|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
6-409 |
7.36e-164 |
|
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: 463.65 E-value: 7.36e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 6 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIegtgsdvdddmsgdekqdnesnvdprddvfgypqqfedkpalsKTE 85
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 86 DRAAYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVL 165
Cdd:cd02659 38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 166 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 245
Cdd:cd02659 118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 246 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDnvnpesqliqqseqSESETAGSTKYRLVGVLVHSGQ 325
Cdd:cd02659 198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGD--------------SEKKDSESYIYELHGVLVHSGD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 326 ASGGHYYSYIIQRNGGdgernRWYKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 405
Cdd:cd02659 264 AHGGHYYSYIKDRDDG-----KWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330
|
....
gi 1418639693 406 RMDT 409
Cdd:cd02659 331 RKSP 334
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
8-404 |
4.48e-86 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 264.69 E-value: 4.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 8 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDekqdnesnvdprddvfgypqqfedkpalsktedr 87
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 88 aaynigVLRHLQVIFGHLA-ASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKA---LGHPAMLSK 163
Cdd:pfam00443 47 ------LLCALRDLFKALQkNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 164 VLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLL------DSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 237
Cdd:pfam00443 121 LFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 238 KKLPPVLAIQLKRFDYDweRECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVnpesqliqqseqsesetagstKYRLV 317
Cdd:pfam00443 201 SRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ---------------------DYRLV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 318 GVLVHSGQASGGHYYSYIIQrnggdGERNRWYKFDDGDVTECKMDDDEEMknqcfggeymgevfdhmmkrmsyrrqkrwW 397
Cdd:pfam00443 258 AVVVHSGSLSSGHYIAYIKA-----YENNRWYKFDDEKVTEVDEETAVLS-----------------------------S 303
|
....*..
gi 1418639693 398 NAYILFY 404
Cdd:pfam00443 304 SAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
131-405 |
1.95e-58 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 191.54 E-value: 1.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 131 LREQHDALEFFNSLVDSLDEALKALG--------HPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI----RNH 198
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSkrtsdsssLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 199 QNLLDSLEQYVKGDLLEGANAYHCEKCnKKVDTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPY 278
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 279 TVAGVAKLEGDNvnpesqliqqseqsesetaGSTKYRLVGVLVHSGQ-ASGGHYYSYIIqrnggDGERNRWYKFDDGDVT 357
Cdd:cd02257 177 LSEGEKDSDSDN-------------------GSYKYELVAVVVHSGTsADSGHYVAYVK-----DPSDGKWYKFNDDKVT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1418639693 358 ECKMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkRWWNAYILFYE 405
Cdd:cd02257 233 EVSEEEVLEFGS-------------------------LSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
9-405 |
1.79e-55 |
|
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: 186.09 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 9 GLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDekQDNESNvdprddvfgypqqfedkpalsktedra 88
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPD--KPHEPQ--------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 89 ayniGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLwgepvNLREQHDALEFFNSLVDSLDEALKALGHP---AMLSKVL 165
Cdd:cd02668 52 ----TIIDQLQLIFAQLQFGNRSVVDPSGFVKALGL-----DTGQQQDAQEFSKLFLSLLEAKLSKSKNPdlkNIVQDLF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 166 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 245
Cdd:cd02668 123 RGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 246 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVagvaklegdnvnpesqliqqsEQSEsetaGSTKYRLVGVLVHSGQ 325
Cdd:cd02668 203 FQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA---------------------ESDE----GSYVYELSGVLIHQGV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 326 -ASGGHYYSYIiqrngGDGERNRWYKFDDGDVTE-----CKMDDDEEMKNQCFGgeymgevfDHMMKRMSYRrqkrwwNA 399
Cdd:cd02668 258 sAYSGHYIAHI-----KDEQTGEWYKFNDEDVEEmpgkpLKLGNSEDPAKPRKS--------EIKKGTHSSR------TA 318
|
....*.
gi 1418639693 400 YILFYE 405
Cdd:cd02668 319 YMLVYK 324
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
6-421 |
3.82e-50 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 182.38 E-value: 3.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 6 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEgtgsdvdddmsgdekQDNEsnvDPRDDVfGYPQQfedkpalskte 85
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP---------------TDHP---RGRDSV-ALALQ----------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 86 dRAAYNIGVLRHlqvifghlAASRLQYYVPRGfwkqfrlWGEPVNLReQHDALEFFNSLVDSLDEALKALGHPAMLSKVL 165
Cdd:COG5077 242 -RLFYNLQTGEE--------PVDTTELTRSFG-------WDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVENALNGIF 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 166 GGSFadqKICQGCPHR-YECE--ESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKcNKKVDTVKRLLIKKLPP 242
Cdd:COG5077 305 VGKM---KSYIKCVNVnYESArvEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPP 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 243 VLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYtvagvaklegdnvnpesqLIQQSEQSESETAgstKYRLVGVLVH 322
Cdd:COG5077 381 VLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF------------------LDRDADKSENSDA---VYVLYGVLVH 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 323 SGQASGGHYYSYIiqRNGGDGernRWYKFDDGDVTECKMdddEEMKNQCFGGEYMGEVfdhmmKRMSYRRQKRWWNAYIL 402
Cdd:COG5077 440 SGDLHEGHYYALL--KPEKDG---RWYKFDDTRVTRATE---KEVLEENFGGDHPYKD-----KIRDHSGIKRFMSAYML 506
|
410
....*....|....*....
gi 1418639693 403 FYERMdtiDQDDELIRYIS 421
Cdd:COG5077 507 VYLRK---SMLDDLLNPVA 522
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
9-363 |
6.58e-47 |
|
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: 163.22 E-value: 6.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 9 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNvdprddvfgypqqfedkpalsktedra 88
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLL-------------SREHSKDCCNE--------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 89 ayNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEA-------LKALGHPA-- 159
Cdd:cd02661 43 --GFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKAcldrfkkLKAVDPSSqe 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 160 --MLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 237
Cdd:cd02661 121 ttLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 238 KKLPPVLAIQLKRFDYDWERecaiKFNDYFEFPRELDMEPYTVagvaklegdnvnpesqliqqseqseSETAGSTKYRLV 317
Cdd:cd02661 201 HRAPNVLTIHLKRFSNFRGG----KINKQISFPETLDLSPYMS-------------------------QPNDGPLKYKLY 251
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1418639693 318 GVLVHSG-QASGGHYYSYIIQRNGgdgernRWYKFDDGDVTECKMDD 363
Cdd:cd02661 252 AVLVHSGfSPHSGHYYCYVKSSNG------KWYNMDDSKVSPVSIET 292
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
133-405 |
2.08e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 143.58 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 133 EQHDALEFFNSLVDSLDealkalghpAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI------RNHQNLLDSLE 206
Cdd:cd02674 21 DQQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 207 QYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYTVAgvak 285
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPlNDLDLTPYVDT---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 286 legdnvnpesqliqqseqseSETAGSTKYRLVGVLVHSGQASGGHYYSYIiqrngGDGERNRWYKFDDGDVTecKMDDDE 365
Cdd:cd02674 166 --------------------RSFTGPFKYDLYAVVNHYGSLNGGHYTAYC-----KNNETNDWYKFDDSRVT--KVSESS 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1418639693 366 EMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYE 405
Cdd:cd02674 219 VVSS----------------------------SAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
9-358 |
7.02e-38 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 139.82 E-value: 7.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 9 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgSDvDDDMSGDEKQDNESNVDPRDDVFgypQQFedkpalSKTEDRA 88
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL------SD-RHSCTCLSCSPNSCLSCAMDEIF---QEF------YYSGDRS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 89 AYnigvlrhlqvifghlAASRLQYyvprGFWKQFRlwgepvNL--REQHDALEFFNSLVDSLDE-ALKALGHPAMLS--- 162
Cdd:cd02660 66 PY---------------GPINLLY----LSWKHSR------NLagYSQQDAHEFFQFLLDQLHThYGGDKNEANDEShcn 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 163 ----KVLGGSFADQKICQGCPHRYECEESFTTLNVDIRN---------------HQNLLDSLEQYVKGDLLeGANAYHCE 223
Cdd:cd02660 121 ciihQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNkstpswalgesgvsgTPTLSDCLDRFTRPEKL-GDFAYKCS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 224 KCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTVAGvaklegdnvnpesqliQQSEQ 303
Cdd:cd02660 200 GCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTSSS----------------IGDTQ 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1418639693 304 SESETAGSTKYRLVGVLVHSGQASGGHYYSYIIQRNGgdgernRWYKFDDGDVTE 358
Cdd:cd02660 263 DSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDG------QWFKFDDAMITR 311
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
9-405 |
8.32e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 131.46 E-value: 8.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 9 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNVdprddvfgypqqfedkpalsktedra 88
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVL-------------SLNLPRLGDSQS-------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 89 aynigVLRHLQVIFGHLAASRLQYY-VPRGFWKQfrLWGEPVNLREQHDALEFFNSLVDSLDealkalghpAMLSKVLGG 167
Cdd:cd02664 42 -----VMKKLQLLQAHLMHTQRRAEaPPDYFLEA--SRPPWFTPGSQQDCSEYLRYLLDRLH---------TLIEKMFGG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 168 SFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDsleQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQ 247
Cdd:cd02664 106 KLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDLLN---YFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 248 LKRFDYDWERECAIKFNDYFEFPRELDMePYTVAgvaklegdNVNPESQLIQQSEQSESETAGSTK---YRLVGVLVHSG 324
Cdd:cd02664 183 LLRFSYDQKTHVREKIMDNVSINEVLSL-PVRVE--------SKSSESPLEKKEEESGDDGELVTRqvhYRLYAVVVHSG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 325 QAS-GGHYYSYIIQRNGGDG---------------ERNRWYKFDDGDVTECKMdddEEMKNqcfggeyMGEVFDHMmkrm 388
Cdd:cd02664 254 YSSeSGHYFTYARDQTDADStgqecpepkdaeendESKNWYLFNDSRVTFSSF---ESVQN-------VTSRFPKD---- 319
|
410
....*....|....*..
gi 1418639693 389 syrrqkrwwNAYILFYE 405
Cdd:cd02664 320 ---------TPYILFYE 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
134-405 |
8.00e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 116.72 E-value: 8.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 134 QHDALEFFNSLVDSLDEALKalghpamlsKVLGGSFADQKICQGCPHRYECEESFTTLN----VDIRNHQNLLDSLEQYV 209
Cdd:cd02667 51 QQDSHELLRYLLDGLRTFID---------SIFGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKSECSIESCLKQFT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 210 KGDLLEGANAYHCEKCNKkvdTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTvagvaklegd 289
Cdd:cd02667 122 EVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFC---------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 290 nvnpesqliqQSEQSESETAGSTKYRLVGVLVHSGQASGGHYYSYI----------------IQRNGGDGERNRWYKFDD 353
Cdd:cd02667 188 ----------DPKCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVkvrppqqrlsdltkskPAADEAGPGSGQWYYISD 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1418639693 354 GDVTEckMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrwwnAYILFYE 405
Cdd:cd02667 258 SDVRE--VSLEEVLKSE----------------------------AYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
134-405 |
1.72e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 113.56 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 134 QHDALEFFNSLVDSLDEALKALG-----------------HPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIR 196
Cdd:cd02663 65 HQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 197 NHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDME 276
Cdd:cd02663 145 QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 277 PYTvagvakleGDNVNPESqliqqseqsesetagstKYRLVGVLVHSGQ-ASGGHYYSyIIQRNGGdgernrWYKFDDGD 355
Cdd:cd02663 225 NTT--------DDAENPDR-----------------LYELVAVVVHIGGgPNHGHYVS-IVKSHGG------WLLFDDET 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1418639693 356 VTecKMDDdeemknqcfggEYMGEVFDHmmkrmsyrrQKRWWNAYILFYE 405
Cdd:cd02663 273 VE--KIDE-----------NAVEEFFGD---------SPNQATAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
9-405 |
7.75e-22 |
|
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: 95.09 E-value: 7.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 9 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvddDMSGDEKQDNESNVDPrddVFGYPQQFEDkpaLSKTEDRa 88
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALK-----------NYNPARRGANQSSDNL---TNALRDLFDT---MDKKQEP- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 89 aynigvlrhlqvifghlaasrlqyYVPRGFWKQFRL----WGEP--VNLREQHDALEFFNSLVDSLDEALK-ALGHPAML 161
Cdd:cd02657 63 ------------------------VPPIEFLQLLRMafpqFAEKqnQGGYAQQDAEECWSQLLSVLSQKLPgAGSKGSFI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 162 SKVLGGSFADQKICQGCPHRYECE-ESFTTLNVDIrNHQNLLDSLEQYVKgDLLEGANAYHCEKCNKKVDTVKRLLIKKL 240
Cdd:cd02657 119 DQLFGIELETKMKCTESPDEEEVStESEYKLQCHI-SITTEVNYLQDGLK-KGLEEEIEKHSPTLGRDAIYTKTSRISRL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 241 PPVLAIQLKRFDydWERECAI--KFNDYFEFPRELDMEPYTvagvaklegdnvnpesqliqqseqsesetAGSTKYRLVG 318
Cdd:cd02657 197 PKYLTVQFVRFF--WKRDIQKkaKILRKVKFPFELDLYELC-----------------------------TPSGYYELVA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 319 VLVHSGQ-ASGGHYYSYIIQRNggdgeRNRWYKFDDGDVTECKMDDDEEMKNqcfGGEYmgevfdHMmkrmsyrrqkrww 397
Cdd:cd02657 246 VITHQGRsADSGHYVAWVRRKN-----DGKWIKFDDDKVSEVTEEDILKLSG---GGDW------HI------------- 298
|
....*...
gi 1418639693 398 nAYILFYE 405
Cdd:cd02657 299 -AYILLYK 305
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
7-371 |
2.89e-18 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 85.33 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 7 FVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSgdekqdnesnvdprddvfgypqQFEDKPALSKTED 86
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQS----------------------SFLLNPEKYNDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 87 RAAYNIGVLRHLQVIfghlaASRLQYYvprgfwkqfrlwgepvnlrEQHDALEFFNSLVDSLDEalkalghpaMLSKVLG 166
Cdd:cd02671 82 ANQAPRRLLNALREV-----NPMYEGY-------------------LQHDAQEVLQCILGNIQE---------LVEKDFQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 167 GSFADQKICQGCPHRYECEESFTTLNVDIRNHQ-------------------NLLDSLEQYVKGDLLEGANAYHCEKCNK 227
Cdd:cd02671 129 GQLVLRTRCLECETFTERREDFQDISVPVQESElskseesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCHH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 228 KVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAI----KFNDYFEFPRELDMEpytvagvaklegdnvnpesqliqqsEQ 303
Cdd:cd02671 209 YTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLE-------------------------EW 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418639693 304 SESETagSTKYRLVGVLVHSG-QASGGHYYSYIiqrnggdgernRWYKFDDGDVtecKMDDDEEMKNQC 371
Cdd:cd02671 264 STKPK--NDVYRLFAVVMHSGaTISSGHYTAYV-----------RWLLFDDSEV---KVTEEKDFLEAL 316
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
9-369 |
5.19e-18 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 84.30 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 9 GLKNAGATCYMNSVIQQLYMIPSirngilaiegtgsdVDDDMSGDEKQDNESNVDPRDDvfgYPQQF-----------ED 77
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPS--------------FQWRYDDLENKFPSDVVDPAND---LNCQLikladgllsgrYS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 78 KPALSKTEDrAAYNIGVLrhlqvifghlaasrlqyyvPRGFwKqfRLWGEpvNLRE-----QHDALEFFNSLVDSLDEAL 152
Cdd:cd02658 64 KPASLKSEN-DPYQVGIK-------------------PSMF-K--ALIGK--GHPEfstmrQQDALEFLLHLIDKLDRES 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 153 KALG--HPAMLSKVlggsFADQKI-CQGCPHRYECEESFTTLNVDIRNH--------------QNLLDSLEQYVKGDLLE 215
Cdd:cd02658 119 FKNLglNPNDLFKF----MIEDRLeCLSCKKVKYTSELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETIE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 216 ganaYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDY--DWErecaikfndyfefPRELDMEpytvagvakLEGDNVnp 293
Cdd:cd02658 195 ----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-------------PKKLDVP---------IDVPEE-- 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418639693 294 esqliqqseqsesetAGSTKYRLVGVLVHSG-QASGGHYYSYIIQRNGGDGernRWYKFDDGDVteCKMDDDEEMKN 369
Cdd:cd02658 247 ---------------LGPGKYELIAFISHKGtSVHSGHYVAHIKKEIDGEG---KWVLFNDEKV--VASQDPPEMKK 303
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
8-358 |
3.67e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 82.15 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 8 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMsGDEKQDNESNVDPRDdvfgypqqfedkpalsktEDR 87
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDY-PTERRIGGREVSRSE------------------LQR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 88 AaynIGVLRHLQVIFGHLAASRLQYYVPRGfwkqfrlwgEPVNLR-EQHDALEFFNSLVDSLDEALKALG-HPAMLSKVL 165
Cdd:cd02666 63 S---NQFVYELRSLFNDLIHSNTRSVTPSK---------ELAYLAlRQQDVTECIDNVLFQLEVALEPISnAFAGPDTED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 166 GGSFADQ-------KICQ--------GCPHRYECEESFTTLNVDIR---------NH-QNLLDSLEQYVKGDLLEganay 220
Cdd:cd02666 131 DKEQSDLikrlfsgKTKQqlvpesmgNQPSVRTKTERFLSLLVDVGkkgreivvlLEpKDLYDALDRYFDYDSLT----- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 221 hcekcnkkvdtvkrllikKLPPVLAIQLKrfdydwerecaikfNDYFEFPRELDMEPYT----VAGVAKLEGDNVNPESQ 296
Cdd:cd02666 206 ------------------KLPQRSQVQAQ--------------LAQPLQRELISMDRYElpssIDDIDELIREAIQSESS 253
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1418639693 297 LIQQSEQSESETAG----------STKYRLVGVLVHSGQASGGHYYSYIiqrngGDGERNRWYKFDDGDVTE 358
Cdd:cd02666 254 LVRQAQNELAELKHeiekqfddlkSYGYRLHAVFIHRGEASSGHYWVYI-----KDFEENVWRKYNDETVTV 320
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
120-363 |
6.59e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 79.72 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 120 KQFRLWGEpvNLREQHDALEFFNSLVDSLDEALKalgHPamlskvLGGSFADQKICQGCPH----RYECeESFTTLNV-- 193
Cdd:cd02662 22 PSLIEYLE--EFLEQQDAHELFQVLLETLEQLLK---FP------FDGLLASRIVCLQCGEsskvRYES-FTMLSLPVpn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 194 -DIRNHQNLLDSLEQYVKGDLLEGanaYHCEKCnkkvdtvkRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRE 272
Cdd:cd02662 90 qSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 273 LDmepytvagvaklegdnvnpesqliqqseqsesetagSTKYRLVGVLVHSGQASGGHYYSY----IIQRNGGDGE---- 344
Cdd:cd02662 158 LP------------------------------------KVLYRLRAVVVHYGSHSSGHYVCYrrkpLFSKDKEPGSfvrm 201
|
250 260
....*....|....*....|....*.
gi 1418639693 345 -------RNRWYKFDDGDVTECKMDD 363
Cdd:cd02662 202 regpsstSHPWWRISDTTVKEVSESE 227
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
134-374 |
3.64e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 77.21 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 134 QHDALEFFNSLVDSLDEALKALGHPAMLSK--------VLGGSFADQKICQGcpHRYECEESFTTLNVDIRNHQNLLDSL 205
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEksknpmvqLFYGTFLTEGVLEG--KPFCNCETFGQYPLQVNGYGNLHECL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 206 E-QYVKGDLlEGANAYHCEKCNKkvdtvkRLLIKKLPPVLAIQLKRFDYDWERECaiKFNDYFEFPRELDMEPYtvagva 284
Cdd:cd02665 100 EaAMFEGEV-ELLPSDHSVKSGQ------ERWFTELPPVLTFELSRFEFNQGRPE--KIHDKLEFPQIIQQVPY------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 285 klegdnvnpesqliqqseqsesetagstkyRLVGVLVHSGQASGGHYYSYIIQRNggdgeRNRWYKFDDGDVTECkmdDD 364
Cdd:cd02665 165 ------------------------------ELHAVLVHEGQANAGHYWAYIYKQS-----RQEWEKYNDISVTES---SW 206
|
250
....*....|
gi 1418639693 365 EEMKNQCFGG 374
Cdd:cd02665 207 EEVERDSFGG 216
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
9-406 |
1.49e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 76.38 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 9 GLKNAGATCYMNSVIQQL-YMIPSIRNGILAIEGTGSDVDDDMSGDEKQDNesnvdprddvfgypqqfedkpalsktEDR 87
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKNVIRKPEPDLN--------------------------QEE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 88 AAYnigVLRHLQVIFGHLAASRLQYYvprgfwkqfrlwgepvnlrEQHDALEFFNSLVDSLDEALKALG----HPAMLSK 163
Cdd:COG5533 55 ALK---LFTALWSSKEHKVGWIPPMG-------------------SQEDAHELLGKLLDELKLDLVNSFtiriFKTTKDK 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 164 V--LGGSFADQKICQgcPHRYECEESFTTlnvdirnhQNLLDSLEQYVkgDLLEGANAyhceKCNKKVDTVKRLL----I 237
Cdd:COG5533 113 KktSTGDWFDIIIEL--PDQTWVNNLKTL--------QEFIDNMEELV--DDETGVKA----KENEELEVQAKQEyevsF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 238 KKLPPVLAIQLKRFDYDwerecaikfndyfefpreldmepytvAGVAKLEgDNVNPESQLIQQSEQSeSETAGSTKYRLV 317
Cdd:COG5533 177 VKLPKILTIQLKRFANL--------------------------GGNQKID-TEVDEKFELPVKHDQI-LNIVKETYYDLV 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 318 GVLVHSGQASGGHYYSYIiqRNGGDgernrWYKFDDGDVTECKMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrww 397
Cdd:COG5533 229 GFVLHQGSLEGGHYIAYV--KKGGK-----WEKANDSDVTPVSEEEAINEKAK--------------------------- 274
|
....*....
gi 1418639693 398 NAYILFYER 406
Cdd:COG5533 275 NAYLYFYER 283
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
8-353 |
2.02e-14 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 73.46 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 8 VGLKNAGATCYMNSVIQQLYMIPSIRNgiLAIEGTGSDVDD------------DMSGDEKQDN--ESNvdprddvfgypq 73
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRN--LALSHLATECLKehcllcelgflfDMLEKAKGKNcqASN------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 74 qFEDkpALSKTEDraAYNIGVLRHLQVIFGHLAASRL-QYyvprgfWKQFRLwgepvnlrEQ--HDALEFFNSLVDSlde 150
Cdd:pfam13423 67 -FLR--ALSSIPE--ASALGLLDEDRETNSAISLSSLiQS------FNRFLL--------DQlsSEENSTPPNPSPA--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 151 alkalghPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLN------VDIRNHQNLLDSLEQYVKGDLL-EGANAYHCE 223
Cdd:pfam13423 125 -------ESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDliyprkPSSNNKKPPNQTFSSILKSSLErETTTKAWCE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 224 KCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWEREcaIKFNDYfeFPRELDMepytvagvaklegdnvnpesqliqQSEQ 303
Cdd:pfam13423 198 KCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL--WKTPGW--LPPEIGL------------------------TLSD 249
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1418639693 304 SESETAGSTKYRLVGVLVH-SGQASGGHYYSYI--IQRNGGDGERNRWYKFDD 353
Cdd:pfam13423 250 DLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVkvADSELEDPTESQWYLFND 302
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
201-406 |
3.23e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 71.45 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 201 LLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYT 279
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPiDDLDLSGVE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 280 VAgvaklegdnvNPESQLIqqseqsesetagstkYRLVGVLVHSGQASGGHYYSYIiqRNGGDgerNRWYKFDDGDVTEc 359
Cdd:COG5560 755 YM----------VDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYA--RNFAN---NGWYLFDDSRITE- 803
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1418639693 360 kMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYER 406
Cdd:COG5560 804 -VDPEDSVTS----------------------------SAYVLFYRR 821
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
6-359 |
1.44e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 62.72 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 6 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNVDPRDDVFGypqqfedkpALSkte 85
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFL-------------LYENYENIKDRKSELVKRLS---------ELI--- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 86 dRAAYNIGVLRhlqvifGHLAASRLQYYVPRGFWKQFRLwgepvnlREQHDALEFFNSLVDSLdealkalgHPAmlskvL 165
Cdd:cd02669 173 -RKIWNPRNFK------GHVSPHELLQAVSKVSKKKFSI-------TEQSDPVEFLSWLLNTL--------HKD-----L 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 166 GGSFAD-----QKICQG---------CPHRYECEES----------------FTTLNVDIRN-----HQNLLDSLEQYVK 210
Cdd:cd02669 226 GGSKKPnssiiHDCFQGkvqietqkiKPHAEEEGSKdkffkdsrvkktsvspFLLLTLDLPPpplfkDGNEENIIPQVPL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 211 GDLLEGANAYHCEKCNKKVdtvKRLLIKKLPPVLAIQLKRFDYdwerecaikfNDYF--------EFPRELDMEPYTVAG 282
Cdd:cd02669 306 KQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSK----------NNFFkeknptivNFPIKNLDLSDYVHF 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418639693 283 VAKLEGDnvnpesqliqqseqsesetagSTKYRLVGVLVHSGQASGGHYYSYIIQRNGgdgeRNRWYKFDDGDVTEC 359
Cdd:cd02669 373 DKPSLNL---------------------STKYNLVANIVHEGTPQEDGTWRVQLRHKS----TNKWFEIQDLNVKEV 424
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
237-405 |
2.24e-07 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 51.76 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 237 IKKLPPVLAIQLKRfdYDWERECAIKFNDYFEFPRELDMePYTVAGvAKLEGDNVNPESQlIQQSEQSESETAGSTKYRL 316
Cdd:cd02670 95 FAKAPSCLIICLKR--YGKTEGKAQKMFKKILIPDEIDI-PDFVAD-DPRACSKCQLECR-VCYDDKDFSPTCGKFKLSL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 317 VGVLVHSGQA-SGGHYYSYI------IQRNGGDGERNRWYKFDDgdvteckMDDDEemknqcfGGEYmgeVFDHMMKRms 389
Cdd:cd02670 170 CSAVCHRGTSlETGHYVAFVrygsysLTETDNEAYNAQWVFFDD-------MADRD-------GVSN---GFNIPAAR-- 230
|
170
....*....|....*.
gi 1418639693 390 yrrqkRWWNAYILFYE 405
Cdd:cd02670 231 -----LLEDPYMLFYQ 241
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
172-358 |
1.18e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 46.74 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 172 QKICQGCPHRYECEESFTTLNVDIRNHQNL-----LDSLEQYVKGDL-LEGANAYHCEKCNKKVDTVKRLLIKKLPP--- 242
Cdd:cd02672 81 SQDQLGTPFSCGTSRNSVSLLYTLSLPLGStktskESTFLQLLKRSLdLEKVTKAWCDTCCKYQPLEQTTSIRHLPDill 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418639693 243 -VLAIQLKRFDydweRECAIKFNDYFEFpreLDMEPytvaGVAKLEGDNVNPESQLIQQSeqsesetagSTKYRLVGVLV 321
Cdd:cd02672 161 lVLVINLSVTN----GEFDDINVVLPSG---KVMQN----KVSPKAIDHDKLVKNRGQES---------IYKYELVGYVC 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1418639693 322 H-SGQASGGHYYSYIIQRNgGDGERNRWYKFDDGDVTE 358
Cdd:cd02672 221 EiNDSSRGQHNVVFVIKVN-EESTHGRWYLFNDFLVTP 257
|
|
| |
