|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-419 |
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: 570.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYtkGDGIRGGKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNIQGHKQL 249
Cdd:cd02668 79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 250 TDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEPY-VE 328
Cdd:cd02668 159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 329 HKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 408
Cdd:cd02668 239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313
|
330
....*....|.
gi 1937918211 409 CSRNAYMLVYR 419
Cdd:cd02668 314 SSRTAYMLVYK 324
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-418 |
1.67e-59 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 206.52 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIrggkdyepqTICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDI---------NLLCALRDLFkALQKNSKSSSVSPKM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYE 238
Cdd:pfam00443 72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 239 LELNIQGHK------QLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 313 AYIGFSESLDMEPYV-----EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDIEkmegkklqlgiE 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------E 293
|
330 340 350
....*....|....*....|....*....|.
gi 1937918211 388 EDLAEPSKSQtrkpkcgkgthcsrNAYMLVY 418
Cdd:pfam00443 294 VDEETAVLSS--------------SAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-458 |
1.77e-45 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 178.53 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 72 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDytkgdgirgGKDyepqTICEHLQYL 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPR---------GRD----SVALALQRL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNVVQQQFCGEYAYVTVCSQCGR 228
Cdd:COG5077 244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 229 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 309 KKLNAYIGFSESLDMEPYVEH-----KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDI---EKMEGK 380
Cdd:COG5077 399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 381 KLQLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTQEkNHTM-----VQVPAFLQELVDRDNSKFEEWCVEMA 455
Cdd:COG5077 478 EENFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSML-DDLLnpvaaVDIPPHVEEVLSEEIDKTEVRCKEID 549
|
...
gi 1937918211 456 EMR 458
Cdd:COG5077 550 EIH 552
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
940-1035 |
4.77e-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: 143.19 E-value: 4.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 940 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1016
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
|
90
....*....|....*....
gi 1937918211 1017 DVMQVCMPEEGFKGTGLLG 1035
Cdd:cd01795 81 DVSRARVPEEGFKGTALLG 99
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
484-554 |
1.16e-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: 55.84 E-value: 1.16e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937918211 484 EPYEFVSLEWLQKWL----DESTPTKPIDNN--ACLCSHDKLHPDKISIMK--RISEYAADIFYSRYGGGPRLTVKALC 554
Cdd:pfam06337 2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
945-1003 |
1.21e-05 |
|
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression
Pssm-ID: 214563 [Multi-domain] Cd Length: 72 Bit Score: 44.17 E-value: 1.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937918211 945 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1003
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
483-556 |
2.70e-05 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 43.50 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 483 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNNACLCSHD--KLHPDKI--SIMKRISEYAADIFYSRYGGGPR-LTVKA 552
Cdd:smart00695 5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84
|
....
gi 1937918211 553 LCKD 556
Cdd:smart00695 85 VCQG 88
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
950-1003 |
1.38e-03 |
|
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.
Pssm-ID: 459726 [Multi-domain] Cd Length: 72 Bit Score: 38.31 E-value: 1.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1937918211 950 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDcATLGTLGVIPESVILL 1003
Cdd:pfam00240 15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDD-QTLGEYGIEDGSTIHL 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-419 |
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: 570.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYtkGDGIRGGKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNIQGHKQL 249
Cdd:cd02668 79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 250 TDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEPY-VE 328
Cdd:cd02668 159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 329 HKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 408
Cdd:cd02668 239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313
|
330
....*....|.
gi 1937918211 409 CSRNAYMLVYR 419
Cdd:cd02668 314 SSRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
88-419 |
3.80e-79 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 261.81 E-value: 3.80e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 88 FVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdytkgdgirGGKDYEPQTICeHLQYLFALLQNSNRRYIDPSG 167
Cdd:cd02659 2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-----------EDDDDNKSVPL-ALQRLFLFLQLSESPVKTTEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELN 242
Cdd:cd02659 70 TDKTRSfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 243 IQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLD 322
Cdd:cd02659 147 VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 323 MEPYVEH------------KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDIEKM---EGKKLQLGIE 387
Cdd:cd02659 227 MEPYTEKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGE 305
|
330 340 350
....*....|....*....|....*....|..
gi 1937918211 388 EDLAEPSKSQTRKPKCGkgthcsrNAYMLVYR 419
Cdd:cd02659 306 ETQKTYDSGPRAFKRTT-------NAYMLFYE 330
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-418 |
1.67e-59 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 206.52 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIrggkdyepqTICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDI---------NLLCALRDLFkALQKNSKSSSVSPKM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYE 238
Cdd:pfam00443 72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 239 LELNIQGHK------QLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 313 AYIGFSESLDMEPYV-----EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDIEkmegkklqlgiE 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------E 293
|
330 340 350
....*....|....*....|....*....|.
gi 1937918211 388 EDLAEPSKSQtrkpkcgkgthcsrNAYMLVY 418
Cdd:pfam00443 294 VDEETAVLSS--------------SAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
90-419 |
2.45e-57 |
|
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: 198.48 E-value: 2.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNtflqvwflnlelrqalylcpSTcsdytkgdgirggkdyepqticehLQYLFAllqnsnrryidpsgfv 169
Cdd:cd02257 1 GLNNLGNTCYLN--------------------SV------------------------LQALFS---------------- 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 170 kalgldtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNIQ 244
Cdd:cd02257 21 --------EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 245 GHKQ----LTDCISEFLKEERLEGDNRYFCEnCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNAYIGFSES 320
Cdd:cd02257 93 VKGLpqvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 321 LDMEPYVEHKG-------GSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEgkklqlgiEEDLAEP 393
Cdd:cd02257 171 LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVLEF 242
|
330 340
....*....|....*....|....*.
gi 1937918211 394 SKSqtrkpkcgkgthcSRNAYMLVYR 419
Cdd:cd02257 243 GSL-------------SSSAYILFYE 255
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-458 |
1.77e-45 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 178.53 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 72 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDytkgdgirgGKDyepqTICEHLQYL 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPR---------GRD----SVALALQRL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNVVQQQFCGEYAYVTVCSQCGR 228
Cdd:COG5077 244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 229 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 309 KKLNAYIGFSESLDMEPYVEH-----KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDI---EKMEGK 380
Cdd:COG5077 399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 381 KLQLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTQEkNHTM-----VQVPAFLQELVDRDNSKFEEWCVEMA 455
Cdd:COG5077 478 EENFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSML-DDLLnpvaaVDIPPHVEEVLSEEIDKTEVRCKEID 549
|
...
gi 1937918211 456 EMR 458
Cdd:COG5077 550 EIH 552
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
178-419 |
7.08e-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: 158.99 E-value: 7.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 178 QQQDAQEFsklfMSLLEDTLskqknpdvRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNI-----QGHKQ-LTD 251
Cdd:cd02674 21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 252 CISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHKKKLNAYIGFS-ESLDMEPYV--E 328
Cdd:cd02674 89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPlNDLDLTPYVdtR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 329 HKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEgkklqlgieedlaepsksqtrkpkcgKGTH 408
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS--------------------------ESSV 219
|
250
....*....|.
gi 1937918211 409 CSRNAYMLVYR 419
Cdd:cd02674 220 VSSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
1.45e-43 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 160.52 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQvwflnlelrqalylcpstCSDYTK--------GDGIRGGKDYEPQTICEHLQYLFALLQNSnRR 161
Cdd:cd02661 3 GLQNLGNTCFLNSVLQ------------------CLTHTPplanyllsREHSKDCCNEGFCMMCALEAHVERALASS-GP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 162 YIDPSGFVKAL-----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NVVQQQFCGEYAYVTVCSQCGR 228
Cdd:cd02661 64 GSAPRIFSSNLkqiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 229 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHk 308
Cdd:cd02661 144 VSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG- 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937918211 309 kKLNAYIGFSESLDMEPYV-EHKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPqSGDWYKFND 371
Cdd:cd02661 221 -KINKQISFPETLDLSPYMsQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDD 282
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
940-1035 |
4.77e-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: 143.19 E-value: 4.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 940 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1016
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
|
90
....*....|....*....
gi 1937918211 1017 DVMQVCMPEEGFKGTGLLG 1035
Cdd:cd01795 81 DVSRARVPEEGFKGTALLG 99
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
5.08e-40 |
|
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: 151.11 E-value: 5.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQvwflnlelrqALYLCPSTCSDYTKGDGIRGGKDyepQTICEHLQYLFALLQNSNRRYIDP-SGF 168
Cdd:cd02664 1 GLINLGNTCYMNSVLQ----------ALFMAKDFRRQVLSLNLPRLGDS---QSVMKKLQLLQAHLMHTQRRAEAPpDYF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 169 VKAL---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrnvVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNIqg 245
Cdd:cd02664 68 LEASrppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 246 hKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEP 325
Cdd:cd02664 134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 326 YVEHKGGSFV--------------------YELSAVLIHRGVSAYSGHYIAHVKDP--------------------QSGD 365
Cdd:cd02664 213 RVESKSSESPlekkeeesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQtdadstgqecpepkdaeendESKN 292
|
....*.
gi 1937918211 366 WYKFND 371
Cdd:cd02664 293 WYLFND 298
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-379 |
6.28e-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: 138.62 E-value: 6.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcSDYTkgdGIRGGKDYEPQTICEHLQYLFALLQNSNRRyIDPSGFV 169
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-------KNYN---PARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 170 KALGL---------DTGQ--QQDAQE-FSKLFMSLledTLSKQKNPDVRNVVQQQFCGEYAYVTVCS-QCGRESKLVSKF 236
Cdd:cd02657 70 QLLRMafpqfaekqNQGGyaQQDAEEcWSQLLSVL---SQKLPGAGSKGSFIDQLFGIELETKMKCTeSPDEEEVSTESE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 237 YELELNIqGHKQLTDCISEFLKEeRLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIG 316
Cdd:cd02657 147 YKLQCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937918211 317 FSESLDMEPYVEHKGgsfVYELSAVLIHRGVSAYSGHYIAHVKDPQSGDWYKFND--------EDIEKMEG 379
Cdd:cd02657 225 FPFELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
3.50e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 137.12 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQVwFLNLELRQALYLcpstcSD-YTKGDGIRGGKDyepqTICEHLQYLFA-LLQNSNRRyidPSG 167
Cdd:cd02660 2 GLINLGATCFMNVILQA-LLHNPLLRNYFL-----SDrHSCTCLSCSPNS----CLSCAMDEIFQeFYYSGDRS---PYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 168 FVKAL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNVVQQQFCGEYAYVTVCSQCGRESK 231
Cdd:cd02660 69 PINLLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVST 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 232 LVSKFYELELNIQGHKQ---------------LTDCISEFLKEERLeGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQL 296
Cdd:cd02660 146 TVDPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 297 MRFVFDrQTGHKKKLNAYIGFSESLDMEPYV----------EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDpQSGDW 366
Cdd:cd02660 225 KRFEHS-LNKTSRKIDTYVQFPLELNMTPYTsssigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQW 301
|
....*
gi 1937918211 367 YKFND 371
Cdd:cd02660 302 FKFDD 306
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-418 |
5.74e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 135.52 E-value: 5.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQVWFLNlelrqALYLCpstcsdytkgdgirggkdyepqticehLQYLFALLQNSNRRY--IDPSG 167
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFE-----NLLTC---------------------------LKDLFESISEQKKRTgvISPKK 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNVVQQQFCGEYAYVTVCSQCGR 228
Cdd:cd02663 49 FITRLKrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCET 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 229 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:cd02663 129 VSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 309 KKLNAYIGFSESL------DMEPYVEHKggsfvYELSAVLIHRGVSAYSGHYIAHVKdpQSGDWYKFNDEDIEKMEGKKL 382
Cdd:cd02663 209 IKLFYRVVFPLELrlfnttDDAENPDRL-----YELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAV 281
|
330 340 350
....*....|....*....|....*....|....*.
gi 1937918211 383 qlgieEDLAEPSKSQTrkpkcgkgthcsrNAYMLVY 418
Cdd:cd02663 282 -----EEFFGDSPNQA-------------TAYVLFY 299
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-401 |
3.88e-30 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 122.31 E-value: 3.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 78 PNCERRKKN--SFVGLTNLGATCYVNTFLQVwflnlelrqaLYLCPSTCSDYTKGDGIRGGKdyepqticEHLQYLFALL 155
Cdd:cd02671 12 ATSCEKRENllPFVGLNNLGNTCYLNSVLQV----------LYFCPGFKHGLKHLVSLISSV--------EQLQSSFLLN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 156 Q---NSNRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNVVQQQFCGEYAYVTVCSQCG 227
Cdd:cd02671 74 PekyNDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLECE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 228 ----------------RESKLVSKFYELELNIQGH---KQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSL 288
Cdd:cd02671 142 tfterredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 289 PCTLNLQLMRF----VFDRQTGHKKKLNAYIGFSESLDMEPYVEhKGGSFVYELSAVLIHRGVSAYSGHYIAHVKdpqsg 364
Cdd:cd02671 222 PEVITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR----- 295
|
330 340 350
....*....|....*....|....*....|....*..
gi 1937918211 365 dWYKFNDEDIEKMEGKKLqlgieEDLAEPSKSQTRKP 401
Cdd:cd02671 296 -WLLFDDSEVKVTEEKDF-----LEALSPNTSSTSTP 326
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-419 |
6.09e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 117.49 E-value: 6.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdytkgdgirggkdyepqticehlqyLFALLQNSNRRYIDpsgfv 169
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE---------------------------LFSQVCRKAPQFKG----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 170 kalgldtGQQQDAQEfskLFMSLLEDtlskqknpdVRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELEL----NIQG 245
Cdd:cd02667 49 -------YQQQDSHE---LLRYLLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 246 HKQLTDCISEFLKEERLEGDNRYFCENCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNAYIGFSESLDMEP 325
Cdd:cd02667 110 ECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 326 Y------VEHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQSGDWYKFNDEDIEkme 378
Cdd:cd02667 186 FcdpkcnSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVR--- 261
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1937918211 379 gkklqlgiEEDLAEPSKSQtrkpkcgkgthcsrnAYMLVYR 419
Cdd:cd02667 262 --------EVSLEEVLKSE---------------AYLLFYE 279
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-372 |
7.71e-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: 118.19 E-value: 7.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQVWFlNLELRQALYLC-----------PSTC--SDYTK-GDGIRGGKDYEPQTICEHlqylfall 155
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLF-SIPSFQWRYDDlenkfpsdvvdPANDlnCQLIKlADGLLSGRYSKPASLKSE-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 156 QNSNRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNVVQQQFCgeyayvtvCSQC 226
Cdd:cd02658 72 NDPYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CLSC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 227 GRESKLVSKFYELELNIQGHKQ--------------LTDCISEFLKEERLEgdnrYFCENCQSKQNATRKIRLLSLPCTL 292
Cdd:cd02658 144 KKVKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 293 NLQLMRFVFDrQTGHKKKLNAYIGFSESLDMEPYvehkggsfvyELSAVLIHRGVSAYSGHYIAHVKDPQSGD--WYKFN 370
Cdd:cd02658 220 VINMKRFQLL-ENWVPKKLDVPIDVPEELGPGKY----------ELIAFISHKGTSVHSGHYVAHIKKEIDGEgkWVLFN 288
|
..
gi 1937918211 371 DE 372
Cdd:cd02658 289 DE 290
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
89-371 |
1.53e-19 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 90.41 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCpsTCSDYTKgdgirggkdyEPQTICEhLQYLFALLQNSNRRYIDPSGF 168
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSH--LATECLK----------EHCLLCE-LGFLFDMLEKAKGKNCQASNF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 169 VKALG----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNVVQQQFCGEYAYVTVCSQCGR 228
Cdd:pfam13423 68 LRALSsipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 229 ESKLVSKFYELELN------IQGHKQLTDCISEFLKE--ERlEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFV 300
Cdd:pfam13423 148 ESVRESSTHVLDLIyprkpsSNNKKPPNQTFSSILKSslER-ETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 301 FD-RQTGHKKKlnayiGFSESLDMEPYVEHKG--GSFVYELSAVLIHRGVSAYSGHYIAHVK-------DPQSGDWYKFN 370
Cdd:pfam13423 227 EEwRQLWKTPG-----WLPPEIGLTLSDDLQGdnEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFN 301
|
.
gi 1937918211 371 D 371
Cdd:pfam13423 302 D 302
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
90-377 |
3.09e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 89.09 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKgDGIRggKDYEPQTICEHLqYLFALLQNSNRRYIDPSGfv 169
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLK-NVIR--KPEPDLNQEEAL-KLFTALWSSKEHKVGWIP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 170 kalglDTGQQQDAQEFsklfMSLLEDTLskqKNPDVRnvvqqqfCGEYAYVTVCSQCGRESK------LVSKFYELELNI 243
Cdd:COG5533 75 -----PMGSQEDAHEL----LGKLLDEL---KLDLVN-------SFTIRIFKTTKDKKKTSTgdwfdiIIELPDQTWVNN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 244 QghKQLTDCIS---EFLKEERL--EGDNRYfcENCQSKQNATRKIRllSLPCTLNLQLMRFVFDrqtGHKKKLNAYIGfs 318
Cdd:COG5533 136 L--KTLQEFIDnmeELVDDETGvkAKENEE--LEVQAKQEYEVSFV--KLPKILTIQLKRFANL---GGNQKIDTEVD-- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937918211 319 ESLDMEPYVEHKGG---SFVYELSAVLIHRGvSAYSGHYIAHVKdpQSGDWYKFNDEDIEKM 377
Cdd:COG5533 205 EKFELPVKHDQILNivkETYYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-376 |
4.51e-19 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 87.81 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 90 GLTNLGATCYVNTFLQvwflnlelrqALYLCPStcsdytkgdgirggkdyepqtICEHLQylfallqnsnrRYIdpsgfv 169
Cdd:cd02662 1 GLVNLGNTCFMNSVLQ----------ALASLPS---------------------LIEYLE-----------EFL------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 170 kalgldtgQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnvvqqqFCGEYAYVTVCSQCGRESKL-VSKFYELELNIQGHKQ 248
Cdd:cd02662 33 --------EQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSS 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 249 -----LTDCISEFLKEERLEGdnrYFCENCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNAYIGFSESLDm 323
Cdd:cd02662 93 gsgttLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP- 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937918211 324 epyvehkggSFVYELSAVLIHRGvSAYSGHYIAH------VKDPQSGD--------------WYKFNDEDIEK 376
Cdd:cd02662 160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKE 222
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
249-376 |
5.80e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 89.56 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 249 LTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNAYIGFS-ESLDMEPYV 327
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVE 754
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1937918211 328 EHKGGS-FVYELSAVLIHRGVSAySGHYIAHVKDPQSGDWYKFNDEDIEK 376
Cdd:COG5560 755 YMVDDPrLIYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLFDDSRITE 803
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-375 |
1.19e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 76.38 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIR---GGKDYEP------QTICEHLQYLFALLQNSN 159
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTErriGGREVSRselqrsNQFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 160 RRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNVVQQQFCGEYAYVTVCSQCGRE 229
Cdd:cd02666 82 TRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTKQQLVPESMGNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 230 SKLVSK---FYEL---------ELNIQGHKQ-LTDCISEFLKEERLEGDNRYFCENCQSKQNATRKI---------RLLS 287
Cdd:cd02666 159 PSVRTKterFLSLlvdvgkkgrEIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 288 LPCTLNLQLMRFVFDRQTGHKKKLNAYigfseSLDMEPYVEHKGgSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWY 367
Cdd:cd02666 239 DIDELIREAIQSESSLVRQAQNELAEL-----KHEIEKQFDDLK-SYGYRLHAVFIHRG-EASSGHYWVYIKDFEENVWR 311
|
....*...
gi 1937918211 368 KFNDEDIE 375
Cdd:cd02666 312 KYNDETVT 319
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
178-418 |
9.62e-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: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 178 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVrnvvqQQFCGEYAYVTVCSqcGRESKLVSKFYELELNIQGHK 247
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMV-----QLFYGTFLTEGVLE--GKPFCNCETFGQYPLQVNGYG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 248 QLTDCISEFLKEERLEGDnryfcENCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNAYIGFSESLDMEPyv 327
Cdd:cd02665 94 NLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVP-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 328 ehkggsfvYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEGKKlqlgIEEDlaepsksqtrkpkcGKGT 407
Cdd:cd02665 164 --------YELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEE----VERD--------------SFGG 216
|
250
....*....|.
gi 1937918211 408 HCSRNAYMLVY 418
Cdd:cd02665 217 GRNPSAYCLMY 227
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
173-374 |
2.37e-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: 62.16 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 173 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNVVQQQFCGEYAYVT----VCSQCGRESKLVSKFYELELNIQG 245
Cdd:cd02673 27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 246 HK--QLTDCISEFLKEERLEGDnryfCENCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIgfsesldM 323
Cdd:cd02673 107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937918211 324 EPYvEHKGGSfvYELSAVLIHRGVSAYSGHYIAHVKDPQSGD-WYKFNDEDI 374
Cdd:cd02673 175 KKY-CGTDAK--YSLVAVICHLGESPYDGHYIAYTKELYNGSsWLYCSDDEI 223
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
484-554 |
1.16e-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: 55.84 E-value: 1.16e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937918211 484 EPYEFVSLEWLQKWL----DESTPTKPIDNN--ACLCSHDKLHPDKISIMK--RISEYAADIFYSRYGGGPRLTVKALC 554
Cdd:pfam06337 2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-378 |
1.39e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 51.94 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 86 NSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdytkgdgirgGKDYEPQ-TICEHLQYLFALL----QNSN- 159
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL----------------YENYENIkDRKSELVKRLSELirkiWNPRn 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 160 -RRYIDPSGFVKALGLDTGQ--QQDAQEFSKLFMSLLEDTLSKQ---KNPDVRNVVQQQFCGEyayVTVCSQCGRESKL- 232
Cdd:cd02669 181 fKGHVSPHELLQAVSKVSKKkfSITEQSDPVEFLSWLLNTLHKDlggSKKPNSSIIHDCFQGK---VQIETQKIKPHAEe 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 233 -----------------VSKFYELELNIQG-----HKQLTDCISEFLKEERLegdNRYFCENCQSKQNATRKIRLLSLPC 290
Cdd:cd02669 258 egskdkffkdsrvkktsVSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPK 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 291 TLNLQLMRFvfDRQTGHKKKLNAYIGFS-ESLDMEPYVE---HKGGSFV-YELSAVLIHRGVSAYSGHYIAHVKDPQSGD 365
Cdd:cd02669 335 YLIFHIKRF--SKNNFFKEKNPTIVNFPiKNLDLSDYVHfdkPSLNLSTkYNLVANIVHEGTPQEDGTWRVQLRHKSTNK 412
|
330
....*....|...
gi 1937918211 366 WYKFNDEDIEKME 378
Cdd:cd02669 413 WFEIQDLNVKEVL 425
|
|
| Ubl_ubiquitin_like |
cd17039 |
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
950-1003 |
1.55e-06 |
|
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.
Pssm-ID: 340559 [Multi-domain] Cd Length: 68 Bit Score: 46.44 E-value: 1.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1937918211 950 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1003
Cdd:cd17039 15 VDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK-TLSDYGIKDGSTIHL 67
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
945-1003 |
1.21e-05 |
|
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression
Pssm-ID: 214563 [Multi-domain] Cd Length: 72 Bit Score: 44.17 E-value: 1.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937918211 945 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1003
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
483-556 |
2.70e-05 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 43.50 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 483 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNNACLCSHD--KLHPDKI--SIMKRISEYAADIFYSRYGGGPR-LTVKA 552
Cdd:smart00695 5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84
|
....
gi 1937918211 553 LCKD 556
Cdd:smart00695 85 VCQG 88
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
75-371 |
1.85e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 44.43 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 75 IDDPNCERRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdytkgdgIRGGKDYEPQTICEhLQYLF-A 153
Cdd:cd02672 2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAI-------------ILVACPKESCLLCE-LGYLFsT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 154 LLQNSNRRYIDPSGFvKALGLDTGQQQDAQEFSKLF-MSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCSQCGRESKL 232
Cdd:cd02672 68 LIQNFTRFLLETISQ-DQLGTPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937918211 233 VSKFyelelNIQGhkqLTDCiseflkeerlegDNRYFCENCqSKQNATRKIRLLSLPCTLNLQlmrfvfdrqtghkkklN 312
Cdd:cd02672 147 EQTT-----SIRH---LPDI------------LLLVLVINL-SVTNGEFDDINVVLPSGKVMQ----------------N 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937918211 313 AYIGFSESLDMEPYVEHKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQ----SGDWYKFND 371
Cdd:cd02672 190 KVSPKAIDHDKLVKNRGQESIYKYELVGYVCEINDSSRGQHNVVFVIKVNeestHGRWYLFND 252
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
950-1003 |
1.38e-03 |
|
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.
Pssm-ID: 459726 [Multi-domain] Cd Length: 72 Bit Score: 38.31 E-value: 1.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1937918211 950 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDcATLGTLGVIPESVILL 1003
Cdd:pfam00240 15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDD-QTLGEYGIEDGSTIHL 67
|
|
| Ubl_AtNPL4_like |
cd17055 |
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ... |
938-995 |
5.93e-03 |
|
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins; The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2.
Pssm-ID: 340575 Cd Length: 73 Bit Score: 36.42 E-value: 5.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937918211 938 RHRKvrGEKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGK---ILNDDCATLGTLGV 995
Cdd:cd17055 6 RSRD--GTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLSLDPGpdlLTAKSSATLSQLGL 64
|
|
| |
