|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1963 |
1.74e-154 |
|
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: 481.76 E-value: 1.74e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1560 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIegtgsdvdddmsgdekqdnesnvdprddvfgypqqfedkpplsKTE 1639
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1640 DRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVL 1719
Cdd:cd02659 38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1720 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1799
Cdd:cd02659 118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1800 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDnvnpesqliqqneqSESEKAGSTKYRLVGVLVHSGQ 1879
Cdd:cd02659 198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGD--------------SEKKDSESYIYELHGVLVHSGD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1880 ASGGHYYSYIIQRNggdgeKNRWYKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 1959
Cdd:cd02659 264 AHGGHYYSYIKDRD-----DGKWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330
|
....
gi 1720434944 1960 RMDT 1963
Cdd:cd02659 331 RKSP 334
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
2102-2481 |
2.59e-103 |
|
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.
Pssm-ID: 463438 Cd Length: 407 Bit Score: 338.12 E-value: 2.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 2102 SNRFSEYLLECPSAEVRGAFAKLIVFIAH-----FSLQDGPCPspfaspgPSSQAYDNLSLSDHLLRAVLNLLRR---EV 2173
Cdd:pfam12030 1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCD-------PDDLEEEWRSLSDSVLEAVVALLDHlwkEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 2174 SEHGRHLQQYFNLFVMYANLGVAEKTQLLKLS-VPATFMLVSLDEGPGPPIKYQYAEL------------GKLYSVVSQL 2240
Cdd:pfam12030 74 HTHLRSWDEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARMlrlvekrrppsyEKLIQLLSVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 2241 IRCCNVSSRMQSSINGNPSLPNpfgdpNLSQPIMPIQQNVVDIL--FVRT---SYVKKIIEDCSNSDETVKLLRFCCWEN 2315
Cdd:pfam12030 154 LRCCDLSLPPQSINEGAEPLPN-----SLPDGPFPLTSEEADLLrpLGRTngsIFVKKLLEIDQNPEATRKILRFLLWEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 2316 PQFSSTVLSELLWQVAYSYTYELR-PYLDLLLQILliEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIK 2394
Cdd:pfam12030 229 PELSDSILKTLLWGIRGAPAHLLRdPFLRAAIVFC--EDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCIN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 2395 CMvALFSSCPVAYQILQgngdlkrkwtwavewlgdelerrpytgnpqyTYNNWSPPVQSNETSN---------------- 2458
Cdd:pfam12030 307 CR-LGFDKEWFASQVLE-------------------------------NIPDWAPPLLSYPDSNvrsetedflqeelfsh 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1720434944 2459 ---------------------------GYFLERS---HSARMTLAKACELCPE 2481
Cdd:pfam12030 355 emgpdpqfrlreaarrlgiacleylrgTYVLRRSqveRSAVETLQRVIELCPE 407
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1562-1958 |
9.10e-80 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 266.62 E-value: 9.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1562 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDvdddmsgdekqdnesnvdprddvfgypqqfedkpplskteDR 1641
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSED----------------------------------------SR 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1642 KEYNIGVLRHLQVIFGHLA-ASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKA---LGHPAMLSK 1717
Cdd:pfam00443 41 YNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1718 VLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLL------DSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 1791
Cdd:pfam00443 121 LFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1792 KKLPPVLAIQLKRFDYDweRECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVnpesqliqqneqsesekagstKYRLV 1871
Cdd:pfam00443 201 SRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ---------------------DYRLV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1872 GVLVHSGQASGGHYYSYIIQrnggdGEKNRWYKFDDGDVTECKMDDDEEMknqcfggeymgevfdhmmkrmsyrrqkrwW 1951
Cdd:pfam00443 258 AVVVHSGSLSSGHYIAYIKA-----YENNRWYKFDDEKVTEVDEETAVLS-----------------------------S 303
|
....*..
gi 1720434944 1952 NAYILFY 1958
Cdd:pfam00443 304 SAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1685-1959 |
7.09e-55 |
|
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: 192.70 E-value: 7.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1685 LREQHDALEFFNSLVDSLDEALKALG--------HPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI----RNH 1752
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSkrtsdsssLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1753 QNLLDSLEQYVKGDLLEGANAYHCEKCnKKVDTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPY 1832
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1833 TVAGVAKLEGDNvnpesqliqqneqsesekaGSTKYRLVGVLVHSGQ-ASGGHYYSYIIqrnggDGEKNRWYKFDDGDVT 1911
Cdd:cd02257 177 LSEGEKDSDSDN-------------------GSYKYELVAVVVHSGTsADSGHYVAYVK-----DPSDGKWYKFNDDKVT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720434944 1912 ECKMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkRWWNAYILFYE 1959
Cdd:cd02257 233 EVSEEEVLEFGS-------------------------LSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1563-1959 |
9.98e-52 |
|
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: 186.47 E-value: 9.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1563 GLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDekQDNESNvdprddvfgypqqfedkpplsktedrk 1642
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPD--KPHEPQ--------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1643 eyniGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLwgepvNLREQHDALEFFNSLVDSLDEALKALGHP---AMLSKVL 1719
Cdd:cd02668 52 ----TIIDQLQLIFAQLQFGNRSVVDPSGFVKALGL-----DTGQQQDAQEFSKLFLSLLEAKLSKSKNPdlkNIVQDLF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1720 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1799
Cdd:cd02668 123 RGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1800 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVagvaklegdnvnpesqliqqnEQSEsekaGSTKYRLVGVLVHSGQ 1879
Cdd:cd02668 203 FQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA---------------------ESDE----GSYVYELSGVLIHQGV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1880 -ASGGHYYSYIIQRNGGdgeknRWYKFDDGDVTE-----CKMDDDEEMKNQCFGgeymgevfDHMMKRMSYRrqkrwwNA 1953
Cdd:cd02668 258 sAYSGHYIAHIKDEQTG-----EWYKFNDEDVEEmpgkpLKLGNSEDPAKPRKS--------EIKKGTHSSR------TA 318
|
....*.
gi 1720434944 1954 YILFYE 1959
Cdd:cd02668 319 YMLVYK 324
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1560-2006 |
2.83e-48 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 190.08 E-value: 2.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1560 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEgtgsdvdddmsgdekQDNEsnvDPRDDV-------FgYPQQFEDK 1632
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP---------------TDHP---RGRDSValalqrlF-YNLQTGEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1633 PpLSKTEdrkeynigvlrhLQVIFGhlaasrlqyyvprgfwkqfrlWGEPVNLReQHDALEFFNSLVDSLDEALKALGHP 1712
Cdd:COG5077 253 P-VDTTE------------LTRSFG---------------------WDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1713 AMLSKVLGGSFadqKICQGCPHR-YECE--ESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKcNKKVDTVKRL 1789
Cdd:COG5077 298 NALNGIFVGKM---KSYIKCVNVnYESArvEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1790 LIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYtvagvaklegdnVNPESqliqqnEQSESEKAgstKYR 1869
Cdd:COG5077 374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF------------LDRDA------DKSENSDA---VYV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1870 LVGVLVHSGQASGGHYYSYIiqRNGGDGeknRWYKFDDGDVTECKMdddEEMKNQCFGGEYMGEVfdhmmKRMSYRRQKR 1949
Cdd:COG5077 433 LYGVLVHSGDLHEGHYYALL--KPEKDG---RWYKFDDTRVTRATE---KEVLEENFGGDHPYKD-----KIRDHSGIKR 499
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720434944 1950 WWNAYILFYERMDTIghdDEVIRYISEIAITTRPHQIVMPSAIERSVRKQNVQFMHN 2006
Cdd:COG5077 500 FMSAYMLVYLRKSML---DDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHL 553
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1563-1917 |
8.05e-44 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 162.83 E-value: 8.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1563 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNvdprddvfgypqqfedkpplsktedrk 1642
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLL-------------SREHSKDCCNE--------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1643 eyNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEA-------LKALGHPA-- 1713
Cdd:cd02661 43 --GFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKAcldrfkkLKAVDPSSqe 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1714 --MLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 1791
Cdd:cd02661 121 ttLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1792 KKLPPVLAIQLKRFDYDWERecaiKFNDYFEFPRELDMEPYTVagvaklegdnvnpesqliqqneqseSEKAGSTKYRLV 1871
Cdd:cd02661 201 HRAPNVLTIHLKRFSNFRGG----KINKQISFPETLDLSPYMS-------------------------QPNDGPLKYKLY 251
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720434944 1872 GVLVHSG-QASGGHYYSYIIQRNGgdgeknRWYKFDDGDVTECKMDD 1917
Cdd:cd02661 252 AVLVHSGfSPHSGHYYCYVKSSNG------KWYNMDDSKVSPVSIET 292
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1687-1959 |
1.44e-38 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 145.12 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1687 EQHDALEFFNSLVDSLDealkalghpAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI------RNHQNLLDSLE 1760
Cdd:cd02674 21 DQQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1761 QYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYTVAgvak 1839
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPlNDLDLTPYVDT---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1840 legdnvnpesqliqqneqseSEKAGSTKYRLVGVLVHSGQASGGHYYSYIiqrngGDGEKNRWYKFDDGDVTecKMDDDE 1919
Cdd:cd02674 166 --------------------RSFTGPFKYDLYAVVNHYGSLNGGHYTAYC-----KNNETNDWYKFDDSRVT--KVSESS 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720434944 1920 EMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYE 1959
Cdd:cd02674 219 VVSS----------------------------SAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1563-1912 |
1.43e-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: 139.43 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1563 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgSDvDDDMSGDEKQDNESNVDPRDDVFgypQQFedkpplSKTEDRK 1642
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL------SD-RHSCTCLSCSPNSCLSCAMDEIF---QEF------YYSGDRS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1643 EYnigvlrhlqvifghlAASRLQYyvprGFWKQFRlwgepvNL--REQHDALEFFNSLVDSLDE-ALKALGHPAMLS--- 1716
Cdd:cd02660 66 PY---------------GPINLLY----LSWKHSR------NLagYSQQDAHEFFQFLLDQLHThYGGDKNEANDEShcn 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1717 ----KVLGGSFADQKICQGCPHRYECEESFTTLNVDIRN---------------HQNLLDSLEQYVKGDLLeGANAYHCE 1777
Cdd:cd02660 121 ciihQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNkstpswalgesgvsgTPTLSDCLDRFTRPEKL-GDFAYKCS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1778 KCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTVAGvaklegdnvnpesqliQQNEQ 1857
Cdd:cd02660 200 GCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTSSS----------------IGDTQ 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720434944 1858 SESEKAGSTKYRLVGVLVHSGQASGGHYYSYIIQRNGgdgeknRWYKFDDGDVTE 1912
Cdd:cd02660 263 DSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDG------QWFKFDDAMITR 311
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1563-1959 |
7.08e-32 |
|
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: 128.76 E-value: 7.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1563 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNVdprddvfgypqqfedkpplsktedrk 1642
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVL-------------SLNLPRLGDSQS-------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1643 eynigVLRHLQVIFGHLAASRLQYY-VPRGFWKQfrLWGEPVNLREQHDALEFFNSLVDSLDealkalghpAMLSKVLGG 1721
Cdd:cd02664 42 -----VMKKLQLLQAHLMHTQRRAEaPPDYFLEA--SRPPWFTPGSQQDCSEYLRYLLDRLH---------TLIEKMFGG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1722 SFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDsleQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQ 1801
Cdd:cd02664 106 KLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDLLN---YFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1802 LKRFDYDWERECAIKFNDYFEFPRELDMePYTVAgvaklegdNVNPESQLIQQNEQSESEKAGSTK---YRLVGVLVHSG 1878
Cdd:cd02664 183 LLRFSYDQKTHVREKIMDNVSINEVLSL-PVRVE--------SKSSESPLEKKEEESGDDGELVTRqvhYRLYAVVVHSG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1879 QAS-GGHYYSYIiqRNGGDGEKNR-----------------WYKFDDGDVTECKMdddEEMKNqcfggeyMGEVFDHMmk 1940
Cdd:cd02664 254 YSSeSGHYFTYA--RDQTDADSTGqecpepkdaeendesknWYLFNDSRVTFSSF---ESVQN-------VTSRFPKD-- 319
|
410
....*....|....*....
gi 1720434944 1941 rmsyrrqkrwwNAYILFYE 1959
Cdd:cd02664 320 -----------TPYILFYE 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1688-1959 |
1.34e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 114.79 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1688 QHDALEFFNSLVDSLDEALKalghpamlsKVLGGSFADQKICQGCPHRYECEESFTTLN----VDIRNHQNLLDSLEQYV 1763
Cdd:cd02667 51 QQDSHELLRYLLDGLRTFID---------SIFGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKSECSIESCLKQFT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1764 KGDLLEGANAYHCEKCNKkvdTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGD 1843
Cdd:cd02667 122 EVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1844 NvnpesqliqqneqsesekagSTKYRLVGVLVHSGQASGGHYYSYI----------------IQRNGGDGEKNRWYKFDD 1907
Cdd:cd02667 198 S--------------------SVLYRLYGVVEHSGTMRSGHYVAYVkvrppqqrlsdltkskPAADEAGPGSGQWYYISD 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720434944 1908 GDVTEckMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrwwnAYILFYE 1959
Cdd:cd02667 258 SDVRE--VSLEEVLKSE----------------------------AYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1688-1959 |
4.34e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 113.94 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1688 QHDALEFFNSLVDSLDEALKALG-----------------HPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIR 1750
Cdd:cd02663 65 HQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1751 NHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDME 1830
Cdd:cd02663 145 QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1831 PYTvagvakleGDNVNPESqliqqneqsesekagstKYRLVGVLVHSGQ-ASGGHYYSyIIQRNGGdgeknrWYKFDDGD 1909
Cdd:cd02663 225 NTT--------DDAENPDR-----------------LYELVAVVVHIGGgPNHGHYVS-IVKSHGG------WLLFDDET 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1910 VTecKMDDdeemknqcfggEYMGEVFDHmmkrmsyrrQKRWWNAYILFYE 1959
Cdd:cd02663 273 VE--KIDE-----------NAVEEFFGD---------SPNQATAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1563-1959 |
1.25e-20 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1563 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvddDMSGDEKQDNESNVDPrddVFGYPQQFEDkppLSKTEDRk 1642
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALK-----------NYNPARRGANQSSDNL---TNALRDLFDT---MDKKQEP- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1643 eynigvlrhlqvifghlaasrlqyYVPRGFWKQFRL----WGEP--VNLREQHDALEFFNSLVDSLDEALK-ALGHPAML 1715
Cdd:cd02657 63 ------------------------VPPIEFLQLLRMafpqFAEKqnQGGYAQQDAEECWSQLLSVLSQKLPgAGSKGSFI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1716 SKVLGGSFADQKICQGCPHRYECE-ESFTTLNVDIrNHQNLLDSLEQYVKgDLLEGANAYHCEKCNKKVDTVKRLLIKKL 1794
Cdd:cd02657 119 DQLFGIELETKMKCTESPDEEEVStESEYKLQCHI-SITTEVNYLQDGLK-KGLEEEIEKHSPTLGRDAIYTKTSRISRL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1795 PPVLAIQLKRFDydWERECAI--KFNDYFEFPRELDMEPYTvagvaklegdnvnpesqliqqneqsesekAGSTKYRLVG 1872
Cdd:cd02657 197 PKYLTVQFVRFF--WKRDIQKkaKILRKVKFPFELDLYELC-----------------------------TPSGYYELVA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1873 VLVHSGQ-ASGGHYYSYIIQRNGgdgekNRWYKFDDGDVTECKMDDDEEMKNqcfGGEYmgevfdHMmkrmsyrrqkrww 1951
Cdd:cd02657 246 VITHQGRsADSGHYVAWVRRKND-----GKWIKFDDDKVSEVTEEDILKLSG---GGDW------HI------------- 298
|
....*...
gi 1720434944 1952 nAYILFYE 1959
Cdd:cd02657 299 -AYILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1563-1923 |
1.44e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 86.22 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1563 GLKNAGATCYMNSVIQQLYMIPSirngilaiegtgsdVDDDMSGDEKQDNESNVDPRDDvfgYPQQF----------EDK 1632
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPS--------------FQWRYDDLENKFPSDVVDPAND---LNCQLikladgllsgRYS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1633 PPLSKTEDRKEYNIGVLrhlqvifghlaasrlqyyvPRGFwKqfRLWGEpvNLRE-----QHDALEFFNSLVDSLDEALK 1707
Cdd:cd02658 64 KPASLKSENDPYQVGIK-------------------PSMF-K--ALIGK--GHPEfstmrQQDALEFLLHLIDKLDRESF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1708 ALG--HPAMLSKVlggsFADQKI-CQGCPHRYECEESFTTLNVDIRNH--------------QNLLDSLEQYVKGDLLEg 1770
Cdd:cd02658 120 KNLglNPNDLFKF----MIEDRLeCLSCKKVKYTSELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETIE- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1771 anaYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDY--DWErecaikfndyfefPRELDMEpytvagvakLEGDNVnpe 1848
Cdd:cd02658 195 ---DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-------------PKKLDVP---------IDVPEE--- 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720434944 1849 sqliqqneqsesekAGSTKYRLVGVLVHSG-QASGGHYYSYIIQRnggDGEKNRWYKFDDGDVteCKMDDDEEMKN 1923
Cdd:cd02658 247 --------------LGPGKYELIAFISHKGtSVHSGHYVAHIKKE---IDGEGKWVLFNDEKV--VASQDPPEMKK 303
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1538-1910 |
3.85e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 85.33 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1538 ITTCEALtewEYLPPvgprppkgFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSgdekqdnesnvd 1617
Cdd:cd02671 12 ATSCEKR---ENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQS------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1618 prddvfgypqQFEDKPPLSKTEDRKEYNIGVLRHLQVIfghlaASRLQYYvprgfwkqfrlwgepvnlrEQHDALEFFNS 1697
Cdd:cd02671 69 ----------SFLLNPEKYNDELANQAPRRLLNALREV-----NPMYEGY-------------------LQHDAQEVLQC 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1698 LVDSLDEalkalghpaMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQ-------------------NLLDS 1758
Cdd:cd02671 115 ILGNIQE---------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESElskseesseispdpktemkTLKWA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1759 LEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAI----KFNDYFEFPRELDMEpytv 1834
Cdd:cd02671 186 ISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLE---- 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720434944 1835 agvaklegdnvnpesqliqqnEQSESEKagSTKYRLVGVLVHSG-QASGGHYYSYIiqrnggdgeknRWYKFDDGDV 1910
Cdd:cd02671 262 ---------------------EWSTKPK--NDVYRLFAVVMHSGaTISSGHYTAYV-----------RWLLFDDSEV 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1563-1960 |
9.61e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 83.31 E-value: 9.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1563 GLKNAGATCYMNSVIQQL-YMIPSIRNGILAIEGTGSDVDDDMSGDEKQDNE-------SNVDPRDDvfgypQQFEDKPP 1634
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKNVIRKPEPDLNQeealklfTALWSSKE-----HKVGWIPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1635 LSKTEDRKEYnigvlrhLQVIFGHLAASRLqyyvprgfwKQFRLWGEPVNLREQHDALEFFNSLVDSLdealkalghpam 1714
Cdd:COG5533 76 MGSQEDAHEL-------LGKLLDELKLDLV---------NSFTIRIFKTTKDKKKTSTGDWFDIIIEL------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1715 lskvlggsfadqkicqgcPHRYECEESFTTlnvdirnhQNLLDSLEQYVkgDLLEGANAyhceKCNKKVDTVKRLL---- 1790
Cdd:COG5533 128 ------------------PDQTWVNNLKTL--------QEFIDNMEELV--DDETGVKA----KENEELEVQAKQEyevs 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1791 IKKLPPVLAIQLKRFDYDwerecaikfndyfefpreldmepytvAGVAKLEgDNVNPESQLIQQNEQSeSEKAGSTKYRL 1870
Cdd:COG5533 176 FVKLPKILTIQLKRFANL--------------------------GGNQKID-TEVDEKFELPVKHDQI-LNIVKETYYDL 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1871 VGVLVHSGQASGGHYYSYIIQrnggdgeKNRWYKFDDGDVTECKMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrw 1950
Cdd:COG5533 228 VGFVLHQGSLEGGHYIAYVKK-------GGKWEKANDSDVTPVSEEEAINEKAK-------------------------- 274
|
410
....*....|
gi 1720434944 1951 wNAYILFYER 1960
Cdd:COG5533 275 -NAYLYFYER 283
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1562-1912 |
1.17e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 84.08 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1562 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMsGDEKQDNESNVDPRDdvFGYPQQFedkpplsktedr 1641
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDY-PTERRIGGREVSRSE--LQRSNQF------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1642 keynigvLRHLQVIFGHLAASRLQYYVPRGfwkqfrlwgEPVNLR-EQHDALEFFNSLVDSLDEALKALG-HPAMLSKVL 1719
Cdd:cd02666 67 -------VYELRSLFNDLIHSNTRSVTPSK---------ELAYLAlRQQDVTECIDNVLFQLEVALEPISnAFAGPDTED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1720 GGSFADQ-------KICQ--------GCPHRYECEESFTTLNVDIR---------NH-QNLLDSLEQYVKGDLLEganay 1774
Cdd:cd02666 131 DKEQSDLikrlfsgKTKQqlvpesmgNQPSVRTKTERFLSLLVDVGkkgreivvlLEpKDLYDALDRYFDYDSLT----- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1775 hcekcnkkvdtvkrllikKLPPVLAIQLKrfdydwerecaikfNDYFEFPRELDMEPYT----VAGVAKLEGDNVNPESQ 1850
Cdd:cd02666 206 ------------------KLPQRSQVQAQ--------------LAQPLQRELISMDRYElpssIDDIDELIREAIQSESS 253
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720434944 1851 LIQQ--------NEQSESEKAG--STKYRLVGVLVHSGQASGGHYYSYIiqrngGDGEKNRWYKFDDGDVTE 1912
Cdd:cd02666 254 LVRQaqnelaelKHEIEKQFDDlkSYGYRLHAVFIHRGEASSGHYWVYI-----KDFEENVWRKYNDETVTV 320
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1674-1917 |
1.64e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 78.56 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1674 KQFRLWGEpvNLREQHDALEFFNSLVDSLDEALKalgHPamlskvLGGSFADQKICQGCPH----RYECeESFTTLNV-- 1747
Cdd:cd02662 22 PSLIEYLE--EFLEQQDAHELFQVLLETLEQLLK---FP------FDGLLASRIVCLQCGEsskvRYES-FTMLSLPVpn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1748 -DIRNHQNLLDSLEQYVKGDLLEGanaYHCEKCnkkvdtvkRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRE 1826
Cdd:cd02662 90 qSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1827 LDmepytvagvaklegdnvnpesqliqqneqsesekagSTKYRLVGVLVHSGQASGGHYYSY----IIQRNGGDGE---- 1898
Cdd:cd02662 158 LP------------------------------------KVLYRLRAVVVHYGSHSSGHYVCYrrkpLFSKDKEPGSfvrm 201
|
250 260
....*....|....*....|....*.
gi 1720434944 1899 -------KNRWYKFDDGDVTECKMDD 1917
Cdd:cd02662 202 regpsstSHPWWRISDTTVKEVSESE 227
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1688-1928 |
6.06e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 76.44 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1688 QHDALEFFNSLVDSLDEALKALGHPAMLSK--------VLGGSFADQKICQGcpHRYECEESFTTLNVDIRNHQNLLDSL 1759
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEksknpmvqLFYGTFLTEGVLEG--KPFCNCETFGQYPLQVNGYGNLHECL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1760 E-QYVKGDLlEGANAYHCEKCNKkvdtvkRLLIKKLPPVLAIQLKRFDYDWERECaiKFNDYFEFPRELDMEPYtvagva 1838
Cdd:cd02665 100 EaAMFEGEV-ELLPSDHSVKSGQ------ERWFTELPPVLTFELSRFEFNQGRPE--KIHDKLEFPQIIQQVPY------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1839 klegdnvnpesqliqqneqsesekagstkyRLVGVLVHSGQASGGHYYSYIIQRNggdgeKNRWYKFDDGDVTECkmdDD 1918
Cdd:cd02665 165 ------------------------------ELHAVLVHEGQANAGHYWAYIYKQS-----RQEWEKYNDISVTES---SW 206
|
250
....*....|
gi 1720434944 1919 EEMKNQCFGG 1928
Cdd:cd02665 207 EEVERDSFGG 216
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1755-1960 |
4.31e-12 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 71.84 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1755 LLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYT 1833
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPiDDLDLSGVE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1834 VAgvaklegdnvNPESQLIqqneqsesekagstkYRLVGVLVHSGQASGGHYYSYIiqRNGGDgekNRWYKFDDGDVTEc 1913
Cdd:COG5560 755 YM----------VDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYA--RNFAN---NGWYLFDDSRITE- 803
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720434944 1914 kMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYER 1960
Cdd:COG5560 804 -VDPEDSVTS----------------------------SAYVLFYRR 821
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1562-1907 |
3.87e-11 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 66.91 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1562 VGLKNAGATCYMNSVIQQLYMIPSIRNgiLAIEGTGSDVDD------------DMSGDEKQDN--ESNvdprddvfgypq 1627
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRN--LALSHLATECLKehcllcelgflfDMLEKAKGKNcqASN------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1628 qfedkppLSKTED--RKEYNIGVLRHLQVIFGHLAASRL-QYyvprgfWKQFRLwgepvnlrEQ--HDALEFFNSLVDSl 1702
Cdd:pfam13423 67 -------FLRALSsiPEASALGLLDEDRETNSAISLSSLiQS------FNRFLL--------DQlsSEENSTPPNPSPA- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1703 dealkalghPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLN------VDIRNHQNLLDSLEQYVKGDLL-EGANAYH 1775
Cdd:pfam13423 125 ---------ESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDliyprkPSSNNKKPPNQTFSSILKSSLErETTTKAW 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1776 CEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWEREcaIKFNDYfeFPRELDMepytvagvaklegdnvnpesqliqQN 1855
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL--WKTPGW--LPPEIGL------------------------TL 247
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720434944 1856 EQSESEKAGSTKYRLVGVLVH-SGQASGGHYYSYI--IQRNGGDGEKNRWYKFDD 1907
Cdd:pfam13423 248 SDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVkvADSELEDPTESQWYLFND 302
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1548-1913 |
6.62e-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: 63.88 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1548 EYLPpvgprppkGFVGLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEkqdnesnvdprddvfgYPQ 1627
Cdd:cd02669 114 PYLP--------GFVGLNNIKNNDYANVIIQALSHVKPIRNFFL-------------LYEN----------------YEN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1628 QFEDKPPLSKTED---RKEYNIGVLRhlqvifGHLAASRLQYYVPRGFWKQFRLwgepvnlREQHDALEFFNSLVDSLde 1704
Cdd:cd02669 157 IKDRKSELVKRLSeliRKIWNPRNFK------GHVSPHELLQAVSKVSKKKFSI-------TEQSDPVEFLSWLLNTL-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1705 alkalgHPAmlskvLGGSFAD-----QKICQG---------CPHRYECEES----------------FTTLNVDIRN--- 1751
Cdd:cd02669 222 ------HKD-----LGGSKKPnssiiHDCFQGkvqietqkiKPHAEEEGSKdkffkdsrvkktsvspFLLLTLDLPPppl 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1752 --HQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVdtvKRLLIKKLPPVLAIQLKRFDYdwerecaikfNDYF-------- 1821
Cdd:cd02669 291 fkDGNEENIIPQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSK----------NNFFkeknptiv 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1822 EFPRELDMEPYTVAgvaklegdnvnpeSQLIQQNEqsesekagSTKYRLVGVLVHSGQASGGHYYSYIIQRNGGdgekNR 1901
Cdd:cd02669 358 NFPIKNLDLSDYVH-------------FDKPSLNL--------STKYNLVANIVHEGTPQEDGTWRVQLRHKST----NK 412
|
410
....*....|..
gi 1720434944 1902 WYKFDDGDVTEC 1913
Cdd:cd02669 413 WFEIQDLNVKEV 424
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1687-1959 |
6.24e-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: 52.91 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1687 EQHDALEFFNSLVDSLDealkalgHPAMLSKVlggsfadqKICQGcPHRYECEESFttlnVDIRNHQNLLDSLEQyVKGD 1766
Cdd:cd02670 22 EQQDPEEFFNFITDKLL-------MPLLEPKV--------DIIHG-GKKDQDDDKL----VNERLLQIPVPDDDD-GGGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1767 LLEganayHCEKC--NKKVdtvkrllIKKLPPVLAIQLKRfdYDWERECAIKFNDYFEFPRELDMePYTVAGvAKLEGDN 1844
Cdd:cd02670 81 TLE-----QCLEQyfNNSV-------FAKAPSCLIICLKR--YGKTEGKAQKMFKKILIPDEIDI-PDFVAD-DPRACSK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1845 VNPESQLIQQNEQSeSEKAGSTKYRLVGVLVHSGQA-SGGHYYSYI------IQRNGGDGEKNRWYKFDDgdvteckMDD 1917
Cdd:cd02670 145 CQLECRVCYDDKDF-SPTCGKFKLSLCSAVCHRGTSlETGHYVAFVrygsysLTETDNEAYNAQWVFFDD-------MAD 216
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720434944 1918 DEemknqcfGGEYmgeVFDHMMKRmsyrrqkRWWNAYILFYE 1959
Cdd:cd02670 217 RD-------GVSN---GFNIPAAR-------LLEDPYMLFYQ 241
|
|
| Ubl_UBP24 |
cd17065 |
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ... |
905-969 |
2.43e-06 |
|
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain.
Pssm-ID: 340585 Cd Length: 79 Bit Score: 47.30 E-value: 2.43e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720434944 905 DDLEVWSHTNDTIGSVRRCILNRIKANVAHtkIELFVGGELIDPGDDRKLIGQLNLKDKSLITAK 969
Cdd:cd17065 17 QEFTLEVHSNETLGSVRQKIAERLNCPVDQ--VQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1726-1912 |
2.26e-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: 45.58 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1726 QKICQGCPHRYECEESFTTLNVDIRNHQNL-----LDSLEQYVKGDL-LEGANAYHCEKCNKKVDTVKRLLIKKLPP--- 1796
Cdd:cd02672 81 SQDQLGTPFSCGTSRNSVSLLYTLSLPLGStktskESTFLQLLKRSLdLEKVTKAWCDTCCKYQPLEQTTSIRHLPDill 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434944 1797 -VLAIQLKRFDydweRECAIKFNDYFEFpreLDMEPytvaGVAKLEGDNVNPESQLIQQNeqsesekagSTKYRLVGVLV 1875
Cdd:cd02672 161 lVLVINLSVTN----GEFDDINVVLPSG---KVMQN----KVSPKAIDHDKLVKNRGQES---------IYKYELVGYVC 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720434944 1876 H-SGQASGGHYYSYIIQRNgGDGEKNRWYKFDDGDVTE 1912
Cdd:cd02672 221 EiNDSSRGQHNVVFVIKVN-EESTHGRWYLFNDFLVTP 257
|
|
| |
