|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-447 |
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: 571.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYtkGDGIRGGKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 197
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 198 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNIQGHKQL 277
Cdd:cd02668 79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 278 TDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEPY-VE 356
Cdd:cd02668 159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 357 HKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 436
Cdd:cd02668 239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313
|
330
....*....|.
gi 564353676 437 CSRNAYMLVYR 447
Cdd:cd02668 314 SSRTAYMLVYK 324
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
117-446 |
1.11e-59 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 207.30 E-value: 1.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 117 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIrggkdyepqTICEHLQYLF-ALLQNSNRRYIDPSG 195
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDI---------NLLCALRDLFkALQKNSKSSSVSPKM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 196 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYE 266
Cdd:pfam00443 72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 267 LELNIQGHK------QLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 340
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 341 AYIGFSESLDMEPYV-----EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDIEkmegkklqlgiE 415
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------E 293
|
330 340 350
....*....|....*....|....*....|.
gi 564353676 416 EDLAEPSKSQtrkpkcgkgthcsrNAYMLVY 446
Cdd:pfam00443 294 VDEETAVLSS--------------SAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
100-486 |
9.42e-46 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 179.30 E-value: 9.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 100 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDytkgdgirgGKDyepqTICEHLQYL 179
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPR---------GRD----SVALALQRL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 180 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNVVQQQFCGEYAYVTVCSQCGR 256
Cdd:COG5077 244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 257 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 336
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 337 KKLNAYIGFSESLDMEPYVEH-----KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDI---EKMEGK 408
Cdd:COG5077 399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 409 KLQLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTQEkNHTM-----VQVPAFLQELVDRDNSKFEEWCVEMA 483
Cdd:COG5077 478 EENFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSML-DDLLnpvaaVDIPPHVEEVLSEEIDKTEVRCKEID 549
|
...
gi 564353676 484 EMR 486
Cdd:COG5077 550 EIH 552
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
968-1063 |
3.33e-40 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.
Pssm-ID: 340493 [Multi-domain] Cd Length: 99 Bit Score: 143.58 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 968 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1044
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
|
90
....*....|....*....
gi 564353676 1045 DVMQVCMPEEGFKGTGLLG 1063
Cdd:cd01795 81 DVSRARVPEEGFKGTALLG 99
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
512-582 |
9.89e-10 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 55.84 E-value: 9.89e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564353676 512 EPYEFVSLEWLQKWL----DESTPTKPIDNN--ACLCSHDKLHPDKISIMK--RISEYAADIFYSRYGGGPRLTVKALC 582
Cdd:pfam06337 2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
973-1031 |
1.13e-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: 1.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 564353676 973 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1031
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
511-584 |
2.40e-05 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 43.89 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 511 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNNACLCSHD--KLHPDKI--SIMKRISEYAADIFYSRYGGGPR-LTVKA 580
Cdd:smart00695 5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84
|
....
gi 564353676 581 LCKD 584
Cdd:smart00695 85 VCQG 88
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
978-1031 |
1.18e-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: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 564353676 978 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDcATLGTLGVIPESVILL 1031
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 ... |
118-447 |
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: 571.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYtkGDGIRGGKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 197
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 198 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNIQGHKQL 277
Cdd:cd02668 79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 278 TDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEPY-VE 356
Cdd:cd02668 159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 357 HKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 436
Cdd:cd02668 239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313
|
330
....*....|.
gi 564353676 437 CSRNAYMLVYR 447
Cdd:cd02668 314 SSRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-447 |
2.39e-79 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 262.96 E-value: 2.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 116 FVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdytkgdgirGGKDYEPQTICeHLQYLFALLQNSNRRYIDPSG 195
Cdd:cd02659 2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-----------EDDDDNKSVPL-ALQRLFLFLQLSESPVKTTEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 196 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELN 270
Cdd:cd02659 70 TDKTRSfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 271 IQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLD 350
Cdd:cd02659 147 VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 351 MEPYVEH------------KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDIEKM---EGKKLQLGIE 415
Cdd:cd02659 227 MEPYTEKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGE 305
|
330 340 350
....*....|....*....|....*....|..
gi 564353676 416 EDLAEPSKSQTRKPKCGkgthcsrNAYMLVYR 447
Cdd:cd02659 306 ETQKTYDSGPRAFKRTT-------NAYMLFYE 330
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
117-446 |
1.11e-59 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 207.30 E-value: 1.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 117 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIrggkdyepqTICEHLQYLF-ALLQNSNRRYIDPSG 195
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDI---------NLLCALRDLFkALQKNSKSSSVSPKM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 196 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYE 266
Cdd:pfam00443 72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 267 LELNIQGHK------QLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 340
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 341 AYIGFSESLDMEPYV-----EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDIEkmegkklqlgiE 415
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------E 293
|
330 340 350
....*....|....*....|....*....|.
gi 564353676 416 EDLAEPSKSQtrkpkcgkgthcsrNAYMLVY 446
Cdd:pfam00443 294 VDEETAVLSS--------------SAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
118-447 |
1.63e-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: 198.86 E-value: 1.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNtflqvwflnlelrqalylcpSTcsdytkgdgirggkdyepqticehLQYLFAllqnsnrryidpsgfv 197
Cdd:cd02257 1 GLNNLGNTCYLN--------------------SV------------------------LQALFS---------------- 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 198 kalgldtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNIQ 272
Cdd:cd02257 21 --------EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 273 GHKQ----LTDCISEFLKEERLEGDNRYFCEnCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNAYIGFSES 348
Cdd:cd02257 93 VKGLpqvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 349 LDMEPYVEHKG-------GSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEgkklqlgiEEDLAEP 421
Cdd:cd02257 171 LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVLEF 242
|
330 340
....*....|....*....|....*.
gi 564353676 422 SKSqtrkpkcgkgthcSRNAYMLVYR 447
Cdd:cd02257 243 GSL-------------SSSAYILFYE 255
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
100-486 |
9.42e-46 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 179.30 E-value: 9.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 100 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDytkgdgirgGKDyepqTICEHLQYL 179
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPR---------GRD----SVALALQRL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 180 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNVVQQQFCGEYAYVTVCSQCGR 256
Cdd:COG5077 244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 257 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 336
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 337 KKLNAYIGFSESLDMEPYVEH-----KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDI---EKMEGK 408
Cdd:COG5077 399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 409 KLQLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTQEkNHTM-----VQVPAFLQELVDRDNSKFEEWCVEMA 483
Cdd:COG5077 478 EENFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSML-DDLLnpvaaVDIPPHVEEVLSEEIDKTEVRCKEID 549
|
...
gi 564353676 484 EMR 486
Cdd:COG5077 550 EIH 552
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-447 |
6.78e-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: 6.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 206 QQQDAQEFsklfMSLLEDTLskqknpdvRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNI-----QGHKQ-LTD 279
Cdd:cd02674 21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 280 CISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHKKKLNAYIGFS-ESLDMEPYV--E 356
Cdd:cd02674 89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPlNDLDLTPYVdtR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 357 HKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEgkklqlgieedlaepsksqtrkpkcgKGTH 436
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS--------------------------ESSV 219
|
250
....*....|.
gi 564353676 437 CSRNAYMLVYR 447
Cdd:cd02674 220 VSSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-399 |
1.63e-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: 1.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQvwflnlelrqalylcpstCSDYTK--------GDGIRGGKDYEPQTICEHLQYLFALLQNSnRR 189
Cdd:cd02661 3 GLQNLGNTCFLNSVLQ------------------CLTHTPplanyllsREHSKDCCNEGFCMMCALEAHVERALASS-GP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 190 YIDPSGFVKAL-----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NVVQQQFCGEYAYVTVCSQCGR 256
Cdd:cd02661 64 GSAPRIFSSNLkqiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 257 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHk 336
Cdd:cd02661 144 VSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG- 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564353676 337 kKLNAYIGFSESLDMEPYV-EHKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPqSGDWYKFND 399
Cdd:cd02661 221 -KINKQISFPETLDLSPYMsQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDD 282
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
968-1063 |
3.33e-40 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.
Pssm-ID: 340493 [Multi-domain] Cd Length: 99 Bit Score: 143.58 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 968 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1044
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
|
90
....*....|....*....
gi 564353676 1045 DVMQVCMPEEGFKGTGLLG 1063
Cdd:cd01795 81 DVSRARVPEEGFKGTALLG 99
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-399 |
4.35e-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: 151.49 E-value: 4.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQvwflnlelrqALYLCPSTCSDYTKGDGIRGGKDyepQTICEHLQYLFALLQNSNRRYIDP-SGF 196
Cdd:cd02664 1 GLINLGNTCYMNSVLQ----------ALFMAKDFRRQVLSLNLPRLGDS---QSVMKKLQLLQAHLMHTQRRAEAPpDYF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 197 VKAL---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrnvVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNIqg 273
Cdd:cd02664 68 LEASrppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 274 hKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEP 353
Cdd:cd02664 134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 354 YVEHKGGSFV--------------------YELSAVLIHRGVSAYSGHYIAHVKDP--------------------QSGD 393
Cdd:cd02664 213 RVESKSSESPlekkeeesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQtdadstgqecpepkdaeendESKN 292
|
....*.
gi 564353676 394 WYKFND 399
Cdd:cd02664 293 WYLFND 298
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-407 |
4.79e-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: 139.00 E-value: 4.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcSDYTkgdGIRGGKDYEPQTICEHLQYLFALLQNSNRRyIDPSGFV 197
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-------KNYN---PARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 198 KALGL---------DTGQ--QQDAQE-FSKLFMSLledTLSKQKNPDVRNVVQQQFCGEYAYVTVCS-QCGRESKLVSKF 264
Cdd:cd02657 70 QLLRMafpqfaekqNQGGyaQQDAEEcWSQLLSVL---SQKLPGAGSKGSFIDQLFGIELETKMKCTeSPDEEEVSTESE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 265 YELELNIqGHKQLTDCISEFLKEeRLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIG 344
Cdd:cd02657 147 YKLQCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564353676 345 FSESLDMEPYVEHKGgsfVYELSAVLIHRGVSAYSGHYIAHVKDPQSGDWYKFND--------EDIEKMEG 407
Cdd:cd02657 225 FPFELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-399 |
3.63e-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: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQVwFLNLELRQALYLcpstcSD-YTKGDGIRGGKDyepqTICEHLQYLFA-LLQNSNRRyidPSG 195
Cdd:cd02660 2 GLINLGATCFMNVILQA-LLHNPLLRNYFL-----SDrHSCTCLSCSPNS----CLSCAMDEIFQeFYYSGDRS---PYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 196 FVKAL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNVVQQQFCGEYAYVTVCSQCGRESK 259
Cdd:cd02660 69 PINLLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVST 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 260 LVSKFYELELNIQGHKQ---------------LTDCISEFLKEERLeGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQL 324
Cdd:cd02660 146 TVDPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 325 MRFVFDrQTGHKKKLNAYIGFSESLDMEPYV----------EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDpQSGDW 394
Cdd:cd02660 225 KRFEHS-LNKTSRKIDTYVQFPLELNMTPYTsssigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQW 301
|
....*
gi 564353676 395 YKFND 399
Cdd:cd02660 302 FKFDD 306
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-446 |
4.13e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 135.90 E-value: 4.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQVWFLNlelrqALYLCpstcsdytkgdgirggkdyepqticehLQYLFALLQNSNRRY--IDPSG 195
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFE-----NLLTC---------------------------LKDLFESISEQKKRTgvISPKK 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 196 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNVVQQQFCGEYAYVTVCSQCGR 256
Cdd:cd02663 49 FITRLKrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCET 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 257 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 336
Cdd:cd02663 129 VSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 337 KKLNAYIGFSESL------DMEPYVEHKggsfvYELSAVLIHRGVSAYSGHYIAHVKdpQSGDWYKFNDEDIEKMEGKKL 410
Cdd:cd02663 209 IKLFYRVVFPLELrlfnttDDAENPDRL-----YELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAV 281
|
330 340 350
....*....|....*....|....*....|....*.
gi 564353676 411 qlgieEDLAEPSKSQTrkpkcgkgthcsrNAYMLVY 446
Cdd:cd02663 282 -----EEFFGDSPNQA-------------TAYVLFY 299
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
106-429 |
3.98e-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: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 106 PNCERRKKN--SFVGLTNLGATCYVNTFLQVwflnlelrqaLYLCPSTCSDYTKGDGIRGGKdyepqticEHLQYLFALL 183
Cdd:cd02671 12 ATSCEKRENllPFVGLNNLGNTCYLNSVLQV----------LYFCPGFKHGLKHLVSLISSV--------EQLQSSFLLN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 184 Q---NSNRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNVVQQQFCGEYAYVTVCSQCG 255
Cdd:cd02671 74 PekyNDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLECE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 256 ----------------RESKLVSKFYELELNIQGH---KQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSL 316
Cdd:cd02671 142 tfterredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 317 PCTLNLQLMRF----VFDRQTGHKKKLNAYIGFSESLDMEPYVEhKGGSFVYELSAVLIHRGVSAYSGHYIAHVKdpqsg 392
Cdd:cd02671 222 PEVITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR----- 295
|
330 340 350
....*....|....*....|....*....|....*..
gi 564353676 393 dWYKFNDEDIEKMEGKKLqlgieEDLAEPSKSQTRKP 429
Cdd:cd02671 296 -WLLFDDSEVKVTEEKDF-----LEALSPNTSSTSTP 326
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-447 |
5.56e-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: 5.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdytkgdgirggkdyepqticehlqyLFALLQNSNRRYIDpsgfv 197
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE---------------------------LFSQVCRKAPQFKG----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 198 kalgldtGQQQDAQEFSKLfmsLLEDtlskqknpdVRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELEL----NIQG 273
Cdd:cd02667 49 -------YQQQDSHELLRY---LLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 274 HKQLTDCISEFLKEERLEGDNRYFCENCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNAYIGFSESLDMEP 353
Cdd:cd02667 110 ECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 354 Y------VEHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQSGDWYKFNDEDIEkme 406
Cdd:cd02667 186 FcdpkcnSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVR--- 261
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 564353676 407 gkklqlgiEEDLAEPSKSQtrkpkcgkgthcsrnAYMLVYR 447
Cdd:cd02667 262 --------EVSLEEVLKSE---------------AYLLFYE 279
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-400 |
7.12e-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: 7.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQVWFlNLELRQALYLC-----------PSTC--SDYTK-GDGIRGGKDYEPQTICEHlqylfall 183
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLF-SIPSFQWRYDDlenkfpsdvvdPANDlnCQLIKlADGLLSGRYSKPASLKSE-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 184 QNSNRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNVVQQQFCgeyayvtvCSQC 254
Cdd:cd02658 72 NDPYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CLSC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 255 GRESKLVSKFYELELNIQGHKQ--------------LTDCISEFLKEERLEgdnrYFCENCQSKQNATRKIRLLSLPCTL 320
Cdd:cd02658 144 KKVKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 321 NLQLMRFVFDrQTGHKKKLNAYIGFSESLDMEPYvehkggsfvyELSAVLIHRGVSAYSGHYIAHVKDPQSGD--WYKFN 398
Cdd:cd02658 220 VINMKRFQLL-ENWVPKKLDVPIDVPEELGPGKY----------ELIAFISHKGTSVHSGHYVAHIKKEIDGEgkWVLFN 288
|
..
gi 564353676 399 DE 400
Cdd:cd02658 289 DE 290
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
117-399 |
1.44e-19 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 90.79 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 117 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCpsTCSDYTKgdgirggkdyEPQTICEhLQYLFALLQNSNRRYIDPSGF 196
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSH--LATECLK----------EHCLLCE-LGFLFDMLEKAKGKNCQASNF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 197 VKALG----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNVVQQQFCGEYAYVTVCSQCGR 256
Cdd:pfam13423 68 LRALSsipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 257 ESKLVSKFYELELN------IQGHKQLTDCISEFLKE--ERlEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFV 328
Cdd:pfam13423 148 ESVRESSTHVLDLIyprkpsSNNKKPPNQTFSSILKSslER-ETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 329 FD-RQTGHKKKlnayiGFSESLDMEPYVEHKG--GSFVYELSAVLIHRGVSAYSGHYIAHVK-------DPQSGDWYKFN 398
Cdd:pfam13423 227 EEwRQLWKTPG-----WLPPEIGLTLSDDLQGdnEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFN 301
|
.
gi 564353676 399 D 399
Cdd:pfam13423 302 D 302
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
118-405 |
1.68e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 89.86 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKgDGIRggKDYEPQTICEHLqYLFALLQNSNRRYIDPSGfv 197
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLK-NVIR--KPEPDLNQEEAL-KLFTALWSSKEHKVGWIP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 198 kalglDTGQQQDAQEFsklfMSLLEDTLskqKNPDVRnvvqqqfCGEYAYVTVCSQCGRESK------LVSKFYELELNI 271
Cdd:COG5533 75 -----PMGSQEDAHEL----LGKLLDEL---KLDLVN-------SFTIRIFKTTKDKKKTSTgdwfdiIIELPDQTWVNN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 272 QghKQLTDCIS---EFLKEERL--EGDNRYfcENCQSKQNATRKIRllSLPCTLNLQLMRFVFDrqtGHKKKLNAYIGfs 346
Cdd:COG5533 136 L--KTLQEFIDnmeELVDDETGvkAKENEE--LEVQAKQEYEVSFV--KLPKILTIQLKRFANL---GGNQKIDTEVD-- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564353676 347 ESLDMEPYVEHKGG---SFVYELSAVLIHRGvSAYSGHYIAHVKdpQSGDWYKFNDEDIEKM 405
Cdd:COG5533 205 EKFELPVKHDQILNivkETYYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-404 |
4.23e-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: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 118 GLTNLGATCYVNTFLQvwflnlelrqALYLCPStcsdytkgdgirggkdyepqtICEHLQylfallqnsnrRYIdpsgfv 197
Cdd:cd02662 1 GLVNLGNTCFMNSVLQ----------ALASLPS---------------------LIEYLE-----------EFL------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 198 kalgldtgQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnvvqqqFCGEYAYVTVCSQCGRESKL-VSKFYELELNIQGHKQ 276
Cdd:cd02662 33 --------EQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSS 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 277 -----LTDCISEFLKEERLEGdnrYFCENCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNAYIGFSESLDm 351
Cdd:cd02662 93 gsgttLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP- 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564353676 352 epyvehkggSFVYELSAVLIHRGvSAYSGHYIAH------VKDPQSGD--------------WYKFNDEDIEK 404
Cdd:cd02662 160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKE 222
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
277-404 |
5.22e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 89.56 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 277 LTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNAYIGFS-ESLDMEPYV 355
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVE 754
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 564353676 356 EHKGGS-FVYELSAVLIHRGVSAySGHYIAHVKDPQSGDWYKFNDEDIEK 404
Cdd:COG5560 755 YMVDDPrLIYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLFDDSRITE 803
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
117-403 |
6.84e-15 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 77.15 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 117 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIR---GGKDYEP------QTICEHLQYLFALLQNSN 187
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTErriGGREVSRselqrsNQFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 188 RRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNVVQQQFCGEYAYVTVCSQCGRE 257
Cdd:cd02666 82 TRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTKQQLVPESMGNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 258 SKLVSK---FYEL---------ELNIQGHKQ-LTDCISEFLKEERLEGDNRYFCENCQSKQNATRKI---------RLLS 315
Cdd:cd02666 159 PSVRTKterFLSLlvdvgkkgrEIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 316 LPCTLNLQLMRFVFDRQTGHKKKLNAYigfseSLDMEPYVEHKGgSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWY 395
Cdd:cd02666 239 DIDELIREAIQSESSLVRQAQNELAEL-----KHEIEKQFDDLK-SYGYRLHAVFIHRG-EASSGHYWVYIKDFEENVWR 311
|
....*...
gi 564353676 396 KFNDEDIE 403
Cdd:cd02666 312 KYNDETVT 319
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-446 |
7.70e-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: 69.12 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 206 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVrnvvqQQFCGEYAYVTVCSqcGRESKLVSKFYELELNIQGHK 275
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMV-----QLFYGTFLTEGVLE--GKPFCNCETFGQYPLQVNGYG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 276 QLTDCISEFLKEERLEGDnryfcENCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNAYIGFSESLDMEPyv 355
Cdd:cd02665 94 NLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVP-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 356 ehkggsfvYELSAVLIHRGvSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEGKKlqlgIEEDlaepsksqtrkpkcGKGT 435
Cdd:cd02665 164 --------YELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEE----VERD--------------SFGG 216
|
250
....*....|.
gi 564353676 436 HCSRNAYMLVY 446
Cdd:cd02665 217 GRNPSAYCLMY 227
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
201-402 |
2.36e-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: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 201 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNVVQQQFCGEYAYVT----VCSQCGRESKLVSKFYELELNIQG 273
Cdd:cd02673 27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 274 HK--QLTDCISEFLKEERLEGDnryfCENCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIgfsesldM 351
Cdd:cd02673 107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564353676 352 EPYvEHKGGSfvYELSAVLIHRGVSAYSGHYIAHVKDPQSGD-WYKFNDEDI 402
Cdd:cd02673 175 KKY-CGTDAK--YSLVAVICHLGESPYDGHYIAYTKELYNGSsWLYCSDDEI 223
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
512-582 |
9.89e-10 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 55.84 E-value: 9.89e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564353676 512 EPYEFVSLEWLQKWL----DESTPTKPIDNN--ACLCSHDKLHPDKISIMK--RISEYAADIFYSRYGGGPRLTVKALC 582
Cdd:pfam06337 2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
114-406 |
1.14e-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: 52.32 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 114 NSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdytkgdgirgGKDYEPQ-TICEHLQYLFALLQ----NSN- 187
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL----------------YENYENIkDRKSELVKRLSELIrkiwNPRn 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 188 -RRYIDPSGFVKALGLDTGQ--QQDAQEFSKLFMSLLEDTLSKQ---KNPDVRNVVQQQFCGEyayVTVCSQCGRESKL- 260
Cdd:cd02669 181 fKGHVSPHELLQAVSKVSKKkfSITEQSDPVEFLSWLLNTLHKDlggSKKPNSSIIHDCFQGK---VQIETQKIKPHAEe 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 261 -----------------VSKFYELELNIQG-----HKQLTDCISEFLKEERLegdNRYFCENCQSKQNATRKIRLLSLPC 318
Cdd:cd02669 258 egskdkffkdsrvkktsVSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPK 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 319 TLNLQLMRFvfDRQTGHKKKLNAYIGFS-ESLDMEPYVE---HKGGSFV-YELSAVLIHRGVSAYSGHYIAHVKDPQSGD 393
Cdd:cd02669 335 YLIFHIKRF--SKNNFFKEKNPTIVNFPiKNLDLSDYVHfdkPSLNLSTkYNLVANIVHEGTPQEDGTWRVQLRHKSTNK 412
|
330
....*....|...
gi 564353676 394 WYKFNDEDIEKME 406
Cdd:cd02669 413 WFEIQDLNVKEVL 425
|
|
| Ubl_ubiquitin_like |
cd17039 |
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
978-1031 |
1.33e-06 |
|
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.
Pssm-ID: 340559 [Multi-domain] Cd Length: 68 Bit Score: 46.82 E-value: 1.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 564353676 978 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1031
Cdd:cd17039 15 VDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK-TLSDYGIKDGSTIHL 67
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
973-1031 |
1.13e-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: 1.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 564353676 973 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1031
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
511-584 |
2.40e-05 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 43.89 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 511 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNNACLCSHD--KLHPDKI--SIMKRISEYAADIFYSRYGGGPR-LTVKA 580
Cdd:smart00695 5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84
|
....
gi 564353676 581 LCKD 584
Cdd:smart00695 85 VCQG 88
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
103-399 |
1.73e-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: 44.81 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 103 IDDPNCERRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdytkgdgIRGGKDYEPQTICEhLQYLF-A 181
Cdd:cd02672 2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAI-------------ILVACPKESCLLCE-LGYLFsT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 182 LLQNSNRRYIDPSGFvKALGLDTGQQQDAQEFSKLF-MSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCSQCGRESKL 260
Cdd:cd02672 68 LIQNFTRFLLETISQ-DQLGTPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564353676 261 VSKFyelelNIQGhkqLTDCiseflkeerlegDNRYFCENCqSKQNATRKIRLLSLPCTLNLQlmrfvfdrqtghkkklN 340
Cdd:cd02672 147 EQTT-----SIRH---LPDI------------LLLVLVINL-SVTNGEFDDINVVLPSGKVMQ----------------N 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564353676 341 AYIGFSESLDMEPYVEHKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQ----SGDWYKFND 399
Cdd:cd02672 190 KVSPKAIDHDKLVKNRGQESIYKYELVGYVCEINDSSRGQHNVVFVIKVNeestHGRWYLFND 252
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
978-1031 |
1.18e-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: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 564353676 978 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDcATLGTLGVIPESVILL 1031
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, ... |
966-1023 |
6.09e-03 |
|
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins; The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2.
Pssm-ID: 340575 Cd Length: 73 Bit Score: 36.42 E-value: 6.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564353676 966 RHRKvrGEKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGK---ILNDDCATLGTLGV 1023
Cdd:cd17055 6 RSRD--GTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLSLDPGpdlLTAKSSATLSQLGL 64
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