|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1764-2179 |
2.25e-120 |
|
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: 384.30 E-value: 2.25e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1764 VGMKNDGGTCYMNAMIQQLVHVPGLSRELIALqnidPQLRWGDNTAALLCELQRVFAQLNFAQCQAIVPEGLWKEFRFeP 1843
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI----PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSF-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1844 DMPLNTKQHHDAIDFYSILLDKCDNVLKKLELPPLFQNRFFGKYSYEKICYGCWHRYkSPDEEFNCISLALSG-DNLEEA 1922
Cdd:cd02659 78 WDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHES-EREEYFLDLQVAVKGkKNLEES 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1923 LENFLAAHVMEGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTYDLVNNMIRKDNQLFRFPFEIDMTPYMTTSRH 2002
Cdd:cd02659 157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2003 VPDehvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesaqkkmfrrhrsstmrlsqsfantsGFDTPS 2082
Cdd:cd02659 237 KKE-----------------------------------------------------------------------GDSEKK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2083 QQKPLIYELVGVLAHSGIATAGHYYSFIKERReefrdsphYNKWHHINDMIVSPMSFNNIEDLWYGGTFTQEGVFIGLDE 2162
Cdd:cd02659 246 DSESYIYELHGVLVHSGDAHGGHYYSYIKDRD--------DGKWYKFNDDVVTPFDPNDAEEECFGGEETQKTYDSGPRA 317
|
410
....*....|....*..
gi 484399540 2163 RVRHWNAYVLFYEKKRD 2179
Cdd:cd02659 318 FKRTTNAYMLFYERKSP 334
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1764-2174 |
8.06e-43 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 160.30 E-value: 8.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1764 VGMKNDGGTCYMNAMIQQLVHVPGLSRELIALQNIDPQLRWgDNTAALLCELQRVFAQLNFAQCQ-AIVPEGLWKEFR-F 1841
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRY-NKDINLLCALRDLFKALQKNSKSsSVSPKMFKKSLGkL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1842 EPDmpLNTKQHHDAIDFYSILLDKCDNVLKKLEL---PPLFQNRFFGKYSYEKICYGCWHRYKSPDEEFNcISLALSGD- 1917
Cdd:pfam00443 80 NPD--FSGYKQQDAQEFLLFLLDGLHEDLNGNHStenESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD-LSLPIPGDs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1918 ------NLEEALENFLAAHVMEGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTYDlvNNMIRKDNQLFRFPFEI 1991
Cdd:pfam00443 157 aelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1992 DMTPYMTTSrhvpdehvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesaqkkmfrrhrsstmrlsqs 2071
Cdd:pfam00443 235 DLSRYLAEE----------------------------------------------------------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2072 fantsgfDTPSQQKPLIYELVGVLAHSGIATAGHYYSFIKERREefrdsphyNKWHHINDMIVSPmsfnniedlwyggtf 2151
Cdd:pfam00443 244 -------LKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYEN--------NRWYKFDDEKVTE--------------- 293
|
410 420
....*....|....*....|...
gi 484399540 2152 tqegvfIGLDERVRHWNAYVLFY 2174
Cdd:pfam00443 294 ------VDEETAVLSSSAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1764-2194 |
5.02e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 118.05 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1764 VGMKNDGGTCYMNAMIQQLVHVPGLSRELIALQNIDPQlrwGDNTAALLceLQRVFAQLNFAQCQAIVPEgLWKEFRFEP 1843
Cdd:COG5077 194 VGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPR---GRDSVALA--LQRLFYNLQTGEEPVDTTE-LTRSFGWDS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1844 DMPLntkQHHDAIDFYSILLDKCDNVLKKLELPPLFQNRFFGKY-SYekicYGCWHR--YKSPDEEFNCISLALSG-DNL 1919
Cdd:COG5077 268 DDSF---MQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMkSY----IKCVNVnyESARVEDFWDIQLNVKGmKNL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1920 EEALENFLAAHVMEGENAYHCEK---CDEKKTTLnrtsFLELPSTMTIQLKRFTYDLVNNMIRKDNQLFRFPFEIDMTPY 1996
Cdd:COG5077 341 QESFRRYIQVETLDGDNRYNAEKhglQDAKKGVI----FESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1997 MTTsrhvpdehvqdlfdemlygngEADEapspphkngvaekpnlgsgsastpslesaqkkmfrrhrsstmrlsqsfants 2076
Cdd:COG5077 417 LDR---------------------DADK---------------------------------------------------- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2077 gfdtpSQQKPLIYELVGVLAHSGIATAGHYYSFIKERREefrdsphyNKWHHINDMIVSPMSFNNIEDLWYGGTFTQEGV 2156
Cdd:COG5077 424 -----SENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKD--------GRWYKFDDTRVTRATEKEVLEENFGGDHPYKDK 490
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 484399540 2157 FIGLDERVRHWNAYVLFYEKKRDEPTAL-------IPRHIIDRLN 2194
Cdd:COG5077 491 IRDHSGIKRFMSAYMLVYLRKSMLDDLLnpvaavdIPPHVEEVLS 535
|
|
| UBA |
smart00165 |
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
78-113 |
4.59e-06 |
|
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.
Pssm-ID: 197551 [Multi-domain] Cd Length: 37 Bit Score: 45.56 E-value: 4.59e-06
10 20 30
....*....|....*....|....*....|....*.
gi 484399540 78 YQDNQDMLITMGFKSEEIDTALRLSNNDVEKAIQYL 113
Cdd:smart00165 1 DEEKIDQLLEMGFSREEALKALRAANGNVERAAEYL 36
|
|
| UBA2_spUBP14_like |
cd14297 |
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
84-113 |
3.70e-05 |
|
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.
Pssm-ID: 270483 [Multi-domain] Cd Length: 39 Bit Score: 42.85 E-value: 3.70e-05
10 20 30
....*....|....*....|....*....|
gi 484399540 84 MLITMGFKSEEIDTALRLSNNDVEKAIQYL 113
Cdd:cd14297 6 QLVDMGFTEAQARKALRKTNNNVERAVDWL 35
|
|
| UBA |
pfam00627 |
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
77-113 |
3.81e-03 |
|
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.
Pssm-ID: 395502 [Multi-domain] Cd Length: 37 Bit Score: 37.03 E-value: 3.81e-03
10 20 30
....*....|....*....|....*....|....*..
gi 484399540 77 QYQDNQDMLITMGFKSEEIDTALRLSNNDVEKAIQYL 113
Cdd:pfam00627 1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1764-2179 |
2.25e-120 |
|
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: 384.30 E-value: 2.25e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1764 VGMKNDGGTCYMNAMIQQLVHVPGLSRELIALqnidPQLRWGDNTAALLCELQRVFAQLNFAQCQAIVPEGLWKEFRFeP 1843
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI----PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSF-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1844 DMPLNTKQHHDAIDFYSILLDKCDNVLKKLELPPLFQNRFFGKYSYEKICYGCWHRYkSPDEEFNCISLALSG-DNLEEA 1922
Cdd:cd02659 78 WDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHES-EREEYFLDLQVAVKGkKNLEES 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1923 LENFLAAHVMEGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTYDLVNNMIRKDNQLFRFPFEIDMTPYMTTSRH 2002
Cdd:cd02659 157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2003 VPDehvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesaqkkmfrrhrsstmrlsqsfantsGFDTPS 2082
Cdd:cd02659 237 KKE-----------------------------------------------------------------------GDSEKK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2083 QQKPLIYELVGVLAHSGIATAGHYYSFIKERReefrdsphYNKWHHINDMIVSPMSFNNIEDLWYGGTFTQEGVFIGLDE 2162
Cdd:cd02659 246 DSESYIYELHGVLVHSGDAHGGHYYSYIKDRD--------DGKWYKFNDDVVTPFDPNDAEEECFGGEETQKTYDSGPRA 317
|
410
....*....|....*..
gi 484399540 2163 RVRHWNAYVLFYEKKRD 2179
Cdd:cd02659 318 FKRTTNAYMLFYERKSP 334
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1764-2174 |
8.06e-43 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 160.30 E-value: 8.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1764 VGMKNDGGTCYMNAMIQQLVHVPGLSRELIALQNIDPQLRWgDNTAALLCELQRVFAQLNFAQCQ-AIVPEGLWKEFR-F 1841
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRY-NKDINLLCALRDLFKALQKNSKSsSVSPKMFKKSLGkL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1842 EPDmpLNTKQHHDAIDFYSILLDKCDNVLKKLEL---PPLFQNRFFGKYSYEKICYGCWHRYKSPDEEFNcISLALSGD- 1917
Cdd:pfam00443 80 NPD--FSGYKQQDAQEFLLFLLDGLHEDLNGNHStenESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD-LSLPIPGDs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1918 ------NLEEALENFLAAHVMEGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTYDlvNNMIRKDNQLFRFPFEI 1991
Cdd:pfam00443 157 aelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1992 DMTPYMTTSrhvpdehvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesaqkkmfrrhrsstmrlsqs 2071
Cdd:pfam00443 235 DLSRYLAEE----------------------------------------------------------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2072 fantsgfDTPSQQKPLIYELVGVLAHSGIATAGHYYSFIKERREefrdsphyNKWHHINDMIVSPmsfnniedlwyggtf 2151
Cdd:pfam00443 244 -------LKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYEN--------NRWYKFDDEKVTE--------------- 293
|
410 420
....*....|....*....|...
gi 484399540 2152 tqegvfIGLDERVRHWNAYVLFY 2174
Cdd:pfam00443 294 ------VDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1765-2175 |
5.85e-38 |
|
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: 144.16 E-value: 5.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLVHvpglsrelialqnidpqlrwgdntaallcelqrvfaqlnfaqcqaivpeglwkefrfepd 1844
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1845 mplntkQHHDAIDFYSILLDKCDNVLKKL--------ELPPLFQNRFFGKYSYEKICYGCWHRYKSpDEEFNCISLALSG 1916
Cdd:cd02257 21 ------EQQDAHEFLLFLLDKLHEELKKSskrtsdssSLKSLIHDLFGGKLESTIVCLECGHESVS-TEPELFLSLPLPV 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1917 D-----NLEEALENFLAAHVMEGENAYHCEKCdEKKTTLNRTSFLELPSTMTIQLKRFTYDLvNNMIRKDNQLFRFPFEI 1991
Cdd:cd02257 94 KglpqvSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLEL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1992 DMTPYMTtsrhvpdehvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesaqkkmfrrhrsstmrlsqs 2071
Cdd:cd02257 172 DLSPYLS------------------------------------------------------------------------- 178
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2072 fanTSGFDTPSQQKPLIYELVGVLAHSG-IATAGHYYSFIKerreefrdSPHYNKWHHINDMIVSPMSFNNIEDLwyggt 2150
Cdd:cd02257 179 ---EGEKDSDSDNGSYKYELVAVVVHSGtSADSGHYVAYVK--------DPSDGKWYKFNDDKVTEVSEEEVLEF----- 242
|
410 420
....*....|....*....|....*
gi 484399540 2151 ftqegvfigldeRVRHWNAYVLFYE 2175
Cdd:cd02257 243 ------------GSLSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1765-2175 |
2.13e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 142.17 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLVHVPGLSR--------ELIALQNIDPQLRWGDNTAalLCELQRVFAQLNFAQCQAIVPEGLW 1836
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKavyecnstEDAELKNMPPDKPHEPQTI--IDQLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1837 KEFRfepdmpLNTKQHHDAIDFYSILLDKCDNVLKKL---ELPPLFQNRFFGKYSYEKICYGCWHRYKSPDEeFNCISLA 1913
Cdd:cd02668 79 KALG------LDTGQQQDAQEFSKLFLSLLEAKLSKSknpDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSK-FYELELQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1914 LSGD-NLEEALENFLAAHVMEGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTYDLVNNMIRKDNQLFRFPFEID 1992
Cdd:cd02668 152 LKGHkTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1993 MTPYMttsrhvpdehvqdlfdemlygngeadeAPSPPHKngvaekpnlgsgsastpslesaqkkmfrrhrsstmrlsqsf 2072
Cdd:cd02668 232 MGEYL---------------------------AESDEGS----------------------------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2073 antsgfdtpsqqkpLIYELVGVLAHSGI-ATAGHYYSFIKErreefrdsPHYNKWHHINDMIVSPMSFNNIEDlwyGGTF 2151
Cdd:cd02668 244 --------------YVYELSGVLIHQGVsAYSGHYIAHIKD--------EQTGEWYKFNDEDVEEMPGKPLKL---GNSE 298
|
410 420
....*....|....*....|....*.
gi 484399540 2152 TQEGVFIGLDERVRHW--NAYVLFYE 2175
Cdd:cd02668 299 DPAKPRKSEIKKGTHSsrTAYMLVYK 324
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1765-2174 |
1.27e-31 |
|
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: 127.39 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLVHVPGLSrelIALQNIDPQLRWGDNTAALLCELQRVFAQLNFAQCQAIVP-------EGLWK 1837
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLA---NYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPrifssnlKQISK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1838 EFRFepdmplntKQHHDAIDFYSILLDKCDNV----LKKLE-LPPLFQ-----NRFFGKYSYEKI----CYGCWHRYksp 1903
Cdd:cd02661 80 HFRI--------GRQEDAHEFLRYLLDAMQKAcldrFKKLKaVDPSSQettlvQQIFGGYLRSQVkclnCKHVSNTY--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1904 dEEFNCISLALSG-DNLEEALENFLAAHVMEGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTydlvNNMIRKDN 1982
Cdd:cd02661 149 -DPFLDLSLDIKGaDSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS----NFRGGKIN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1983 QLFRFPFEIDMTPYMTTSRHVpdehvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesaqkkmfrrhr 2062
Cdd:cd02661 224 KQISFPETLDLSPYMSQPNDG----------------------------------------------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2063 sstmrlsqsfantsgfdtpsqqkPLIYELVGVLAHSGIAT-AGHYYSFIKerreefrDSPhyNKWHHINDMIVSPMSFnn 2141
Cdd:cd02661 245 -----------------------PLKYKLYAVLVHSGFSPhSGHYYCYVK-------SSN--GKWYNMDDSKVSPVSI-- 290
|
410 420 430
....*....|....*....|....*....|...
gi 484399540 2142 iedlwyggtftqegvfigldERVRHWNAYVLFY 2174
Cdd:cd02661 291 --------------------ETVLSQKAYILFY 303
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1764-2194 |
5.02e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 118.05 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1764 VGMKNDGGTCYMNAMIQQLVHVPGLSRELIALQNIDPQlrwGDNTAALLceLQRVFAQLNFAQCQAIVPEgLWKEFRFEP 1843
Cdd:COG5077 194 VGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPR---GRDSVALA--LQRLFYNLQTGEEPVDTTE-LTRSFGWDS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1844 DMPLntkQHHDAIDFYSILLDKCDNVLKKLELPPLFQNRFFGKY-SYekicYGCWHR--YKSPDEEFNCISLALSG-DNL 1919
Cdd:COG5077 268 DDSF---MQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMkSY----IKCVNVnyESARVEDFWDIQLNVKGmKNL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1920 EEALENFLAAHVMEGENAYHCEK---CDEKKTTLnrtsFLELPSTMTIQLKRFTYDLVNNMIRKDNQLFRFPFEIDMTPY 1996
Cdd:COG5077 341 QESFRRYIQVETLDGDNRYNAEKhglQDAKKGVI----FESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1997 MTTsrhvpdehvqdlfdemlygngEADEapspphkngvaekpnlgsgsastpslesaqkkmfrrhrsstmrlsqsfants 2076
Cdd:COG5077 417 LDR---------------------DADK---------------------------------------------------- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2077 gfdtpSQQKPLIYELVGVLAHSGIATAGHYYSFIKERREefrdsphyNKWHHINDMIVSPMSFNNIEDLWYGGTFTQEGV 2156
Cdd:COG5077 424 -----SENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKD--------GRWYKFDDTRVTRATEKEVLEENFGGDHPYKDK 490
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 484399540 2157 FIGLDERVRHWNAYVLFYEKKRDEPTAL-------IPRHIIDRLN 2194
Cdd:COG5077 491 IRDHSGIKRFMSAYMLVYLRKSMLDDLLnpvaavdIPPHVEEVLS 535
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1765-2175 |
3.00e-23 |
|
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: 100.82 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLVHvpglsrelialqnidpqlrwgdntaallcelqrvfaqlnfaqcqaivpeglwkefrfepd 1844
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1845 mplntkQHHDAIDFYSILLDKCDNVLKKLelpplfqnrFFGKYSYEKICYGCwHRYKSPDEEFNCISLAL---SGD---- 1917
Cdd:cd02674 21 ------DQQDAQEFLLFLLDGLHSIIVDL---------FQGQLKSRLTCLTC-GKTSTTFEPFTYLSLPIpsgSGDapkv 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1918 NLEEALENFLAAHVMEGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTYDlvNNMIRKDNQLFRFPFEI-DMTPY 1996
Cdd:cd02674 85 TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPLNDlDLTPY 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1997 mttsrhvpdehvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesaqkkmfrrhrsstmrlsqsfants 2076
Cdd:cd02674 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2077 gFDTPSQQKPLIYELVGVLAHSGIATAGHYYSFIKerreefrdSPHYNKWHHINDMIVSPMSFNNIEDLwyggtftqegv 2156
Cdd:cd02674 163 -VDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCK--------NNETNDWYKFDDSRVTKVSESSVVSS----------- 222
|
410
....*....|....*....
gi 484399540 2157 figldervrhwNAYVLFYE 2175
Cdd:cd02674 223 -----------SAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1765-2175 |
1.78e-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 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: 95.25 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLVHVPGLSRELIALQnidpqLRWGDNTAALLCELQRVFAQLNFAQCQAIVPEglwkEFRFEPD 1844
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLN-----LPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPP----DYFLEAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1845 MP--LNTKQHHDAIDFYSILLDKCDnvlkklelpPLFQNRFFGKYSYEKICYGCwHRYKSPDEEFNCISLALSgdNLEEA 1922
Cdd:cd02664 72 RPpwFTPGSQQDCSEYLRYLLDRLH---------TLIEKMFGGKLSTTIRCLNC-NSTSARTERFRDLDLSFP--SVQDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1923 LENFLAAHVMEGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTYDlvnnmirkdnqlfrfpfeidmtpymttsrh 2002
Cdd:cd02664 140 LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYD------------------------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2003 vPDEHV-QDLFDEMLYgngeadeapspphkNGVAEKPnlgsgsastpslesaqkkmFRRHRSSTMRLSQSFANTSGFDTP 2081
Cdd:cd02664 190 -QKTHVrEKIMDNVSI--------------NEVLSLP-------------------VRVESKSSESPLEKKEEESGDDGE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2082 SQQKPLIYELVGVLAHSGIAT-AGHYYSFIK-----ERREEFRDSPHYNK-------WHHINDMIVSPMSFNNIEDlwyg 2148
Cdd:cd02664 236 LVTRQVHYRLYAVVVHSGYSSeSGHYFTYARdqtdaDSTGQECPEPKDAEendesknWYLFNDSRVTFSSFESVQN---- 311
|
410 420
....*....|....*....|....*..
gi 484399540 2149 gtftqegvfigLDERVRHWNAYVLFYE 2175
Cdd:cd02664 312 -----------VTSRFPKDTPYILFYE 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1765-2175 |
4.50e-19 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 90.14 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLVHVPGLsRELIalqnidpqlrwGDNTAALLCELQRvfaqlnfaqcqaivpeglwKEFRFepd 1844
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPAL-RELL-----------SETPKELFSQVCR-------------------KAPQF--- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1845 mplNTKQHHDAIDFYSILLDKCDNVLKKLelpplfqnrFFGKYSYEKICYGCwHRYKSPDEEFNCISL-----ALSGDNL 1919
Cdd:cd02667 47 ---KGYQQQDSHELLRYLLDGLRTFIDSI---------FGGELTSTIMCESC-GTVSLVYEPFLDLSLprsdeIKSECSI 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1920 EEALENFLAAHVMEGENAYHCEKCDE-KKTTLnrtsFLELPSTMTIQLKRFTYDLVNNMiRKDNQLFRFPFEIDMTPYMT 1998
Cdd:cd02667 114 ESCLKQFTEVEILEGNNKFACENCTKaKKQYL----ISKLPPVLVIHLKRFQQPRSANL-RKVSRHVSFPEILDLAPFCD 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1999 TSRHVPDEhvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesaqkkmfrrhrsstmrlsqsfantsgf 2078
Cdd:cd02667 189 PKCNSSED------------------------------------------------------------------------ 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2079 dtpsqQKPLIYELVGVLAHSGIATAGHYYSFIKERREEFRDSPHYN-------------KWHHINDMIVSPMSFnniedl 2145
Cdd:cd02667 197 -----KSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQRLSDLTKskpaadeagpgsgQWYYISDSDVREVSL------ 265
|
410 420 430
....*....|....*....|....*....|
gi 484399540 2146 wyggtftqegvfigldERVRHWNAYVLFYE 2175
Cdd:cd02667 266 ----------------EEVLKSEAYLLFYE 279
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1765-2174 |
5.60e-19 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 90.89 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLVHVPGLSRELIAlQNIDPQLRWGDNTAALLCELQRVFAqlNFAQCQAIVPEGL-------WK 1837
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLS-DRHSCTCLSCSPNSCLSCAMDEIFQ--EFYYSGDRSPYGPinllylsWK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1838 EFRfepdmPLNTKQHHDAIDFYSILLDK----CDNVLKKLELPP----LFQNRFFGKYSYEKICYGCWHRYKSPDEeFNC 1909
Cdd:cd02660 79 HSR-----NLAGYSQQDAHEFFQFLLDQlhthYGGDKNEANDEShcncIIHQTFSGSLQSSVTCQRCGGVSTTVDP-FLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1910 ISLALSGDN----------------LEEALENFLAAHVMeGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTYDL 1973
Cdd:cd02660 153 LSLDIPNKStpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1974 vNNMIRKDNQLFRFPFEIDMTPYMTTSRHVPDehvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesa 2053
Cdd:cd02660 232 -NKTSRKIDTYVQFPLELNMTPYTSSSIGDTQ------------------------------------------------ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2054 qkkmfrrhrsstmrlsqsfantsgfDTPSQQKPLIYELVGVLAHSGIATAGHYYSFIKERREEfrdsphynkWHHINDMI 2133
Cdd:cd02660 263 -------------------------DSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQ---------WFKFDDAM 308
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 484399540 2134 VSPMSfnniedlwyggtftqegvfiglDERVRHWNAYVLFY 2174
Cdd:cd02660 309 ITRVS----------------------EEEVLKSQAYLLFY 327
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1765-1971 |
2.84e-13 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 73.51 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLVHVPGLSRELIALQNIdPQLRWGDNTAALLCEL---------QRVFAQLNFAQCQAIVPEGL 1835
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENK-FPSDVVDPANDLNCQLikladgllsGRYSKPASLKSENDPYQVGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1836 wKEFRFE-------PDmpLNTKQHHDAIDFYSILLDKCDNVLKKLELPPLFQNRFFGkySYEKICYGCWHRYKSPDEEFN 1908
Cdd:cd02658 80 -KPSMFKaligkghPE--FSTMRQQDALEFLLHLIDKLDRESFKNLGLNPNDLFKFM--IEDRLECLSCKKVKYTSELSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 484399540 1909 CISLALSGD---------------NLEEALENFLAAHVMEgenaYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTY 1971
Cdd:cd02658 155 ILSLPVPKDeatekeegelvyepvPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQL 228
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1765-2175 |
2.16e-11 |
|
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: 67.72 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLVHvpglsrelialqnidpqlrwgdntAALLCELQRVFAQlnFAQCQAIVPEGLWKEF--RFE 1842
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF------------------------ENLLTCLKDLFES--ISEQKKRTGVISPKKFitRLK 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1843 PDMPL-NTKQHHDAIDFYSILLDKCDNVLKK--------------LELPP-------LFQnrffGKYSYEKICYGCwHRY 1900
Cdd:cd02663 55 RENELfDNYMHQDAHEFLNFLLNEIAEILDAerkaekanrklnnnNNAEPqptwvheIFQ----GILTNETRCLTC-ETV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1901 KSPDEEFncisLALSGD-----NLEEALENFLAAHVMEGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTYdlvn 1975
Cdd:cd02663 130 SSRDETF----LDLSIDveqntSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKY---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1976 nmirkDNQLFRFpfeidmtpymttsrhvpdehvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesaqK 2055
Cdd:cd02663 202 -----DEQLNRY-------------------------------------------------------------------I 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2056 KMFRR-HRSSTMRLSqsfaNTSGFDTPSQQkplIYELVGVLAHSGI-ATAGHYYSFIKerreefrdspHYNKWHHINDMI 2133
Cdd:cd02663 210 KLFYRvVFPLELRLF----NTTDDAENPDR---LYELVAVVVHIGGgPNHGHYVSIVK----------SHGGWLLFDDET 272
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 484399540 2134 VSPMSFNNIEDlWYGGTFTQEgvfigldervrhwNAYVLFYE 2175
Cdd:cd02663 273 VEKIDENAVEE-FFGDSPNQA-------------TAYVLFYQ 300
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1765-2177 |
2.29e-11 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 67.13 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLV--------HVPGLSRELIALQNIDPqlrwGDNTAALLCELQRVFAQLnfaqcqaiVPEglw 1836
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlylpkldeLLDDLSKELKVLKNVIR----KPEPDLNQEEALKLFTAL--------WSS--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1837 KEFRFEPDMPLNTKQhhDAIDFYSILLDKcdnvlkkLELPPLFQN---RFFGKYSYEKICYGCWHRY--KSPDEefncis 1911
Cdd:COG5533 66 KEHKVGWIPPMGSQE--DAHELLGKLLDE-------LKLDLVNSFtirIFKTTKDKKKTSTGDWFDIiiELPDQ------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1912 lalSGDNLEEALENFLAAhvMEGENAYHC---EKCDEKKTTLNR----TSFLELPSTMTIQLKRFTYDLVNNMIRKD-NQ 1983
Cdd:COG5533 131 ---TWVNNLKTLQEFIDN--MEELVDDETgvkAKENEELEVQAKqeyeVSFVKLPKILTIQLKRFANLGGNQKIDTEvDE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1984 LFRFPFEIDmtpymttsrhvpdehvqdlfdemlygngeadeapspphkngvaekpnlgsgsastpslesaQKKMFRRHrs 2063
Cdd:COG5533 206 KFELPVKHD-------------------------------------------------------------QILNIVKE-- 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2064 stmrlsqsfantsgfdtpsqqkpLIYELVGVLAHSGIATAGHYYSFIKERreefrdsphyNKWHHINDMIVSPMSFNNIE 2143
Cdd:COG5533 223 -----------------------TYYDLVGFVLHQGSLEGGHYIAYVKKG----------GKWEKANDSDVTPVSEEEAI 269
|
410 420 430
....*....|....*....|....*....|....
gi 484399540 2144 DLwyggtfTQEgvfigldervrhwNAYVLFYEKK 2177
Cdd:COG5533 270 NE------KAK-------------NAYLYFYERI 284
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1765-2175 |
8.26e-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 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: 62.73 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1765 GMKNDGGTCYMNAMIQQLVHVPGLsreLIALQNIDPQLRWGDNTAA-LLCELQRVFAQLNFAQcQAIVPEGLWKEFR--- 1840
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPEL---RDALKNYNPARRGANQSSDnLTNALRDLFDTMDKKQ-EPVPPIEFLQLLRmaf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1841 --FEPDMPLNTKQHHDAIDFYSILLDKCDNVLKKLELPPLFQNRFFG-KYSYEKICYGCWHRYKSPDEEFNCISLALSGD 1917
Cdd:cd02657 77 pqFAEKQNQGGYAQQDAEECWSQLLSVLSQKLPGAGSKGSFIDQLFGiELETKMKCTESPDEEEVSTESEYKLQCHISIT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1918 nleeALENFLAAHVMEGENayhcEKCDEKKTTLNRTS-------FLELPSTMTIQLKRFTYDLVNNMIRKDNQLFRFPFE 1990
Cdd:cd02657 157 ----TEVNYLQDGLKKGLE----EEIEKHSPTLGRDAiytktsrISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 1991 IDMTPYMTtsrhvpdehvqdlfdemlygngeadeapspphkngvaekpnlGSGsastpslesaqkkmfrrhrsstmrlsq 2070
Cdd:cd02657 229 LDLYELCT------------------------------------------PSG--------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484399540 2071 sfantsgfdtpsqqkplIYELVGVLAHSGI-ATAGHYYSFIKerreefrdSPHYNKWHHINDMIVSPMSFNNIEDLWYGG 2149
Cdd:cd02657 240 -----------------YYELVAVITHQGRsADSGHYVAWVR--------RKNDGKWIKFDDDKVSEVTEEDILKLSGGG 294
|
410 420
....*....|....*....|....*.
gi 484399540 2150 TFtqegvFIgldervrhwnAYVLFYE 2175
Cdd:cd02657 295 DW-----HI----------AYILLYK 305
|
|
| UBA |
smart00165 |
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
78-113 |
4.59e-06 |
|
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.
Pssm-ID: 197551 [Multi-domain] Cd Length: 37 Bit Score: 45.56 E-value: 4.59e-06
10 20 30
....*....|....*....|....*....|....*.
gi 484399540 78 YQDNQDMLITMGFKSEEIDTALRLSNNDVEKAIQYL 113
Cdd:smart00165 1 DEEKIDQLLEMGFSREEALKALRAANGNVERAAEYL 36
|
|
| UBA2_spUBP14_like |
cd14297 |
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
84-113 |
3.70e-05 |
|
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.
Pssm-ID: 270483 [Multi-domain] Cd Length: 39 Bit Score: 42.85 E-value: 3.70e-05
10 20 30
....*....|....*....|....*....|
gi 484399540 84 MLITMGFKSEEIDTALRLSNNDVEKAIQYL 113
Cdd:cd14297 6 QLVDMGFTEAQARKALRKTNNNVERAVDWL 35
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2083-2149 |
7.05e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 46.78 E-value: 7.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 484399540 2083 QQKPliYELVGVLAHSGIATAGHYYSFIKERreefrdspHYNKWHHINDMIVSPMSFNNIEDLWYGG 2149
Cdd:cd02665 160 QQVP--YELHAVLVHEGQANAGHYWAYIYKQ--------SRQEWEKYNDISVTESSWEEVERDSFGG 216
|
|
| UBA |
cd14270 |
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ... |
83-111 |
1.81e-04 |
|
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains.
Pssm-ID: 270456 [Multi-domain] Cd Length: 30 Bit Score: 40.80 E-value: 1.81e-04
10 20
....*....|....*....|....*....
gi 484399540 83 DMLITMGFKSEEIDTALRLSNNDVEKAIQ 111
Cdd:cd14270 2 AQLVEMGFSREQARRALRATNGDVEAAVE 30
|
|
| UBA_UBP24 |
cd14286 |
UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; ... |
79-114 |
1.12e-03 |
|
UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24, also called deubiquitinating enzyme 24, ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24, 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 and a C-terminal peptidase C19 domain.
Pssm-ID: 270472 Cd Length: 37 Bit Score: 38.58 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|....*..
gi 484399540 79 QDNQDMLITMGFKS-EEIDTALRLSNNDVEKAIQYLT 114
Cdd:cd14286 1 EEHVTTLLCMGFSDpEEIRKALRLAKNDLNEAVAILT 37
|
|
| UBA1_NUB1_like |
cd14291 |
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ... |
84-113 |
2.58e-03 |
|
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain.
Pssm-ID: 270477 [Multi-domain] Cd Length: 36 Bit Score: 37.81 E-value: 2.58e-03
10 20 30
....*....|....*....|....*....|
gi 484399540 84 MLITMGFKSEEIDTALRLSNNDVEKAIQYL 113
Cdd:cd14291 7 QLMEMGFSEAEARLALRACNGNVERAVDYI 36
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
2088-2131 |
3.51e-03 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 42.26 E-value: 3.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 484399540 2088 IYELVGVLAH-SGIATAGHYYSFIKERREEFRDSPHyNKWHHIND 2131
Cdd:pfam13423 259 KYELRGVVVHiGDSGTSGHLVSFVKVADSELEDPTE-SQWYLFND 302
|
|
| UBA |
pfam00627 |
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
77-113 |
3.81e-03 |
|
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.
Pssm-ID: 395502 [Multi-domain] Cd Length: 37 Bit Score: 37.03 E-value: 3.81e-03
10 20 30
....*....|....*....|....*....|....*..
gi 484399540 77 QYQDNQDMLITMGFKSEEIDTALRLSNNDVEKAIQYL 113
Cdd:pfam00627 1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1919-1996 |
4.32e-03 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 42.56 E-value: 4.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 484399540 1919 LEEALENFLAAHVMEGENAYHCEKCDEKKTTLNRTSFLELPSTMTIQLKRFTYDLVNNMIRKDnqLFRFP-FEIDMTPY 1996
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDD--LVEYPiDDLDLSGV 753
|
|
| UBA2_scUBP14_like |
cd14298 |
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ... |
83-113 |
6.37e-03 |
|
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.
Pssm-ID: 270484 [Multi-domain] Cd Length: 38 Bit Score: 36.67 E-value: 6.37e-03
10 20 30
....*....|....*....|....*....|.
gi 484399540 83 DMLITMGFKSEEIDTALRLSNNDVEKAIQYL 113
Cdd:cd14298 5 AQLVSMGFDPEVARKALILTNGNVERAIEWL 35
|
|
| UBA2_UBAP1_like |
cd14316 |
UBA2 domain found in ubiquitin-associated protein 1 (UBAP-1) and similar proteins; UBAP-1, ... |
81-114 |
8.61e-03 |
|
UBA2 domain found in ubiquitin-associated protein 1 (UBAP-1) and similar proteins; UBAP-1, also called nasopharyngeal carcinoma-associated gene 20 protein, is a ubiquitously expressed protein that may play an important role in the ubiquitin pathway and cell progression. It co-localizes with TDP-43 proteins in neuronal cytoplasmic inclusions and acts as a genetic risk factor for frontotemporal lobar degeneration (FTLD). Moreover, UBAP-1, together with VPS37A, forms an endosome-specific endosomal sorting complexes I required for transport (ESCRT-I) complex that displays a restricted cellular function, ubiquitin-dependent endosomal sorting and multivesicular body (MVB) biogenesis. UBAP-1 contains an N-terminal UBAP-1-MVB12-associated (UMA) domain, and two tandem ubiquitin-associated (UBA) domains that may be responsible for the binding of ubiquitin-conjugating enzymes. This model corresponds to UBA2 domain.
Pssm-ID: 270501 Cd Length: 37 Bit Score: 36.35 E-value: 8.61e-03
10 20 30
....*....|....*....|....*....|....
gi 484399540 81 NQDMLITMGFKSEEIDTALRLSNNDVEKAIQYLT 114
Cdd:cd14316 4 LLNQLHELGFPEDKIKEALLKHNNDRDKALDELV 37
|
|
| |
