|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
23-333 |
3.17e-162 |
|
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: 467.52 E-value: 3.17e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 23 PLGLRNLGNTCYLNSVLQCLTFTPPLANFCLTHKHSSHCdtyvdgERKRDCPFCIVEKRIARSLSVDLTTDAPNKISSCL 102
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDC------CNEGFCMMCALEAHVERALASSGPGSAPRIFSSNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 103 KIFAEHFKLGRQEDAHEFLRYVIDACHNTSLRLKKLRYNGNEPFNGNSVVKEIFGGALQSQVKCLSCGAESNKADEIMDI 182
Cdd:cd02661 75 KQISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 183 SLEILQSSSVKESLQKFFQSEILDGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRFGGIFGGKIDKAISFGEILVL 262
Cdd:cd02661 155 SLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11993490 263 SNFMSKaSKDPQPEYKLFGIIVHSGFSPESGHYYAYVKDSLGRWYCCNDSFVSLSTLQEVLSEKAYILFFS 333
Cdd:cd02661 235 SPYMSQ-PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
25-332 |
5.02e-77 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 248.51 E-value: 5.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLANFCLTHKHSSHCDTYvdgerKRDCPFCIVEKRIARSLSVDLTTDA--PNKISSCL 102
Cdd:pfam00443 2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRY-----NKDINLLCALRDLFKALQKNSKSSSvsPKMFKKSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 103 KIFAEHFKLGRQEDAHEFLRYVIDACHNTSlrlkklryNGNEPFNGNSVVKEIFGGALQSQVKCLSCGAESNKADEIMDI 182
Cdd:pfam00443 77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEDL--------NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 183 SLEILQSSSVK------ESLQKFFQSEILDGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRF--GGIFGGKIDKAI 254
Cdd:pfam00443 149 SLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFsyNRSTWEKLNTEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 255 SFGEILVLSNFMSKASKDPQPE---YKLFGIIVHSGfSPESGHYYAYVKDSL-GRWYCCNDSFVSLSTLQ-EVLSEKAYI 329
Cdd:pfam00443 229 EFPLELDLSRYLAEELKPKTNNlqdYRLVAVVVHSG-SLSSGHYIAYIKAYEnNRWYKFDDEKVTEVDEEtAVLSSSAYI 307
|
...
gi 11993490 330 LFF 332
Cdd:pfam00443 308 LFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
25-332 |
2.05e-72 |
|
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: 234.30 E-value: 2.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFtpplanfclthkhsshcdtyvdgerkrdcpfcivekriarslsvdlttdapnkissclki 104
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 105 faehfklgRQEDAHEFLRYVIDACHNTslrLKKLRYNGNEPFNGNSVVKEIFGGALQSQVKCLSCGAESNKADEIMDISL 184
Cdd:cd02257 21 --------EQQDAHEFLLFLLDKLHEE---LKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 185 EI----LQSSSVKESLQKFFQSEILDGNNKYRCESCeKLVTARKQMSILQAPNILVIQLKRF---GGIFGGKIDKAISFG 257
Cdd:cd02257 90 PLpvkgLPQVSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFsfnEDGTKEKLNTKVSFP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 258 EILVLSNFMSK-----ASKDPQPEYKLFGIIVHSGFSPESGHYYAYVKDSL-GRWYCCNDSFVSLSTLQEVL-----SEK 326
Cdd:cd02257 169 LELDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSdGKWYKFNDDKVTEVSEEEVLefgslSSS 248
|
....*.
gi 11993490 327 AYILFF 332
Cdd:cd02257 249 AYILFY 254
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-332 |
2.92e-61 |
|
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: 207.23 E-value: 2.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLANFCLTHKHSSHCdtyvDGERKRDCPFCIVEKRIARSLSVDLTTD-APNKISSCLK 103
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTC----LSCSPNSCLSCAMDEIFQEFYYSGDRSPyGPINLLYLSW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 104 IFAEHFKLGRQEDAHEFLRYVIDACHNTSLRLKKLRYNGNEpfnGNSVVKEIFGGALQSQVKCLSCGAESNKADEIMDIS 183
Cdd:cd02660 78 KHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESH---CNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 184 LEIlQSSSVK----------------ESLQKFFQSEILdGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRFGGIFG 247
Cdd:cd02660 155 LDI-PNKSTPswalgesgvsgtptlsDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 248 G---KIDKAISFGEILVLSNFMS--------KASKDPQPEYKLFGIIVHSGfSPESGHYYAYVKDSLGRWYCCNDSFVSL 316
Cdd:cd02660 233 KtsrKIDTYVQFPLELNMTPYTSssigdtqdSNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITR 311
|
330
....*....|....*.
gi 11993490 317 STLQEVLSEKAYILFF 332
Cdd:cd02660 312 VSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-332 |
2.59e-58 |
|
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: 197.99 E-value: 2.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLAnfclthkhsshcdtyvdgerkrdcpfcivekriarslsvDLTTDAPNKISSCLKI 104
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALR---------------------------------------ELLSETPKELFSQVCR 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 105 FAEHFKLGRQEDAHEFLRYVIDachntSLRlkklryngnepfngnSVVKEIFGGALQSQVKCLSCGAESNKADEIMDISL 184
Cdd:cd02667 42 KAPQFKGYQQQDSHELLRYLLD-----GLR---------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 185 EILQSS----SVKESLQKFFQSEILDGNNKYRCESCEKlvtARKQMSILQAPNILVIQLKRF-GGIFGG--KIDKAISFG 257
Cdd:cd02667 102 PRSDEIksecSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqQPRSANlrKVSRHVSFP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 258 EILVLSNFMSKASKDPQPE----YKLFGIIVHSGfSPESGHYYAYVKD----------------------SLGRWYCCND 311
Cdd:cd02667 179 EILDLAPFCDPKCNSSEDKssvlYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagpGSGQWYYISD 257
|
330 340
....*....|....*....|.
gi 11993490 312 SFVSLSTLQEVLSEKAYILFF 332
Cdd:cd02667 258 SDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-337 |
4.31e-57 |
|
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: 196.32 E-value: 4.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLANFCLthkhSSHCDTYVDGERKRDCPFCIVEKRIARSLSVDLTTDAPNKISSCLKi 104
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVY----SIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGW- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 105 faEHFKLGRQEDAHEFLRYVIDACHNTS--LRLKKLryngnepfngnsvVKEIFGGALQSQVKCLSCGAESNKADEIMDI 182
Cdd:cd02659 79 --DSLNTFEQHDVQEFFRVLFDKLEEKLkgTGQEGL-------------IKNLFGGKLVNYIICKECPHESEREEYFLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 183 SLEILQSSSVKESLQKFFQSEILDGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRFG-------GIfggKIDKAIS 255
Cdd:cd02659 144 QVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfdfetmmRI---KINDRFE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 256 FGEILVLSNFMSK---------ASKDPQP-EYKLFGIIVHSGfSPESGHYYAYVKDSL-GRWYCCNDSFVSLSTLQEVLS 324
Cdd:cd02659 221 FPLELDMEPYTEKglakkegdsEKKDSESyIYELHGVLVHSG-DAHGGHYYSYIKDRDdGKWYKFNDDVVTPFDPNDAEE 299
|
330 340 350
....*....|....*....|....*....|....*
gi 11993490 325 E----------------------KAYILFFSRSNQ 337
Cdd:cd02659 300 EcfggeetqktydsgprafkrttNAYMLFYERKSP 334
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-333 |
4.45e-57 |
|
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: 192.89 E-value: 4.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLtftpplanfclthkhsSHcdtyvdgerkrdcpfcivekriarslsvdlttdapnkissclki 104
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL----------------SA-------------------------------------------- 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 105 faehfklgRQEDAHEFLRYVIDACHntslrlkklryngnepfngnSVVKEIFGGALQSQVKCLSCGAESNKADEIMDISL 184
Cdd:cd02674 21 --------DQQDAQEFLLFLLDGLH--------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSL 72
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 185 EILQSSSV--KESLQ----KFFQSEILDGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRFG--GIFGGKIDKAISF 256
Cdd:cd02674 73 PIPSGSGDapKVTLEdclrLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSfsRGSTRKLTTPVTF 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11993490 257 G-EILVLSNFMSKASKDPQPEYKLFGIIVHSGfSPESGHYYAYVKDSL-GRWYCCNDSFVSLSTLQEVLSEKAYILFFS 333
Cdd:cd02674 153 PlNDLDLTPYVDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNEtNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-333 |
3.81e-50 |
|
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: 176.73 E-value: 3.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLAnfCLthkhsshcdtyvdgerkRDCPFCIVEKRiARSLSVdlttdAPNKISSCLKI 104
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT--CL-----------------KDLFESISEQK-KRTGVI-----SPKKFITRLKR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 105 FAEHFKLGRQEDAHEFLRYVIDAC------HNTSLRLKKLRYNGNEPFNGNSVVKEIFGGALQSQVKCLSCGAESNKADE 178
Cdd:cd02663 56 ENELFDNYMHQDAHEFLNFLLNEIaeildaERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDET 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 179 IMDISLEILQSSSVKESLQKFFQSEILDGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRFG--GIFGG--KIDKAI 254
Cdd:cd02663 136 FLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKydEQLNRyiKLFYRV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 255 SFGEILVLSNFMSKASkDPQPEYKLFGIIVHSGFSPESGHYYAYVKdSLGRWYCCNDSFVSL---STLQEVL-----SEK 326
Cdd:cd02663 216 VFPLELRLFNTTDDAE-NPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKideNAVEEFFgdspnQAT 293
|
....*..
gi 11993490 327 AYILFFS 333
Cdd:cd02663 294 AYVLFYQ 300
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-332 |
9.65e-41 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 151.49 E-value: 9.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLtftpplanfcLTHKHSSHCDTYVDGERKRDC---PFCIVEKRIARSLSVDLTTDAPNK-ISS 100
Cdd:cd02664 1 GLINLGNTCYMNSVLQAL----------FMAKDFRRQVLSLNLPRLGDSqsvMKKLQLLQAHLMHTQRRAEAPPDYfLEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 101 CLkifAEHFKLGRQEDAHEFLRYVIDACHntslrlkklryngnepfngnSVVKEIFGGALQSQVKCLSCGAESNKADEIM 180
Cdd:cd02664 71 SR---PPWFTPGSQQDCSEYLRYLLDRLH--------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 181 DISLEIlqsSSVKESLQKFFQSEILDGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRFGGIFG----GKIDKAISF 256
Cdd:cd02664 128 DLDLSF---PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKthvrEKIMDNVSI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 257 GEILVL--------SNFMSKASKDPQPE----------YKLFGIIVHSGFSPESGHYYAYVKDSLGR------------- 305
Cdd:cd02664 205 NEVLSLpvrvesksSESPLEKKEEESGDdgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQTDAdstgqecpepkda 284
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 11993490 306 --------WYCCNDSFVSLSTLQEVL-------SEKAYILFF 332
Cdd:cd02664 285 eendesknWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-315 |
8.19e-39 |
|
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: 146.03 E-value: 8.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLANFCLTHKHSSHCDTYVDGERKRDCPFCIVEKriARSLSVDLTTDAPNKISSCLKI 104
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQ--LQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 105 FAEHFKLGRQEDAHEFLRYVIdachntSLRLKKLRYNGNEpfNGNSVVKEIFGGALQSQVKCLSCGAESNKADEIMDISL 184
Cdd:cd02668 79 KALGLDTGQQQDAQEFSKLFL------SLLEAKLSKSKNP--DLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 185 EILQSSSVKESLQKFFQSEILDGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRFggIFG------GKIDKAISFGE 258
Cdd:cd02668 151 QLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRF--VFDrktgakKKLNASISFPE 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 11993490 259 ILVLSNFMskASKDPQP-EYKLFGIIVHSGFSPESGHYYAYVKDS-LGRWYCCNDSFVS 315
Cdd:cd02668 229 ILDMGEYL--AESDEGSyVYELSGVLIHQGVSAYSGHYIAHIKDEqTGEWYKFNDEDVE 285
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
11-332 |
2.16e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 136.56 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 11 PSLLSQKRRNGPPL-GLRNLGNTCYLNSVLQCLTFTPplaNFclthKHSSHCDTYVDGERKRDCPFCIVEKRIARSLsvd 89
Cdd:cd02671 11 SATSCEKRENLLPFvGLNNLGNTCYLNSVLQVLYFCP---GF----KHGLKHLVSLISSVEQLQSSFLLNPEKYNDE--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 90 LTTDAPNKISSCLKIFAEHFKLGRQEDAHEFLRYVIDACHNtslrlkklryngnepfngnsVVKEIFGGALQSQVKCLSC 169
Cdd:cd02671 81 LANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE--------------------LVEKDFQGQLVLRTRCLEC 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 170 GAESNKADEIMDISLEILQS-------------------SSVKESLQKFFQSEILDGNNKYRCESCEKLVTARKQMSILQ 230
Cdd:cd02671 141 ETFTERREDFQDISVPVQESelskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 231 APNILVIQLKRFGG------IFGG--KIDKAISfgEILVLSNFmSKASKDPQPEYKLFGIIVHSGFSPESGHYYAYVkds 302
Cdd:cd02671 221 LPEVITIHLKCFAAngsefdCYGGlsKVNTPLL--TPLKLSLE-EWSTKPKNDVYRLFAVVMHSGATISSGHYTAYV--- 294
|
330 340 350
....*....|....*....|....*....|....*....
gi 11993490 303 lgRWYCCNDSFVSLST---LQEVLSEKA------YILFF 332
Cdd:cd02671 295 --RWLLFDDSEVKVTEekdFLEALSPNTsststpYLLFY 331
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
24-325 |
5.70e-33 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 136.15 E-value: 5.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 24 LGLRNLGNTCYLNSVLQCLTFTPPLANfclthkhsshcDTY---VDGERKRDCPFCIVEKRIARSLSVDLTTDAPNKISS 100
Cdd:COG5077 194 VGLRNQGATCYMNSLLQSLFFIAKFRK-----------DVYgipTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELTRS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 101 CLKIFAEHFklgRQEDAHEFLRYVIDACHNtSLRLKKLRyngnepfngnSVVKEIFGGALQSQVKCLSCGAESNKADEIM 180
Cdd:COG5077 263 FGWDSDDSF---MQHDIQEFNRVLQDNLEK-SMRGTVVE----------NALNGIFVGKMKSYIKCVNVNYESARVEDFW 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 181 DISLEILQSSSVKESLQKFFQSEILDGNNKYRCEScEKLVTARKQMSILQAPNILVIQLKRFGGIF----GGKIDKAISF 256
Cdd:COG5077 329 DIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFerdmMVKINDRYEF 407
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11993490 257 GEILVLSNFMSKASKDPQP---EYKLFGIIVHSGfSPESGHYYAYVKDSL-GRWYCCNDSFVSLSTLQEVLSE 325
Cdd:COG5077 408 PLEIDLLPFLDRDADKSENsdaVYVLYGVLVHSG-DLHEGHYYALLKPEKdGRWYKFDDTRVTRATEKEVLEE 479
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-332 |
2.65e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 127.05 E-value: 2.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLANFCLTHKHSSHCDTyVDGERKRDCPF-----------CIVEKRIarSLSVDLTTD 93
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDV-VDPANDLNCQLikladgllsgrYSKPASL--KSENDPYQV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 94 --APNKISSCLKIFAEHFKLGRQEDAHEFLRYVIDachntslRL-KKLRYNGNEPFNgnsvvkEIFGGALQSQVKCLSCG 170
Cdd:cd02658 78 giKPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLdRESFKNLGLNPN------DLFKFMIEDRLECLSCK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 171 A--ESNKADEIMDISLEILQSS------------SVKESLQKFFQSEILDgnnkYRCESCEKLVTARKQMSILQAPNILV 236
Cdd:cd02658 145 KvkYTSELSEILSLPVPKDEATekeegelvyepvPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 237 IQLKRFGGIFGG---KIDKAISFGEILVLSNfmskaskdpqpeYKLFGIIVHSGFSPESGHYYAYVK---DSLGRWYCCN 310
Cdd:cd02658 221 INMKRFQLLENWvpkKLDVPIDVPEELGPGK------------YELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFN 288
|
330 340
....*....|....*....|..
gi 11993490 311 DSFVSLSTLQEVLSEKAYILFF 332
Cdd:cd02658 289 DEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
25-334 |
3.75e-29 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 117.21 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTF-TPPLANFCLTHKHSSHCDTYVDGERKRDCPFCivekRIARSLSVDLTTDAPNkissclk 103
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALyLPKLDELLDDLSKELKVLKNVIRKPEPDLNQE----EALKLFTALWSSKEHK------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 104 iFAEHFKLGRQEDAHEFLRYVIDAchntslrLKKLRYNGNEPFNGNSVVKEifggalqsqvkclscgaESNKADEIMDIS 183
Cdd:COG5533 70 -VGWIPPMGSQEDAHELLGKLLDE-------LKLDLVNSFTIRIFKTTKDK-----------------KKTSTGDWFDII 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 184 LEILQSSSVKES--LQKF---FQSEILDGNNKYRCESCEKLVTARKQ--MSILQAPNILVIQLKRFGGIFGG-KIDKAis 255
Cdd:COG5533 125 IELPDQTWVNNLktLQEFidnMEELVDDETGVKAKENEELEVQAKQEyeVSFVKLPKILTIQLKRFANLGGNqKIDTE-- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 256 fgeilVLSNFMSKASKDPQPE------YKLFGIIVHSGfSPESGHYYAYVKDSlGRWYCCNDSFVSLSTLQEVL---SEK 326
Cdd:COG5533 203 -----VDEKFELPVKHDQILNivketyYDLVGFVLHQG-SLEGGHYIAYVKKG-GKWEKANDSDVTPVSEEEAInekAKN 275
|
....*...
gi 11993490 327 AYILFFSR 334
Cdd:COG5533 276 AYLYFYER 283
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-332 |
7.49e-22 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 95.13 E-value: 7.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLtftpplanfclthkhSShcdtyvdgerkrdCPfcivekriarSLSVDLttdapNKISSclki 104
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL---------------AS-------------LP----------SLIEYL-----EEFLE---- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 105 faehfklgrQEDAHEFLRYVIDACHNtslrlkklryngnepfngnsVVKEIFGGALQSQVKCLSCGAESNKADEIMD-IS 183
Cdd:cd02662 34 ---------QQDAHELFQVLLETLEQ--------------------LLKFPFDGLLASRIVCLQCGESSKVRYESFTmLS 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 184 LEILQSSSV-----KESLQKFFQSEILDGnnkYRCESCeklvtarkQMSILQAPNILVIQLKRFggIFGGKID-----KA 253
Cdd:cd02662 85 LPVPNQSSGsgttlEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRS--VFDGRGTstknsCK 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 254 ISFGEILvlsnfmskaskdPQPEYKLFGIIVHSGfSPESGHYYAYVKDSL---------------------GRWYCCNDS 312
Cdd:cd02662 152 VSFPERL------------PKVLYRLRAVVVHYG-SHSSGHYVCYRRKPLfskdkepgsfvrmregpsstsHPWWRISDT 218
|
330 340
....*....|....*....|.
gi 11993490 313 FVSLSTLQEVLSEK-AYILFF 332
Cdd:cd02662 219 TVKEVSESEVLEQKsAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
196-336 |
7.74e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 94.18 E-value: 7.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 196 LQKFFQSEILDGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRFGGI--FGGKIDKAISFG-EILVLSNFMSkASKD 272
Cdd:COG5560 681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVrsFRDKIDDLVEYPiDDLDLSGVEY-MVDD 759
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11993490 273 PQPEYKLFGIIVHSGFSpESGHYYAYVKD-SLGRWYCCNDSFVSLSTLQEVLSEKAYILFFSRSN 336
Cdd:COG5560 760 PRLIYDLYAVDNHYGGL-SGGHYTAYARNfANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-330 |
1.44e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 83.92 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLANFCLTHKhsshcdtyvdGERKRDCPFCIvekRIARSLSvDLTTDAPNKISS---- 100
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYN----------PARRGANQSSD---NLTNALR-DLFDTMDKKQEPvppi 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 101 -CLKIFAEHF----KLGR-----QEDAHEFLRYVIdachnTSLRLKkLRYNGNEPfngnSVVKEIFGGALQSQVKCLSCG 170
Cdd:cd02657 67 eFLQLLRMAFpqfaEKQNqggyaQQDAEECWSQLL-----SVLSQK-LPGAGSKG----SFIDQLFGIELETKMKCTESP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 171 AESNKADEI-------MDISLEI--LQS---SSVKESLQKFfqSEILDGNNKYRcesceklvtarKQMSILQAPNILVIQ 238
Cdd:cd02657 137 DEEEVSTESeyklqchISITTEVnyLQDglkKGLEEEIEKH--SPTLGRDAIYT-----------KTSRISRLPKYLTVQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 239 LKRFggiF-------GGKIDKAISFGEILVLSNFMSKASKdpqpeYKLFGIIVHSGFSPESGHYYAYVKDSL-GRWYCCN 310
Cdd:cd02657 204 FVRF---FwkrdiqkKAKILRKVKFPFELDLYELCTPSGY-----YELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFD 275
|
330 340
....*....|....*....|....*..
gi 11993490 311 DSFVSLSTLQEVL-------SEKAYIL 330
Cdd:cd02657 276 DDKVSEVTEEDILklsgggdWHIAYIL 302
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
25-311 |
2.75e-17 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 83.09 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLANFCLthkhsSHCdtyvdgerKRDCP--FCIV-EkriaRSLSVDLTTDAPNKI--- 98
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLAL-----SHL--------ATECLkeHCLLcE----LGFLFDMLEKAKGKNcqa 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 99 ---SSCLKIFAEHFKLGRQEDAHE-------------FLRYVIDACHNTSLRLKKlryngnEPFNGNSVVKEIFGGALQS 162
Cdd:pfam13423 65 snfLRALSSIPEASALGLLDEDREtnsaislssliqsFNRFLLDQLSSEENSTPP------NPSPAESPLEQLFGIDAET 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 163 QVKCLSCGAESNKADEIMDISL---EILQSSSVKESLQKFfqSEIL------DGNNKYRCESCEKLVTARKQMSILQAPN 233
Cdd:pfam13423 139 TIRCSNCGHESVRESSTHVLDLiypRKPSSNNKKPPNQTF--SSILksslerETTTKAWCEKCKRYQPLESRRTVRNLPP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 234 ILVIQLKRFGGIFGGKIDKAISFGEILVLSNFMSKASKDPQPEYKLFGIIVHSGFSPESGHYYAYVK--------DSLGR 305
Cdd:pfam13423 217 VLSLNAALTNEEWRQLWKTPGWLPPEIGLTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseledPTESQ 296
|
....*.
gi 11993490 306 WYCCND 311
Cdd:pfam13423 297 WYLFND 302
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
25-186 |
5.92e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 72.22 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLANFCLThkhsshcDTYVDgERKRDCPFCIVEKrIARSLS--------VDLTTDAPN 96
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLS-------DEYEE-SINEENPLGMHGS-VASAYAdlikqlydGNLHAFTPS 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 97 KISSCLKIFAEHFKLGRQEDAHEFLRYVIDACHNTSLRLKKLRYNGN-EPFNGN--------------------SVVKEI 155
Cdd:COG5560 338 GFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKpDLSPGDdvvvkkkakecwwehlkrndSIITDL 417
|
170 180 190
....*....|....*....|....*....|.
gi 11993490 156 FGGALQSQVKCLSCGAESNKADEIMDISLEI 186
Cdd:COG5560 418 FQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-330 |
5.06e-12 |
|
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: 68.50 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 25 GLRNLGNTCYLNSVLQCLTFTPPLANFCLTHKHSshcdtyvdgERKRDCPFCIVeKRIARSLsvdlttdapNKISSClKI 104
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENY---------ENIKDRKSELV-KRLSELI---------RKIWNP-RN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 105 FAEH-----------------FKLGRQEDAHEFLRYVIDACHNTSLRLKKlryngnepfNGNSVVKEIFGGALQSQVKCL 167
Cdd:cd02669 181 FKGHvsphellqavskvskkkFSITEQSDPVEFLSWLLNTLHKDLGGSKK---------PNSSIIHDCFQGKVQIETQKI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 168 ScgaesNKADEIMDISLEILQSSSVKESLQKFF----------------------QSEILDGNNKYRCESCEKLVTARKQ 225
Cdd:cd02669 252 K-----PHAEEEGSKDKFFKDSRVKKTSVSPFLlltldlpppplfkdgneeniipQVPLKQLLKKYDGKTETELKDSLKR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 226 MSILQAPNILVIQLKRF--GGIFGGKIDKAISFGEILV-LSNFMSKASKDPQPE--YKLFGIIVHSGFSPESGHYYAYV- 299
Cdd:cd02669 327 YLISRLPKYLIFHIKRFskNNFFKEKNPTIVNFPIKNLdLSDYVHFDKPSLNLStkYNLVANIVHEGTPQEDGTWRVQLr 406
|
330 340 350
....*....|....*....|....*....|.
gi 11993490 300 KDSLGRWYCCNDSFVSLSTLQEVLSEKAYIL 330
Cdd:cd02669 407 HKSTNKWFEIQDLNVKEVLPQLIFLSESYIQ 437
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
26-332 |
1.87e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 64.47 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 26 LRNLGNTCYLNSVLQCLtftpplanfclthkhsshcdtyvdgerkrdcpfcivekriarslsvdlttdapnkiSSCLKIF 105
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL--------------------------------------------------------SSIGKIN 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 106 AEhFKLGRQEDAHEFLRYVIDACHNTSLRLKKlryngNEPFNGNSVVK----EIFGGALQSQVKCLSCGAESNKAD--EI 179
Cdd:cd02673 26 TE-FDNDDQQDAHEFLLTLLEAIDDIMQVNRT-----NVPPSNIEIKRlnplEAFKYTIESSYVCIGCSFEENVSDvgNF 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 180 MDISLEILQSSSVKESLQKFFQ-SEILDGNNKYRCE---SCEKLVTArkqmsilqaPNILVIQLKRFggifggkiDKAIS 255
Cdd:cd02673 100 LDVSMIDNKLDIDELLISNFKTwSPIEKDCSSCKCEsaiSSERIMTF---------PECLSINLKRY--------KLRIA 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 256 FGEILVLSNFMSKASKDPQPEYKLFGIIVHSGFSPESGHYYAYVKDSLG--RWYCCNDSF---VSLSTLQEVLSEKAYIL 330
Cdd:cd02673 163 TSDYLKKNEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAYTKELYNgsSWLYCSDDEirpVSKNDVSTNARSSGYLI 242
|
..
gi 11993490 331 FF 332
Cdd:cd02673 243 FY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
23-323 |
2.41e-09 |
|
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: 59.43 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 23 PLGLRNLGNTCYLNSVLQCLTFTPPLANFCLTHKHSSHCDTYVDGERKRdcpfcIVEKRIA--------------RSLSV 88
Cdd:cd02666 1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTERR-----IGGREVSrselqrsnqfvyelRSLFN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 89 DL-TTDA----PNKISSCLKIfaehfklgRQEDAHEflryVIDAChntslrLKKLRYNGNEPFNGNSVVKEIFGGALQSQ 163
Cdd:cd02666 76 DLiHSNTrsvtPSKELAYLAL--------RQQDVTE----CIDNV------LFQLEVALEPISNAFAGPDTEDDKEQSDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 164 VKCL-SCGAESNKADEIMDisleilQSSSVKESLQKFFQSEI-------LDGNNKYRCESCEKLVTARKQMSILQAPNIL 235
Cdd:cd02666 138 IKRLfSGKTKQQLVPESMG------NQPSVRTKTERFLSLLVdvgkkgrEIVVLLEPKDLYDALDRYFDYDSLTKLPQRS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 236 VIQLKRFGGIFGGKID-------KAISFGEILVLSNFMSKASKDPQPE---------------------YKLFGIIVHSG 287
Cdd:cd02666 212 QVQAQLAQPLQRELISmdryelpSSIDDIDELIREAIQSESSLVRQAQnelaelkheiekqfddlksygYRLHAVFIHRG 291
|
330 340 350
....*....|....*....|....*....|....*..
gi 11993490 288 fSPESGHYYAYVKDSLGR-WYCCNDSFVSLSTLQEVL 323
Cdd:cd02666 292 -EASSGHYWVYIKDFEENvWRKYNDETVTVVPASEVF 327
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
150-331 |
4.86e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 48.66 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 150 SVVKEIFGGALQSQVKC------LSCGAESNKADEIMDISLEILQSSSVKES--LQKFFQSEILDGNNKYRCESCEKLVT 221
Cdd:cd02672 66 STLIQNFTRFLLETISQdqlgtpFSCGTSRNSVSLLYTLSLPLGSTKTSKEStfLQLLKRSLDLEKVTKAWCDTCCKYQP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 222 ARKQMSILQAPNI----LVIQLKRFGGIFGGKIDKAISFGeilVLSNFMS-KASKDPQPE----------YKLFGIIVHS 286
Cdd:cd02672 146 LEQTTSIRHLPDIlllvLVINLSVTNGEFDDINVVLPSGK---VMQNKVSpKAIDHDKLVknrgqesiykYELVGYVCEI 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 11993490 287 GFSPESGHYYAYVKDS-----LGRWYCCNDSFVSlstlqEVlSEKAYILF 331
Cdd:cd02672 223 NDSSRGQHNVVFVIKVneestHGRWYLFNDFLVT-----PV-SELAYILL 266
|
|
| EnY2 |
pfam10163 |
Transcription factor e(y)2; EnY2 is a small transcription factor which is combined in a ... |
576-652 |
9.31e-06 |
|
Transcription factor e(y)2; EnY2 is a small transcription factor which is combined in a complex with the TAFII40 protein. The protein is conserved from paramecium to humans.
Pssm-ID: 462972 Cd Length: 78 Bit Score: 44.06 E-value: 9.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11993490 576 ELEAIKESLKkdalSHLRSCGWYDKVliSMHAKKRLRTeqsgGEDGSDLKrRLIEDVKSSLKSQIPEELKADLVNRI 652
Cdd:pfam10163 10 EYERLKNLLR----ERLIESGWRDEV--KELCKEIIRE----LEDVLTFD-ELVEKITPKARALVPDEVKKELLQRI 75
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
230-332 |
5.44e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 42.13 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 230 QAPNILVIQLKRFGGIFGG--KIDKAISFGEILVLSNFMSKASKDPQPEY---------------------KLFGIIVHS 286
Cdd:cd02670 97 KAPSCLIICLKRYGKTEGKaqKMFKKILIPDEIDIPDFVADDPRACSKCQlecrvcyddkdfsptcgkfklSLCSAVCHR 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11993490 287 GFSPESGHYYAYVK-----------DSLGRWYCCNDSFVSLSTLQEV-------LSEKAYILFF 332
Cdd:cd02670 177 GTSLETGHYVAFVRygsysltetdnEAYNAQWVFFDDMADRDGVSNGfnipaarLLEDPYMLFY 240
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
232-332 |
7.65e-03 |
|
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: 38.31 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993490 232 PNILVIQLKRF--GGIFGGKIDKAISFGEILvlsnfmskaskdPQPEYKLFGIIVHSGfSPESGHYYAYV-KDSLGRWYC 308
Cdd:cd02665 129 PPVLTFELSRFefNQGRPEKIHDKLEFPQII------------QQVPYELHAVLVHEG-QANAGHYWAYIyKQSRQEWEK 195
|
90 100 110
....*....|....*....|....*....|..
gi 11993490 309 CNDSFVSLSTLQEVLSE--------KAYILFF 332
Cdd:cd02665 196 YNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
|
|
| |
