTKSSVDSAAFATT 148
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstedAELKNMPPDkphepqTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 149 LELDNAVQQDGQEFLKLLLTLLERVLAQSRVPEARDVVQNLFRGTFSYVTKCSSCGKESGASDqfvDFYELEVNVKGFSS 228
Cdd:cd02668 81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPS---KFYELELQLKGHKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 229 LEESLDDYLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLKTSTKKKVTSKFMFPKVLDMERRVs 308
Cdd:cd02668 158 LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 309 pvtsDGSPGEPAHYDLFAILMHKGNMASSGHYVVHIRDERTGQWWQFDDEEVTMLGSNPLGEPTSKlDKVSPDRDD---N 385
Cdd:cd02668 237 ----AESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSE-DPAKPRKSEikkG 311
|
330
....*....|...
gi 300172100 386 LLMSPDAYMLMFS 398
Cdd:cd02668 312 THSSRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-399 |
1.02e-76 |
|
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: 254.87 E-value: 1.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNTTFRNGVFSAEmELVRNDPVLH---QLARLFAQLHSGtkssvDSAAFATTL-------- 149
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIP-PTEDDDDNKSvplALQRLFLFLQLS-----ESPVKTTELtdktrsfg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 150 --ELDNAVQQDGQEFLKLLLTLLERVLAQSRVPearDVVQNLFRGTFSYVTKCSSCGKESgaSDQFvDFYELEVNVKGFS 227
Cdd:cd02659 78 wdSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQE---GLIKNLFGGKLVNYIICKECPHES--EREE-YFLDLQVAVKGKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 228 SLEESLDDYLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLKTSTKKKVTSKFMFPKVLDMER-- 305
Cdd:cd02659 152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPyt 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 306 ----RVSPVTSDGSPGEPAHYDLFAILMHKGNmASSGHYVVHIRDERTGQWWQFDDEEVTMLGSNPL------GEPTSKL 375
Cdd:cd02659 232 ekglAKKEGDSEKKDSESYIYELHGVLVHSGD-AHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfgGEETQKT 310
|
330 340
....*....|....*....|....*..
gi 300172100 376 DKVSPD---RDDNllmspdAYMLMFSR 399
Cdd:cd02659 311 YDSGPRafkRTTN------AYMLFYER 331
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
80-397 |
1.27e-60 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 209.61 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 80 AGLTNLGATCYVNSVLQCLFMNTTFRNGVFSAEMELVRNDP-----VLHQLARLFAQLHSGTKSS-VDSAAFATTLELDN 153
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYnkdinLLCALRDLFKALQKNSKSSsVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 154 AV-----QQDGQEFLKLLLTLLERVLAQSRVPEARDVVQNLFRGTFSYVTKCSSCGKESGASDQFVDF---YELEVNVKG 225
Cdd:pfam00443 81 PDfsgykQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpIPGDSAELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 226 FSSLEESLDDYLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLktSTKKKVTSKFMFPKVLDMER 305
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNR--STWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 306 RVSPvTSDGSPGEPAHYDLFAILMHKGNmASSGHYVVHIRDERTGQWWQFDDEEVTmlgsnplgeptskldKVSPDRDdn 385
Cdd:pfam00443 239 YLAE-ELKPKTNNLQDYRLVAVVVHSGS-LSSGHYIAYIKAYENNRWYKFDDEKVT---------------EVDEETA-- 299
|
330
....*....|..
gi 300172100 386 lLMSPDAYMLMF 397
Cdd:pfam00443 300 -VLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
81-397 |
5.81e-60 |
|
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: 205.79 E-value: 5.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNttfrngvfsaemelvrndpvlhqlarlfaqlhsgtkssvdsaafattleldnavQQDGQ 160
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFSE------------------------------------------------------QQDAH 26
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 161 EFLKLLLTLLERVLAQSRVPE-----ARDVVQNLFRGTFSYVTKCSSCGKESGASDQFvDFYELEVNVKGF--SSLEESL 233
Cdd:cd02257 27 EFLLFLLDKLHEELKKSSKRTsdsssLKSLIHDLFGGKLESTIVCLECGHESVSTEPE-LFLSLPLPVKGLpqVSLEDCL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 234 DDYLNEEKLSGENQYFCEyCKARVDATHSTKLRLLPPVLNFQLKRFVFNlKTSTKKKVTSKFMFPKVLDMERRVSPVTSD 313
Cdd:cd02257 106 EKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPYLSEGEKD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 314 GSPGEPAH-YDLFAILMHKGNMASSGHYVVHIRDERTGQWWQFDDEEVTmlgsnplgeptskldKVSPDRDDNLL-MSPD 391
Cdd:cd02257 184 SDSDNGSYkYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVT---------------EVSEEEVLEFGsLSSS 248
|
....*.
gi 300172100 392 AYMLMF 397
Cdd:cd02257 249 AYILFY 254
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
81-425 |
4.37e-49 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 189.70 E-value: 4.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNTTFRNGVFSAEMELVR-NDPVLHQLARLFAQLHSGtKSSVDSAAFATTLELDNAV---Q 156
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRgRDSVALALQRLFYNLQTG-EEPVDTTELTRSFGWDSDDsfmQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 157 QDGQEFLKLLLTLLERVLAQSRVpeaRDVVQNLFRGTFSYVTKCSSCGKESGASDqfvDFYELEVNVKGFSSLEESLDDY 236
Cdd:COG5077 274 HDIQEFNRVLQDNLEKSMRGTVV---ENALNGIFVGKMKSYIKCVNVNYESARVE---DFWDIQLNVKGMKNLQESFRRY 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 237 LNEEKLSGENQYFCEYcKARVDATHSTKLRLLPPVLNFQLKRFVFNLKTSTKKKVTSKFMFPKVLDMERRVSPvTSDGSP 316
Cdd:COG5077 348 IQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDR-DADKSE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 317 GEPAHYDLFAILMHKGNMaSSGHYVVHIRDERTGQWWQFDDEEVT------MLGSNPLGEPTSKlDKVSPDRDDNLLMSp 390
Cdd:COG5077 426 NSDAVYVLYGVLVHSGDL-HEGHYYALLKPEKDGRWYKFDDTRVTratekeVLEENFGGDHPYK-DKIRDHSGIKRFMS- 502
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 300172100 391 dAYMLMFSRRTS-----TPRVAEEpvrsIPEFLKAEVDEQ 425
Cdd:COG5077 503 -AYMLVYLRKSMlddllNPVAAVD----IPPHVEEVLSEE 537
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-398 |
1.63e-42 |
|
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: 157.44 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 79 PAGLTNLGATCYVNSVLQCLFMNTTFRNGVFSAEMELVRNDP---VLHQLARLFAQLHSGTKSSVDSAAFATTLE----- 150
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEgfcMMCALEAHVERALASSGPGSAPRIFSSNLKqiskh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 151 LDNAVQQDGQEFLKLLLTLLERVLAQSRVPE--------ARDVVQNLFRGTFSYVTKCSSCGKESGASDQFVDfyeLEVN 222
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavdpssqETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLD---LSLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 223 VKGFSSLEESLDDYLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNlktsTKKKVTSKFMFPKVLD 302
Cdd:cd02661 158 IKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF----RGGKINKQISFPETLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 303 MerrvSPVTSDgSPGEPAHYDLFAILMHKGNMASSGHYVVHIRDERtGQWWQFDDeevtmlgsnplgeptsklDKVSPDR 382
Cdd:cd02661 234 L----SPYMSQ-PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSN-GKWYNMDD------------------SKVSPVS 289
|
330
....*....|....*.
gi 300172100 383 DDNLLmSPDAYMLMFS 398
Cdd:cd02661 290 IETVL-SQKAYILFYI 304
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-363 |
1.26e-38 |
|
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: 147.13 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNTTFRNGVFS-----AEMELVRNDPVLHQLARLFAQLH-SGTKSSVDSAAFATTL----- 149
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrhscTCLSCSPNSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSwkhsr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 150 ELDNAVQQDGQEFLKLLLTLLERVLAqSRVPEARD------VVQNLFRGTFSYVTKCSSCGKESGASDQFVDFyELEVN- 222
Cdd:cd02660 82 NLAGYSQQDAHEFFQFLLDQLHTHYG-GDKNEANDeshcncIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDL-SLDIPn 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 223 ------------VKGFSSLEESLDDYLNEEKLsGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLkTSTKKK 290
Cdd:cd02660 160 kstpswalgesgVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL-NKTSRK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300172100 291 VTSKFMFPKVLDMERRVSPVTSDGSPGEPAH----YDLFAILMHKGNMaSSGHYVVHIRDeRTGQWWQFDDEEVTML 363
Cdd:cd02660 238 IDTYVQFPLELNMTPYTSSSIGDTQDSNSLDpdytYDLFAVVVHKGTL-DTGHYTAYCRQ-GDGQWFKFDDAMITRV 312
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-398 |
3.28e-38 |
|
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: 142.81 E-value: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNttfrngvfsaemelvrndpvlhqlarlfaqlhsgtkssvdsaafattleldnavQQDGQ 160
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSAD------------------------------------------------------QQDAQ 26
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 161 EFLKLLLTLLERVlaqsrvpeardvVQNLFRGTFSYVTKCSSCGKESGASDQFVDfyeLEVNV------KGFSSLEESLD 234
Cdd:cd02674 27 EFLLFLLDGLHSI------------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTY---LSLPIpsgsgdAPKVTLEDCLR 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 235 DYLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNlkTSTKKKVTSKFMFP-KVLDMerrvSPVTSD 313
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPlNDLDL----TPYVDT 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 314 GSPGEPAHYDLFAILMHKGNMaSSGHYVVHIRDERTGQWWQFDDEEVTmlgsnplgeptskldKVSPDRDDnllmSPDAY 393
Cdd:cd02674 166 RSFTGPFKYDLYAVVNHYGSL-NGGHYTAYCKNNETNDWYKFDDSRVT---------------KVSESSVV----SSSAY 225
|
....*
gi 300172100 394 MLMFS 398
Cdd:cd02674 226 ILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-361 |
3.83e-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 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: 139.93 E-value: 3.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNTTFRNGVFSAEMELVRND---PVLHQLARLFAQLHSGTKSSVDSAAFATTLE--LDNAV 155
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSqsvMKKLQLLQAHLMHTQRRAEAPPDYFLEASRPpwFTPGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 156 QQDGQEFLkllltlleRVLAQSRVPeardVVQNLFRGTFSYVTKCSSCGKESGASDQFVDfyeLEVNvkgFSSLEESLDD 235
Cdd:cd02664 81 QQDCSEYL--------RYLLDRLHT----LIEKMFGGKLSTTIRCLNCNSTSARTERFRD---LDLS---FPSVQDLLNY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 236 YLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLKTSTKKKVTSKFMFPKVLDMERRVSPVTS--- 312
Cdd:cd02664 143 FLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKSSesp 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 313 -------DGSPGE----PAHYDLFAILMHKGNMASSGHYVVHIRD----ERTGQ----------------WWQFDDEEVT 361
Cdd:cd02664 223 lekkeeeSGDDGElvtrQVHYRLYAVVVHSGYSSESGHYFTYARDqtdaDSTGQecpepkdaeendesknWYLFNDSRVT 302
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-361 |
6.87e-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: 6.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLF----MNTTFRNGVFSAEMELVRNDPVLHQLARLFAQLhSGTKSSVDSAAFATTL------- 149
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRsvpeLRDALKNYNPARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLrmafpqf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 150 -ELDNA---VQQDGQEFLKLLLtlleRVLAQSRVPEARD--VVQNLFRGTFSYVTKCSSCGKESGASDqfVDFYELEVNV 223
Cdd:cd02657 80 aEKQNQggyAQQDAEECWSQLL----SVLSQKLPGAGSKgsFIDQLFGIELETKMKCTESPDEEEVST--ESEYKLQCHI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 224 KG---FSSLEESLDDYLNEE--KLSGENQYfceyckarvDATHSTKLRL--LPPVLNFQLKRFVFNLKTSTKKKVTSKFM 296
Cdd:cd02657 154 SItteVNYLQDGLKKGLEEEieKHSPTLGR---------DAIYTKTSRIsrLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300172100 297 FPKVLDMERRVSPvtsdgspgePAHYDLFAILMHKGNMASSGHYVVHIRDERTGQWWQFDDEEVT 361
Cdd:cd02657 225 FPFELDLYELCTP---------SGYYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVS 280
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-363 |
9.55e-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: 134.74 E-value: 9.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNTTFrngvfsaemelvrndpvlHQLARLFAQLhSGTKSSVDSAA---FATTL----EL-D 152
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLL------------------TCLKDLFESI-SEQKKRTGVISpkkFITRLkrenELfD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 153 NAVQQDGQEF--------------LKLLLTLLERVLAQSRVPEARDVVQNLFRGTFSYVTKCSSCGKESGASDQFVDfye 218
Cdd:cd02663 62 NYMHQDAHEFlnfllneiaeildaERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLD--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 219 LEVNVKGFSSLEESLDDYLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLKTSTKKKVTSKFMFP 298
Cdd:cd02663 139 LSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFP 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300172100 299 KVLDMerrvsPVTSDGSPGEPAHYDLFAILMHKGNMASSGHYVVHIRDerTGQWWQFDDEEVTML 363
Cdd:cd02663 219 LELRL-----FNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKS--HGGWLLFDDETVEKI 276
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
889-996 |
1.55e-27 |
|
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: 107.37 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 889 RRTVATgnkQVKLTVSGTTTVYQLKMLIWEWLGVVKENQEVHFGKVELTDESTTLADVGVLPNSQLWVSDSGLHEHRDIA 968
Cdd:cd01795 1 RRVRGE---RKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDA 77
|
90 100
....*....|....*....|....*...
gi 300172100 969 GkpmlslFIYVSLIASLWFSQTSSRLHS 996
Cdd:cd01795 78 D------EADVSRARVPEEGFKGTALLG 99
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-360 |
3.58e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 113.19 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNTTF--RNGVFSAEMELVRNDPVLH---QLARLFAQLHSGtKSSVDSAAFATTLELDNAV 155
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqwRYDDLENKFPSDVVDPANDlncQLIKLADGLLSG-RYSKPASLKSENDPYQVGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 156 --------------------QQDGQEFLKLLLTLLERVLAQSRVPEARDVvqnlfrgtFSYVT----KCSSCGKeSGASD 211
Cdd:cd02658 80 kpsmfkaligkghpefstmrQQDALEFLLHLIDKLDRESFKNLGLNPNDL--------FKFMIedrlECLSCKK-VKYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 212 QFVDFYELEV--NVKGFS----------SLEESLDDYLNEEKLsgenQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRF 279
Cdd:cd02658 151 ELSEILSLPVpkDEATEKeegelvyepvPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 280 VFNlKTSTKKKvtskfmfpkvLDMerrvsPVTSDGSPGePAHYDLFAILMHKGNMASSGHYVVHIR--DERTGQWWQFDD 357
Cdd:cd02658 227 QLL-ENWVPKK----------LDV-----PIDVPEELG-PGKYELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFND 289
|
...
gi 300172100 358 EEV 360
Cdd:cd02658 290 EKV 292
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-346 |
1.01e-26 |
|
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: 110.94 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMnTTFRNGVFSAemelvrnDPVLhqlarLFAQLHSgtKSSvdsaafattlELDNAVQQDGQ 160
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQ-TPALRELLSE-------TPKE-----LFSQVCR--KAP----------QFKGYQQQDSH 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 161 EFLkllltlleRVLAQSrvpeARDVVQNLFRGTFSYVTKCSSCGKESGASDQFVDF----YELEVNVKgfsSLEESLDDY 236
Cdd:cd02667 56 ELL--------RYLLDG----LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLslprSDEIKSEC---SIESCLKQF 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 237 LNEEKLSGENQYFCEYCkarvdaTHSTKLRL---LPPVLNFQLKRFvFNLKTSTKKKVTSKFMFPKVLDMERRVSPVTSD 313
Cdd:cd02667 121 TEVEILEGNNKFACENC------TKAKKQYLiskLPPVLVIHLKRF-QQPRSANLRKVSRHVSFPEILDLAPFCDPKCNS 193
|
250 260 270
....*....|....*....|....*....|...
gi 300172100 314 GSPGEPAHYDLFAILMHKGNMaSSGHYVVHIRD 346
Cdd:cd02667 194 SEDKSSVLYRLYGVVEHSGTM-RSGHYVAYVKV 225
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
67-404 |
1.85e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 108.83 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 67 PDPSRELRVMDIP-AGLTNLGATCYVNSVLQCLFMNTTFRNGVFSaemeLVRNDPVLHQLARLFAQLHSGTKSSVDSAAF 145
Cdd:cd02671 11 SATSCEKRENLLPfVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKH----LVSLISSVEQLQSSFLLNPEKYNDELANQAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 146 ATTLeldNAVQQDGQEFLKLLLTLLERVLaQSRVPEARDVVQNLFRGTFSYVTKCSSCgkESgASDQFVDFYELEVNVK- 224
Cdd:cd02671 87 RRLL---NALREVNPMYEGYLQHDAQEVL-QCILGNIQELVEKDFQGQLVLRTRCLEC--ET-FTERREDFQDISVPVQe 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 225 -GFSSLEESLD-----------------DYLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLKTS 286
Cdd:cd02671 160 sELSKSEESSEispdpktemktlkwaisQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 287 TK----KKVTSKFMFPKVLDMERRvspvtsdgSPGEPAH-YDLFAILMHKGNMASSGHYVVHIRdertgqWWQFDDEEVt 361
Cdd:cd02671 240 DCygglSKVNTPLLTPLKLSLEEW--------STKPKNDvYRLFAVVMHSGATISSGHYTAYVR------WLLFDDSEV- 304
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 300172100 362 mlgsnplgeptskldKVSPDRDDNLLMSPDaymlmfSRRTSTP 404
Cdd:cd02671 305 ---------------KVTEEKDFLEALSPN------TSSTSTP 326
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-395 |
6.59e-18 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 84.34 E-value: 6.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLfmnttfrngvfsaemelvrndpvlhqlarlfaqlhsgtkSSVDSaaFATTLElDNAVQQDGQ 160
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL---------------------------------------ASLPS--LIEYLE-EFLEQQDAH 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 161 EFLKllltllerVLAQSrvpeARDVVQNLFRGTFSYVTKCSSCGKESGasDQFVDFYELEVNV-----KGFSSLEESLDD 235
Cdd:cd02662 39 ELFQ--------VLLET----LEQLLKFPFDGLLASRIVCLQCGESSK--VRYESFTMLSLPVpnqssGSGTTLEHCLDD 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 236 YLNEEKLSGenqYFCEYCKARVDAthstklrlLPPVLNFQLKRFVFNLK-TSTKKkvTSKFMFPKVLdmeRRVSpvtsdg 314
Cdd:cd02662 105 FLSTEIIDD---YKCDRCQTVIVR--------LPQILCIHLSRSVFDGRgTSTKN--SCKVSFPERL---PKVL------ 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 315 spgepahYDLFAILMHKGNMaSSGHYVVH--------------------IRDERTGQWWQFDDEEVTmlgsnplgeptsk 374
Cdd:cd02662 163 -------YRLRAVVVHYGSH-SSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVK------------- 221
|
330 340
....*....|....*....|.
gi 300172100 375 ldKVSpdrDDNLLMSPDAYML 395
Cdd:cd02662 222 --EVS---ESEVLEQKSAYML 237
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-361 |
1.30e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 85.62 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 79 PAGLTNLGATCYVNSVLQCLFMNTTFRNGVFSAE-----------------------MELVRNDPVLHQLARLFAQLHSG 135
Cdd:cd02666 1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDeskaelasdypterriggrevsrSELQRSNQFVYELRSLFNDLIHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 136 TKSSVdsaafATTLELDNAV--QQDGQEFLKLLLTLLERVLAQSRV----------PEARDVVQNLFRGTFSYVTKCSSC 203
Cdd:cd02666 81 NTRSV-----TPSKELAYLAlrQQDVTECIDNVLFQLEVALEPISNafagpdteddKEQSDLIKRLFSGKTKQQLVPESM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 204 GKESGASDQFVDFYELEVNV-KGFS---------SLEESLDDYLNEE---KLSGENQYFCEYCKARVDATHSTKLRLLPP 270
Cdd:cd02666 156 GNQPSVRTKTERFLSLLVDVgKKGReivvllepkDLYDALDRYFDYDsltKLPQRSQVQAQLAQPLQRELISMDRYELPS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 271 VLN-------------FQLKRFVFNLKTSTKKKVTSKFmfpkvlDMERRVSpvtsdgspgepahYDLFAILMHKGNmASS 337
Cdd:cd02666 236 SIDdidelireaiqseSSLVRQAQNELAELKHEIEKQF------DDLKSYG-------------YRLHAVFIHRGE-ASS 295
|
330 340
....*....|....*....|....
gi 300172100 338 GHYVVHIRDERTGQWWQFDDEEVT 361
Cdd:cd02666 296 GHYWVYIKDFEENVWRKYNDETVT 319
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
228-361 |
2.90e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 80.70 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 228 SLEESLDDYLNEEKLSGENQYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLKTSTKKKVTSKFMFPKvLDMERRV 307
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDD-LDLSGVE 754
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 300172100 308 SPVTSdgspgEPAHYDLFAILMHKGNMaSSGHYVVHIRDERTGQWWQFDDEEVT 361
Cdd:COG5560 755 YMVDD-----PRLIYDLYAVDNHYGGL-SGGHYTAYARNFANNGWYLFDDSRIT 802
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
81-399 |
3.93e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 70.99 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNT----------TFRNGVFSAEMELVRNDPVLHQLARLFAQLHSGTKSSVDSAAfattle 150
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLpkldellddlSKELKVLKNVIRKPEPDLNQEEALKLFTALWSSKEHKVGWIP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 151 lDNAVQQDGQEFLKLLLtllervlaqsrvpearDVVQNLFRGTFSYVTKCSSCGKESGASDQFVDFY---ELEVNVKGFS 227
Cdd:COG5533 75 -PMGSQEDAHELLGKLL----------------DELKLDLVNSFTIRIFKTTKDKKKTSTGDWFDIIielPDQTWVNNLK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 228 SLEESLD--DYLNEEKLS---GENQYFceycKARVDATHSTKLRLLPPVLNFQLKRFVFNL-KTSTKKKVTSKFMFPKVL 301
Cdd:COG5533 138 TLQEFIDnmEELVDDETGvkaKENEEL----EVQAKQEYEVSFVKLPKILTIQLKRFANLGgNQKIDTEVDEKFELPVKH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 302 DMERRVSPVTsdgspgepaHYDLFAILMHKGNMaSSGHYVVHIRdeRTGQWWQFDDeevtmlgsnplgeptSKLDKVSPD 381
Cdd:COG5533 214 DQILNIVKET---------YYDLVGFVLHQGSL-EGGHYIAYVK--KGGKWEKAND---------------SDVTPVSEE 266
|
330
....*....|....*...
gi 300172100 382 RDDNlLMSPDAYMLMFSR 399
Cdd:COG5533 267 EAIN-EKAKNAYLYFYER 283
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
135-397 |
8.73e-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: 68.74 E-value: 8.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 135 GTKSSVDSAAFATTLELDNAVQQDGQEFLKLLLTLLERVL-AQSRVPEARDVVQN----LFRGTFSYVTkcSSCGKESGA 209
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLFSQQQDVSEFTHLLLDWLEDAFqAAAEAISPGEKSKNpmvqLFYGTFLTEG--VLEGKPFCN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 210 SDQFvdfYELEVNVKGFSSLEESLDDYLNEEKLSGENqyfceyckarvdATHSTKLRL------LPPVLNFQLKRFVFNl 283
Cdd:cd02665 79 CETF---GQYPLQVNGYGNLHECLEAAMFEGEVELLP------------SDHSVKSGQerwfteLPPVLTFELSRFEFN- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 284 kTSTKKKVTSKFMFPKVLDMERrvspvtsdgspgepahYDLFAILMHKGNmASSGHYVVHIRDERTGQWWQFDDEEVTml 363
Cdd:cd02665 143 -QGRPEKIHDKLEFPQIIQQVP----------------YELHAVLVHEGQ-ANAGHYWAYIYKQSRQEWEKYNDISVT-- 202
|
250 260 270
....*....|....*....|....*....|....*
gi 300172100 364 gsnplgeptsKLDKVSPDRDD-NLLMSPDAYMLMF 397
Cdd:cd02665 203 ----------ESSWEEVERDSfGGGRNPSAYCLMY 227
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
467-531 |
6.20e-11 |
|
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: 59.30 E-value: 6.20e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300172100 467 KGFWISAEWLRNWTDSLKP----PSAIDNSILLCEHERVSPKSIQLMK----CISDAAWQSLHSKYGGQPVVT 531
Cdd:pfam06337 3 KVYLISSKWLNKWKSYVKEpnnePGPIDNSDLLDDESNGQLKPNLQEGvdyvIVPEEVWEFLVEWYGGGPEIK 75
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
80-357 |
1.35e-10 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 63.83 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 80 AGLTNLGATCYVNSVLQCLFMNTTFRN-GVFSAEMELVRNDPVLHQLARLFAQLHSGTKS---------SVDSAAFATTL 149
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLATECLKEHCLLCELGFLFDMLEKAKGKncqasnflrALSSIPEASAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 150 ELdnavqqdGQEFLKLLLTLLERVLAQS------------------RVPEARDVVQNLFRGTFSYVTKCSSCGKES-GAS 210
Cdd:pfam13423 81 GL-------LDEDRETNSAISLSSLIQSfnrflldqlsseenstppNPSPAESPLEQLFGIDAETTIRCSNCGHESvRES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 211 DQFVdfYELEVNVKGFSSLEE----SLDDYLnEEKLSGENQY--FCEYCKARVDATHSTKLRLLPPVLnfqlkrfVFNLK 284
Cdd:pfam13423 154 STHV--LDLIYPRKPSSNNKKppnqTFSSIL-KSSLERETTTkaWCEKCKRYQPLESRRTVRNLPPVL-------SLNAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 285 TSTKK----KVTSKFmFPKVLDMERRVSPVTSDGSpgepAHYDLFAILMHKGNMASSGHYVVHIR-------DERTGQWW 353
Cdd:pfam13423 224 LTNEEwrqlWKTPGW-LPPEIGLTLSDDLQGDNEI----VKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWY 298
|
....
gi 300172100 354 QFDD 357
Cdd:pfam13423 299 LFND 302
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-361 |
3.80e-09 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 60.02 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLFMNTTFRNGVFS---AEMELVRNDPVLHQLARLFAQLHSGT--KSSVDSAAFATTLEL---- 151
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLyenYENIKDRKSELVKRLSELIRKIWNPRnfKGHVSPHELLQAVSKvskk 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 152 --DNAVQQDGQEFLKLLLTLLERVLAQSRvPEARDVVQNLFRGTFSYVTKCSSCGKESGASDQ--FVDFYELEVNVKGFS 227
Cdd:cd02669 201 kfSITEQSDPVEFLSWLLNTLHKDLGGSK-KPNSSIIHDCFQGKVQIETQKIKPHAEEEGSKDkfFKDSRVKKTSVSPFL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 228 SLeeSLD--------DYLNE---------EKLSGenqYFCEYCKARVDATHSTKLRLLPPVLNFQLKRFVFNLKTSTKKK 290
Cdd:cd02669 280 LL--TLDlpppplfkDGNEEniipqvplkQLLKK---YDGKTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNP 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300172100 291 --VTskfmFP-KVLDMERRVSPVTSDGSPGEpaHYDLFAILMHKGNMASSGHYVVHIRDERTGQWWQFDDEEVT 361
Cdd:cd02669 355 tiVN----FPiKNLDLSDYVHFDKPSLNLST--KYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVK 422
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
81-162 |
4.17e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 54.12 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 81 GLTNLGATCYVNSVLQCLfMNTTFRNGVF---SAEMELVRNDPV-LH-QLARLFA----QLHSGTKSSVDSAAFATTL-- 149
Cdd:COG5560 267 GLRNLGNTCYMNSALQCL-MHTWELRDYFlsdEYEESINEENPLgMHgSVASAYAdlikQLYDGNLHAFTPSGFKKTIgs 345
|
90
....*....|....*.
gi 300172100 150 ---ELDNAVQQDGQEF 162
Cdd:COG5560 346 fneEFSGYDQQDSQEF 361
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
469-528 |
1.17e-06 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 47.35 E-value: 1.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300172100 469 FWISAEWLRNWTDSL-----KPPSAIDNSILLCEHERVSPKSI----QLMKCISDAAWQSLHSKYGGQP 528
Cdd:smart00695 9 YLISTRWYRQWADFVegkdgKDPGPIDNSGILCSHGGPRLKEHlvegEDYVLIPEELWNKLVRWYGGGP 77
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
82-366 |
9.76e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 48.29 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 82 LTNLGATCYVNSVLQCLfmnttfrngvfsAEMELVRNdpvlhqlarlfaqlhsgtkssvdsaafattlELDNAVQQDGQE 161
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL------------SSIGKINT-------------------------------EFDNDDQQDAHE 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 162 FLKLLLTLLERVLA--QSRVPEARDVVQNL-----FRGTFSYVTKCSSCGKESGASDQFVDfyeLEVNVKGFSSLEesLD 234
Cdd:cd02673 39 FLLTLLEAIDDIMQvnRTNVPPSNIEIKRLnpleaFKYTIESSYVCIGCSFEENVSDVGNF---LDVSMIDNKLDI--DE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 235 DYLNEEKLSGENQYFCEYCKARvDATHSTKLRLLPPVLNFQLKRFVFNLKTSTKKKvTSKFMFPKVLdmerrvspvtsdg 314
Cdd:cd02673 114 LLISNFKTWSPIEKDCSSCKCE-SAISSERIMTFPECLSINLKRYKLRIATSDYLK-KNEEIMKKYC------------- 178
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 300172100 315 spGEPAHYDLFAILMHKGNMASSGHYVVHIRDERTG-QWWQFDDEEVTMLGSN 366
Cdd:cd02673 179 --GTDAKYSLVAVICHLGESPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKN 229
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
895-954 |
1.44e-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: 41.00 E-value: 1.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 895 GNKQVKLTVSGTTTVYQLKMLIWEWLGVVKENQEVHFGKVELTDEStTLADVGVLPNSQL 954
Cdd:pfam00240 7 DGKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQ-TLGEYGIEDGSTI 65
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
199-397 |
2.31e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 44.05 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 199 KCSSCGKESGASDQFVDFYELEVNVkgfssleeslDDYLNEEKLSGEN---QYFceyckarvdatHSTKLRLLPPVLNFQ 275
Cdd:cd02670 47 DIIHGGKKDQDDDKLVNERLLQIPV----------PDDDDGGGITLEQcleQYF-----------NNSVFAKAPSCLIIC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300172100 276 LKRFVFNlkTSTKKKVTSKFMFPKVLDM----------------ERRVSPVTSDgSPGEPAHYDLF--AILMHKGNMASS 337
Cdd:cd02670 106 LKRYGKT--EGKAQKMFKKILIPDEIDIpdfvaddpracskcqlECRVCYDDKD-FSPTCGKFKLSlcSAVCHRGTSLET 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300172100 338 GHYVVHIR-----------DERTGQWWQFDD---EEVTMLGSNplgeptskldkvspdRDDNLLMSpDAYMLMF 397
Cdd:cd02670 183 GHYVAFVRygsysltetdnEAYNAQWVFFDDmadRDGVSNGFN---------------IPAARLLE-DPYMLFY 240
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| Ubl_ubiquitin_like |
cd17039 |
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
895-956 |
3.16e-04 |
|
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: 39.89 E-value: 3.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300172100 895 GNKQVKLTVSGTTTVYQLKMLIWEWLGVVKENQE-VHFGKvELTDEsTTLADVGVLPNSQLWV 956
Cdd:cd17039 7 DGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRlIYNGK-ELKDD-KTLSDYGIKDGSTIHL 67
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
895-956 |
1.13e-03 |
|
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: 38.39 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300172100 895 GNKQVKLTVSGTTTVYQLKMLIWEWLGVVKENQEV-HFGKVeLTDEsTTLADVGVLPNSQLWV 956
Cdd:smart00213 9 DGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLiYKGKV-LEDD-RTLADYGIQDGSTIHL 69
|
|
| Ubiquitin_like_fold |
cd00196 |
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ... |
892-954 |
5.48e-03 |
|
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily.
Pssm-ID: 340450 Cd Length: 68 Bit Score: 36.53 E-value: 5.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300172100 892 VATGNKQVK-LTVSGTTTVYQLKMLIWEWLGVVKENQEVHFGKVELTDeSTTLADVGVLPNSQL 954
Cdd:cd00196 3 VETPSLKKIvVAVPPSTTLRQVLEKVAKRIGLPPDVIRLLFNGQVLDD-LMTAKQVGLEPGEEL 65
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