|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1555-1958 |
1.50e-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: 482.14 E-value: 1.50e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1555 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIegtgsdvdddmsgdekqdnesnvdprddvfgypqqfedkpplsKTE 1634
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1635 DRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVL 1714
Cdd:cd02659 38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1715 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1794
Cdd:cd02659 118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1795 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDnvnpesqliqqneqSESEKAGSTKYRLVGVLVHSGQ 1874
Cdd:cd02659 198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGD--------------SEKKDSESYIYELHGVLVHSGD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1875 ASGGHYYSYIIQRNggdgeKNRWYKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 1954
Cdd:cd02659 264 AHGGHYYSYIKDRD-----DGKWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330
|
....
gi 1907203398 1955 RMDT 1958
Cdd:cd02659 331 RKSP 334
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
2097-2476 |
2.83e-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: 2.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 2097 SNRFSEYLLECPSAEVRGAFAKLIVFIAH-----FSLQDGPCPspfaspgPSSQAYDNLSLSDHLLRAVLNLLRR---EV 2168
Cdd:pfam12030 1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCD-------PDDLEEEWRSLSDSVLEAVVALLDHlwkEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 2169 SEHGRHLQQYFNLFVMYANLGVAEKTQLLKLS-VPATFMLVSLDEGPGPPIKYQYAEL------------GKLYSVVSQL 2235
Cdd:pfam12030 74 HTHLRSWDEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARMlrlvekrrppsyEKLIQLLSVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 2236 IRCCNVSSRMQSSINGNPSLPNpfgdpNLSQPIMPIQQNVVDIL--FVRT---SYVKKIIEDCSNSDETVKLLRFCCWEN 2310
Cdd:pfam12030 154 LRCCDLSLPPQSINEGAEPLPN-----SLPDGPFPLTSEEADLLrpLGRTngsIFVKKLLEIDQNPEATRKILRFLLWEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 2311 PQFSSTVLSELLWQVAYSYTYELR-PYLDLLLQILliEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIK 2389
Cdd:pfam12030 229 PELSDSILKTLLWGIRGAPAHLLRdPFLRAAIVFC--EDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCIN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 2390 CMvALFSSCPVAYQILQgngdlkrkwtwavewlgdelerrpytgnpqyTYNNWSPPVQSNETSN---------------- 2453
Cdd:pfam12030 307 CR-LGFDKEWFASQVLE-------------------------------NIPDWAPPLLSYPDSNvrsetedflqeelfsh 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907203398 2454 ---------------------------GYFLERS---HSARMTLAKACELCPE 2476
Cdd:pfam12030 355 emgpdpqfrlreaarrlgiacleylrgTYVLRRSqveRSAVETLQRVIELCPE 407
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1557-1953 |
9.02e-80 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 266.62 E-value: 9.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1557 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDvdddmsgdekqdnesnvdprddvfgypqqfedkpplskteDR 1636
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSED----------------------------------------SR 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1637 KEYNIGVLRHLQVIFGHLA-ASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKA---LGHPAMLSK 1712
Cdd:pfam00443 41 YNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1713 VLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLL------DSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 1786
Cdd:pfam00443 121 LFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1787 KKLPPVLAIQLKRFDYDweRECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVnpesqliqqneqsesekagstKYRLV 1866
Cdd:pfam00443 201 SRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ---------------------DYRLV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1867 GVLVHSGQASGGHYYSYIIQrnggdGEKNRWYKFDDGDVTECKMDDDEEMknqcfggeymgevfdhmmkrmsyrrqkrwW 1946
Cdd:pfam00443 258 AVVVHSGSLSSGHYIAYIKA-----YENNRWYKFDDEKVTEVDEETAVLS-----------------------------S 303
|
....*..
gi 1907203398 1947 NAYILFY 1953
Cdd:pfam00443 304 SAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1680-1954 |
7.10e-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: 7.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1680 LREQHDALEFFNSLVDSLDEALKALG--------HPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI----RNH 1747
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSkrtsdsssLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1748 QNLLDSLEQYVKGDLLEGANAYHCEKCnKKVDTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPY 1827
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1828 TVAGVAKLEGDNvnpesqliqqneqsesekaGSTKYRLVGVLVHSGQ-ASGGHYYSYIIqrnggDGEKNRWYKFDDGDVT 1906
Cdd:cd02257 177 LSEGEKDSDSDN-------------------GSYKYELVAVVVHSGTsADSGHYVAYVK-----DPSDGKWYKFNDDKVT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907203398 1907 ECKMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkRWWNAYILFYE 1954
Cdd:cd02257 233 EVSEEEVLEFGS-------------------------LSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1558-1954 |
9.89e-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: 9.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1558 GLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDekQDNESNvdprddvfgypqqfedkpplsktedrk 1637
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPD--KPHEPQ--------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1638 eyniGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLwgepvNLREQHDALEFFNSLVDSLDEALKALGHP---AMLSKVL 1714
Cdd:cd02668 52 ----TIIDQLQLIFAQLQFGNRSVVDPSGFVKALGL-----DTGQQQDAQEFSKLFLSLLEAKLSKSKNPdlkNIVQDLF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1715 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1794
Cdd:cd02668 123 RGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1795 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVagvaklegdnvnpesqliqqnEQSEsekaGSTKYRLVGVLVHSGQ 1874
Cdd:cd02668 203 FQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA---------------------ESDE----GSYVYELSGVLIHQGV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1875 -ASGGHYYSYIIQRNGGdgeknRWYKFDDGDVTE-----CKMDDDEEMKNQCFGgeymgevfDHMMKRMSYRrqkrwwNA 1948
Cdd:cd02668 258 sAYSGHYIAHIKDEQTG-----EWYKFNDEDVEEmpgkpLKLGNSEDPAKPRKS--------EIKKGTHSSR------TA 318
|
....*.
gi 1907203398 1949 YILFYE 1954
Cdd:cd02668 319 YMLVYK 324
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1555-2001 |
2.61e-48 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 190.08 E-value: 2.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1555 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEgtgsdvdddmsgdekQDNEsnvDPRDDV-------FgYPQQFEDK 1627
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP---------------TDHP---RGRDSValalqrlF-YNLQTGEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1628 PpLSKTEdrkeynigvlrhLQVIFGhlaasrlqyyvprgfwkqfrlWGEPVNLReQHDALEFFNSLVDSLDEALKALGHP 1707
Cdd:COG5077 253 P-VDTTE------------LTRSFG---------------------WDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1708 AMLSKVLGGSFadqKICQGCPHR-YECE--ESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKcNKKVDTVKRL 1784
Cdd:COG5077 298 NALNGIFVGKM---KSYIKCVNVnYESArvEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1785 LIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYtvagvaklegdnVNPESqliqqnEQSESEKAgstKYR 1864
Cdd:COG5077 374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF------------LDRDA------DKSENSDA---VYV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1865 LVGVLVHSGQASGGHYYSYIiqRNGGDGeknRWYKFDDGDVTECKMdddEEMKNQCFGGEYMGEVfdhmmKRMSYRRQKR 1944
Cdd:COG5077 433 LYGVLVHSGDLHEGHYYALL--KPEKDG---RWYKFDDTRVTRATE---KEVLEENFGGDHPYKD-----KIRDHSGIKR 499
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907203398 1945 WWNAYILFYERMDTIghdDEVIRYISEIAITTRPHQIVMPSAIERSVRKQNVQFMHN 2001
Cdd:COG5077 500 FMSAYMLVYLRKSML---DDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHL 553
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1558-1912 |
8.13e-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: 8.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1558 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNvdprddvfgypqqfedkpplsktedrk 1637
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLL-------------SREHSKDCCNE--------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1638 eyNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEA-------LKALGHPA-- 1708
Cdd:cd02661 43 --GFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKAcldrfkkLKAVDPSSqe 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1709 --MLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 1786
Cdd:cd02661 121 ttLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1787 KKLPPVLAIQLKRFDYDWERecaiKFNDYFEFPRELDMEPYTVagvaklegdnvnpesqliqqneqseSEKAGSTKYRLV 1866
Cdd:cd02661 201 HRAPNVLTIHLKRFSNFRGG----KINKQISFPETLDLSPYMS-------------------------QPNDGPLKYKLY 251
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907203398 1867 GVLVHSG-QASGGHYYSYIIQRNGgdgeknRWYKFDDGDVTECKMDD 1912
Cdd:cd02661 252 AVLVHSGfSPHSGHYYCYVKSSNG------KWYNMDDSKVSPVSIET 292
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1682-1954 |
1.62e-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: 144.74 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1682 EQHDALEFFNSLVDSLDealkalghpAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI------RNHQNLLDSLE 1755
Cdd:cd02674 21 DQQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1756 QYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYTVAgvak 1834
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPlNDLDLTPYVDT---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1835 legdnvnpesqliqqneqseSEKAGSTKYRLVGVLVHSGQASGGHYYSYIiqrngGDGEKNRWYKFDDGDVTecKMDDDE 1914
Cdd:cd02674 166 --------------------RSFTGPFKYDLYAVVNHYGSLNGGHYTAYC-----KNNETNDWYKFDDSRVT--KVSESS 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907203398 1915 EMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYE 1954
Cdd:cd02674 219 VVSS----------------------------SAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1558-1907 |
1.52e-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: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1558 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgSDvDDDMSGDEKQDNESNVDPRDDVFgypQQFedkpplSKTEDRK 1637
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL------SD-RHSCTCLSCSPNSCLSCAMDEIF---QEF------YYSGDRS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1638 EYnigvlrhlqvifghlAASRLQYyvprGFWKQFRlwgepvNL--REQHDALEFFNSLVDSLDE-ALKALGHPAMLS--- 1711
Cdd:cd02660 66 PY---------------GPINLLY----LSWKHSR------NLagYSQQDAHEFFQFLLDQLHThYGGDKNEANDEShcn 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1712 ----KVLGGSFADQKICQGCPHRYECEESFTTLNVDIRN---------------HQNLLDSLEQYVKGDLLeGANAYHCE 1772
Cdd:cd02660 121 ciihQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNkstpswalgesgvsgTPTLSDCLDRFTRPEKL-GDFAYKCS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1773 KCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTVAGvaklegdnvnpesqliQQNEQ 1852
Cdd:cd02660 200 GCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTSSS----------------IGDTQ 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907203398 1853 SESEKAGSTKYRLVGVLVHSGQASGGHYYSYIIQRNGgdgeknRWYKFDDGDVTE 1907
Cdd:cd02660 263 DSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDG------QWFKFDDAMITR 311
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1558-1954 |
7.72e-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: 7.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1558 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNVdprddvfgypqqfedkpplsktedrk 1637
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVL-------------SLNLPRLGDSQS-------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1638 eynigVLRHLQVIFGHLAASRLQYY-VPRGFWKQfrLWGEPVNLREQHDALEFFNSLVDSLDealkalghpAMLSKVLGG 1716
Cdd:cd02664 42 -----VMKKLQLLQAHLMHTQRRAEaPPDYFLEA--SRPPWFTPGSQQDCSEYLRYLLDRLH---------TLIEKMFGG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1717 SFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDsleQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQ 1796
Cdd:cd02664 106 KLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDLLN---YFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1797 LKRFDYDWERECAIKFNDYFEFPRELDMePYTVAgvaklegdNVNPESQLIQQNEQSESEKAGSTK---YRLVGVLVHSG 1873
Cdd:cd02664 183 LLRFSYDQKTHVREKIMDNVSINEVLSL-PVRVE--------SKSSESPLEKKEEESGDDGELVTRqvhYRLYAVVVHSG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1874 QAS-GGHYYSYIiqRNGGDGEKNR-----------------WYKFDDGDVTECKMdddEEMKNqcfggeyMGEVFDHMmk 1935
Cdd:cd02664 254 YSSeSGHYFTYA--RDQTDADSTGqecpepkdaeendesknWYLFNDSRVTFSSF---ESVQN-------VTSRFPKD-- 319
|
410
....*....|....*....
gi 1907203398 1936 rmsyrrqkrwwNAYILFYE 1954
Cdd:cd02664 320 -----------TPYILFYE 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1683-1954 |
1.37e-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: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1683 QHDALEFFNSLVDSLDEALKalghpamlsKVLGGSFADQKICQGCPHRYECEESFTTLN----VDIRNHQNLLDSLEQYV 1758
Cdd:cd02667 51 QQDSHELLRYLLDGLRTFID---------SIFGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKSECSIESCLKQFT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1759 KGDLLEGANAYHCEKCNKkvdTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTVAgvaklegd 1838
Cdd:cd02667 122 EVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFCDP-------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1839 nvnpesqliqqnEQSESEKAGSTKYRLVGVLVHSGQASGGHYYSYI----------------IQRNGGDGEKNRWYKFDD 1902
Cdd:cd02667 190 ------------KCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVkvrppqqrlsdltkskPAADEAGPGSGQWYYISD 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907203398 1903 GDVTEckMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrwwnAYILFYE 1954
Cdd:cd02667 258 SDVRE--VSLEEVLKSE----------------------------AYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1683-1954 |
4.26e-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: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1683 QHDALEFFNSLVDSLDEALKALG-----------------HPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIR 1745
Cdd:cd02663 65 HQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1746 NHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDME 1825
Cdd:cd02663 145 QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1826 PYTvagvakleGDNVNPESqliqqneqsesekagstKYRLVGVLVHSGQ-ASGGHYYSyIIQRNGGdgeknrWYKFDDGD 1904
Cdd:cd02663 225 NTT--------DDAENPDR-----------------LYELVAVVVHIGGgPNHGHYVS-IVKSHGG------WLLFDDET 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1905 VTecKMDDdeemknqcfggEYMGEVFDHmmkrmsyrrQKRWWNAYILFYE 1954
Cdd:cd02663 273 VE--KIDE-----------NAVEEFFGD---------SPNQATAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1558-1954 |
1.21e-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: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1558 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvddDMSGDEKQDNESNVDPrddVFGYPQQFEDkppLSKTEDRk 1637
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALK-----------NYNPARRGANQSSDNL---TNALRDLFDT---MDKKQEP- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1638 eynigvlrhlqvifghlaasrlqyYVPRGFWKQFRL----WGEP--VNLREQHDALEFFNSLVDSLDEALK-ALGHPAML 1710
Cdd:cd02657 63 ------------------------VPPIEFLQLLRMafpqFAEKqnQGGYAQQDAEECWSQLLSVLSQKLPgAGSKGSFI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1711 SKVLGGSFADQKICQGCPHRYECE-ESFTTLNVDIrNHQNLLDSLEQYVKgDLLEGANAYHCEKCNKKVDTVKRLLIKKL 1789
Cdd:cd02657 119 DQLFGIELETKMKCTESPDEEEVStESEYKLQCHI-SITTEVNYLQDGLK-KGLEEEIEKHSPTLGRDAIYTKTSRISRL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1790 PPVLAIQLKRFDydWERECAI--KFNDYFEFPRELDMEPYTvagvaklegdnvnpesqliqqneqsesekAGSTKYRLVG 1867
Cdd:cd02657 197 PKYLTVQFVRFF--WKRDIQKkaKILRKVKFPFELDLYELC-----------------------------TPSGYYELVA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1868 VLVHSGQ-ASGGHYYSYIIQRNGgdgekNRWYKFDDGDVTECKMDDDEEMKNqcfGGEYmgevfdHMmkrmsyrrqkrww 1946
Cdd:cd02657 246 VITHQGRsADSGHYVAWVRRKND-----GKWIKFDDDKVSEVTEEDILKLSG---GGDW------HI------------- 298
|
....*...
gi 1907203398 1947 nAYILFYE 1954
Cdd:cd02657 299 -AYILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1558-1918 |
1.34e-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: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1558 GLKNAGATCYMNSVIQQLYMIPSirngilaiegtgsdVDDDMSGDEKQDNESNVDPRDDvfgYPQQF----------EDK 1627
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPS--------------FQWRYDDLENKFPSDVVDPAND---LNCQLikladgllsgRYS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1628 PPLSKTEDRKEYNIGVLrhlqvifghlaasrlqyyvPRGFwKqfRLWGEpvNLRE-----QHDALEFFNSLVDSLDEALK 1702
Cdd:cd02658 64 KPASLKSENDPYQVGIK-------------------PSMF-K--ALIGK--GHPEfstmrQQDALEFLLHLIDKLDRESF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1703 ALG--HPAMLSKVlggsFADQKI-CQGCPHRYECEESFTTLNVDIRNH--------------QNLLDSLEQYVKGDLLEg 1765
Cdd:cd02658 120 KNLglNPNDLFKF----MIEDRLeCLSCKKVKYTSELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETIE- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1766 anaYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDY--DWErecaikfndyfefPRELDMEpytvagvakLEGDNVnpe 1843
Cdd:cd02658 195 ---DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-------------PKKLDVP---------IDVPEE--- 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907203398 1844 sqliqqneqsesekAGSTKYRLVGVLVHSG-QASGGHYYSYIIQRnggDGEKNRWYKFDDGDVteCKMDDDEEMKN 1918
Cdd:cd02658 247 --------------LGPGKYELIAFISHKGtSVHSGHYVAHIKKE---IDGEGKWVLFNDEKV--VASQDPPEMKK 303
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1533-1905 |
3.78e-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: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1533 ITTCEALtewEYLPPvgprppkgFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSgdekqdnesnvd 1612
Cdd:cd02671 12 ATSCEKR---ENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQS------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1613 prddvfgypqQFEDKPPLSKTEDRKEYNIGVLRHLQVIfghlaASRLQYYvprgfwkqfrlwgepvnlrEQHDALEFFNS 1692
Cdd:cd02671 69 ----------SFLLNPEKYNDELANQAPRRLLNALREV-----NPMYEGY-------------------LQHDAQEVLQC 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1693 LVDSLDEalkalghpaMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQ-------------------NLLDS 1753
Cdd:cd02671 115 ILGNIQE---------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESElskseesseispdpktemkTLKWA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1754 LEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAI----KFNDYFEFPRELDMEpytv 1829
Cdd:cd02671 186 ISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLE---- 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907203398 1830 agvaklegdnvnpesqliqqnEQSESEKagSTKYRLVGVLVHSG-QASGGHYYSYIiqrnggdgeknRWYKFDDGDV 1905
Cdd:cd02671 262 ---------------------EWSTKPK--NDVYRLFAVVMHSGaTISSGHYTAYV-----------RWLLFDDSEV 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1558-1955 |
9.52e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 83.31 E-value: 9.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1558 GLKNAGATCYMNSVIQQL-YMIPSIRNGILAIEGTGSDVDDDMSGDEKQDNE-------SNVDPRDDvfgypQQFEDKPP 1629
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKNVIRKPEPDLNQeealklfTALWSSKE-----HKVGWIPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1630 LSKTEDRKEYnigvlrhLQVIFGHLAASRLqyyvprgfwKQFRLWGEPVNLREQHDALEFFNSLVDSLdealkalghpam 1709
Cdd:COG5533 76 MGSQEDAHEL-------LGKLLDELKLDLV---------NSFTIRIFKTTKDKKKTSTGDWFDIIIEL------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1710 lskvlggsfadqkicqgcPHRYECEESFTTlnvdirnhQNLLDSLEQYVkgDLLEGANAyhceKCNKKVDTVKRLL---- 1785
Cdd:COG5533 128 ------------------PDQTWVNNLKTL--------QEFIDNMEELV--DDETGVKA----KENEELEVQAKQEyevs 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1786 IKKLPPVLAIQLKRFDYDwerecaikfndyfefpreldmepytvAGVAKLEgDNVNPESQLIQQNEQSeSEKAGSTKYRL 1865
Cdd:COG5533 176 FVKLPKILTIQLKRFANL--------------------------GGNQKID-TEVDEKFELPVKHDQI-LNIVKETYYDL 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1866 VGVLVHSGQASGGHYYSYIIQrnggdgeKNRWYKFDDGDVTECKMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrw 1945
Cdd:COG5533 228 VGFVLHQGSLEGGHYIAYVKK-------GGKWEKANDSDVTPVSEEEAINEKAK-------------------------- 274
|
410
....*....|
gi 1907203398 1946 wNAYILFYER 1955
Cdd:COG5533 275 -NAYLYFYER 283
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1557-1907 |
1.13e-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: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1557 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMsGDEKQDNESNVDPRDdvFGYPQQFedkpplsktedr 1636
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDY-PTERRIGGREVSRSE--LQRSNQF------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1637 keynigvLRHLQVIFGHLAASRLQYYVPRGfwkqfrlwgEPVNLR-EQHDALEFFNSLVDSLDEALKALG-HPAMLSKVL 1714
Cdd:cd02666 67 -------VYELRSLFNDLIHSNTRSVTPSK---------ELAYLAlRQQDVTECIDNVLFQLEVALEPISnAFAGPDTED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1715 GGSFADQ-------KICQ--------GCPHRYECEESFTTLNVDIR---------NH-QNLLDSLEQYVKGDLLEganay 1769
Cdd:cd02666 131 DKEQSDLikrlfsgKTKQqlvpesmgNQPSVRTKTERFLSLLVDVGkkgreivvlLEpKDLYDALDRYFDYDSLT----- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1770 hcekcnkkvdtvkrllikKLPPVLAIQLKrfdydwerecaikfNDYFEFPRELDMEPYT----VAGVAKLEGDNVNPESQ 1845
Cdd:cd02666 206 ------------------KLPQRSQVQAQ--------------LAQPLQRELISMDRYElpssIDDIDELIREAIQSESS 253
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907203398 1846 LIQQ--------NEQSESEKAG--STKYRLVGVLVHSGQASGGHYYSYIiqrngGDGEKNRWYKFDDGDVTE 1907
Cdd:cd02666 254 LVRQaqnelaelKHEIEKQFDDlkSYGYRLHAVFIHRGEASSGHYWVYI-----KDFEENVWRKYNDETVTV 320
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1669-1912 |
1.72e-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: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1669 KQFRLWGEpvNLREQHDALEFFNSLVDSLDEALKalgHPamlskvLGGSFADQKICQGCPH----RYECeESFTTLNV-- 1742
Cdd:cd02662 22 PSLIEYLE--EFLEQQDAHELFQVLLETLEQLLK---FP------FDGLLASRIVCLQCGEsskvRYES-FTMLSLPVpn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1743 -DIRNHQNLLDSLEQYVKGDLLEGanaYHCEKCnkkvdtvkRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRE 1821
Cdd:cd02662 90 qSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1822 LDmepytvagvaklegdnvnpesqliqqneqsesekagSTKYRLVGVLVHSGQASGGHYYSY----IIQRNGGDGE---- 1893
Cdd:cd02662 158 LP------------------------------------KVLYRLRAVVVHYGSHSSGHYVCYrrkpLFSKDKEPGSfvrm 201
|
250 260
....*....|....*....|....*.
gi 1907203398 1894 -------KNRWYKFDDGDVTECKMDD 1912
Cdd:cd02662 202 regpsstSHPWWRISDTTVKEVSESE 227
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1683-1923 |
6.01e-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: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1683 QHDALEFFNSLVDSLDEALKALGHPAMLSK--------VLGGSFADQKICQGcpHRYECEESFTTLNVDIRNHQNLLDSL 1754
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEksknpmvqLFYGTFLTEGVLEG--KPFCNCETFGQYPLQVNGYGNLHECL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1755 E-QYVKGDLlEGANAYHCEKCNKkvdtvkRLLIKKLPPVLAIQLKRFDYDWERECaiKFNDYFEFPRELDMEPYtvagva 1833
Cdd:cd02665 100 EaAMFEGEV-ELLPSDHSVKSGQ------ERWFTELPPVLTFELSRFEFNQGRPE--KIHDKLEFPQIIQQVPY------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1834 klegdnvnpesqliqqneqsesekagstkyRLVGVLVHSGQASGGHYYSYIIQRNggdgeKNRWYKFDDGDVTECkmdDD 1913
Cdd:cd02665 165 ------------------------------ELHAVLVHEGQANAGHYWAYIYKQS-----RQEWEKYNDISVTES---SW 206
|
250
....*....|
gi 1907203398 1914 EEMKNQCFGG 1923
Cdd:cd02665 207 EEVERDSFGG 216
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1750-1955 |
4.20e-12 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 71.84 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1750 LLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYT 1828
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPiDDLDLSGVE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1829 VAgvaklegdnvNPESQLIqqneqsesekagstkYRLVGVLVHSGQASGGHYYSYIiqRNGGDgekNRWYKFDDGDVTEc 1908
Cdd:COG5560 755 YM----------VDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYA--RNFAN---NGWYLFDDSRITE- 803
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907203398 1909 kMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYER 1955
Cdd:COG5560 804 -VDPEDSVTS----------------------------SAYVLFYRR 821
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1557-1902 |
4.35e-11 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 66.53 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1557 VGLKNAGATCYMNSVIQQLYMIPSIRNgiLAIEGTGSDVDD------------DMSGDEKQDN--ESNvdprddvfgypq 1622
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRN--LALSHLATECLKehcllcelgflfDMLEKAKGKNcqASN------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1623 qfedkppLSKTED--RKEYNIGVLRHLQVIFGHLAASRL-QYyvprgfWKQFRLwgepvnlrEQ--HDALEFFNSLVDSl 1697
Cdd:pfam13423 67 -------FLRALSsiPEASALGLLDEDRETNSAISLSSLiQS------FNRFLL--------DQlsSEENSTPPNPSPA- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1698 dealkalghPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLN------VDIRNHQNLLDSLEQYVKGDLL-EGANAYH 1770
Cdd:pfam13423 125 ---------ESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDliyprkPSSNNKKPPNQTFSSILKSSLErETTTKAW 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1771 CEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWEREcaIKFNDYfeFPRELDMepytvagvaklegdnvnpesqliqQN 1850
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL--WKTPGW--LPPEIGL------------------------TL 247
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907203398 1851 EQSESEKAGSTKYRLVGVLVH-SGQASGGHYYSYI--IQRNGGDGEKNRWYKFDD 1902
Cdd:pfam13423 248 SDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVkvADSELEDPTESQWYLFND 302
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1543-1908 |
6.56e-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: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1543 EYLPpvgprppkGFVGLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEkqdnesnvdprddvfgYPQ 1622
Cdd:cd02669 114 PYLP--------GFVGLNNIKNNDYANVIIQALSHVKPIRNFFL-------------LYEN----------------YEN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1623 QFEDKPPLSKTED---RKEYNIGVLRhlqvifGHLAASRLQYYVPRGFWKQFRLwgepvnlREQHDALEFFNSLVDSLde 1699
Cdd:cd02669 157 IKDRKSELVKRLSeliRKIWNPRNFK------GHVSPHELLQAVSKVSKKKFSI-------TEQSDPVEFLSWLLNTL-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1700 alkalgHPAmlskvLGGSFAD-----QKICQG---------CPHRYECEES----------------FTTLNVDIRN--- 1746
Cdd:cd02669 222 ------HKD-----LGGSKKPnssiiHDCFQGkvqietqkiKPHAEEEGSKdkffkdsrvkktsvspFLLLTLDLPPppl 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1747 --HQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVdtvKRLLIKKLPPVLAIQLKRFDYdwerecaikfNDYF-------- 1816
Cdd:cd02669 291 fkDGNEENIIPQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSK----------NNFFkeknptiv 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1817 EFPRELDMEPYTVAgvaklegdnvnpeSQLIQQNEqsesekagSTKYRLVGVLVHSGQASGGHYYSYIIQRNGGdgekNR 1896
Cdd:cd02669 358 NFPIKNLDLSDYVH-------------FDKPSLNL--------STKYNLVANIVHEGTPQEDGTWRVQLRHKST----NK 412
|
410
....*....|..
gi 1907203398 1897 WYKFDDGDVTEC 1908
Cdd:cd02669 413 WFEIQDLNVKEV 424
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1682-1954 |
6.19e-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: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1682 EQHDALEFFNSLVDSLDealkalgHPAMLSKVlggsfadqKICQGcPHRYECEESFttlnVDIRNHQNLLDSLEQyVKGD 1761
Cdd:cd02670 22 EQQDPEEFFNFITDKLL-------MPLLEPKV--------DIIHG-GKKDQDDDKL----VNERLLQIPVPDDDD-GGGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1762 LLEganayHCEKC--NKKVdtvkrllIKKLPPVLAIQLKRfdYDWERECAIKFNDYFEFPRELDMePYTVAGvAKLEGDN 1839
Cdd:cd02670 81 TLE-----QCLEQyfNNSV-------FAKAPSCLIICLKR--YGKTEGKAQKMFKKILIPDEIDI-PDFVAD-DPRACSK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1840 VNPESQLIQQNEQSeSEKAGSTKYRLVGVLVHSGQA-SGGHYYSYI------IQRNGGDGEKNRWYKFDDgdvteckMDD 1912
Cdd:cd02670 145 CQLECRVCYDDKDF-SPTCGKFKLSLCSAVCHRGTSlETGHYVAFVrygsysLTETDNEAYNAQWVFFDD-------MAD 216
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907203398 1913 DEemknqcfGGEYmgeVFDHMMKRmsyrrqkRWWNAYILFYE 1954
Cdd:cd02670 217 RD-------GVSN---GFNIPAAR-------LLEDPYMLFYQ 241
|
|
| Ubl_UBP24 |
cd17065 |
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ... |
900-964 |
2.41e-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: 2.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907203398 900 DDLEVWSHTNDTIGSVRRCILNRIKANVAHtkIELFVGGELIDPGDDRKLIGQLNLKDKSLITAK 964
Cdd:cd17065 17 QEFTLEVHSNETLGSVRQKIAERLNCPVDQ--VQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1721-1907 |
2.32e-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: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1721 QKICQGCPHRYECEESFTTLNVDIRNHQNL-----LDSLEQYVKGDL-LEGANAYHCEKCNKKVDTVKRLLIKKLPP--- 1791
Cdd:cd02672 81 SQDQLGTPFSCGTSRNSVSLLYTLSLPLGStktskESTFLQLLKRSLdLEKVTKAWCDTCCKYQPLEQTTSIRHLPDill 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203398 1792 -VLAIQLKRFDydweRECAIKFNDYFEFpreLDMEPytvaGVAKLEGDNVNPESQLIQQNeqsesekagSTKYRLVGVLV 1870
Cdd:cd02672 161 lVLVINLSVTN----GEFDDINVVLPSG---KVMQN----KVSPKAIDHDKLVKNRGQES---------IYKYELVGYVC 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907203398 1871 H-SGQASGGHYYSYIIQRNgGDGEKNRWYKFDDGDVTE 1907
Cdd:cd02672 221 EiNDSSRGQHNVVFVIKVN-EESTHGRWYLFNDFLVTP 257
|
|
| |
