|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-314 |
6.59e-132 |
|
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: 377.99 E-value: 6.59e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFCTEVL------LKQIDAPPFSEIQQLLALLIHSRRPELTPRAVLASTRPPGFAPGY 74
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLslnlprLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASRPPWFTPGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 75 QQDSSEFLSYLLDRLHeqekkilngnvtqqhntsalissngsgtiatnstkTLVQKTFEGQLSVGCLCTVCNSTNHTTET 154
Cdd:cd02664 81 QQDCSEYLRYLLDRLH-----------------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTER 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 155 FRSLDLSFPedsdlsaagdgthSVQKLLDYFCSSEKLVGENQYFCDRCRQLRDCERSVTVAVPPQNLILTIKHFRYDQSR 234
Cdd:cd02664 126 FRDLDLSFP-------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKT 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 235 NLRAKLMNKILHNEDISLTI-------------------TDEAGHCRQLHYRNYAVVVHYGTSMDSGHYYTYAQDGTGT- 294
Cdd:cd02664 193 HVREKIMDNVSINEVLSLPVrveskssesplekkeeesgDDGELVTRQVHYRLYAVVVHSGYSSESGHYFTYARDQTDAd 272
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 157014223 295 --------------------WFKFNDNYVTECTTSELQNI 314
Cdd:cd02664 273 stgqecpepkdaeendesknWYLFNDSRVTFSSFESVQNV 312
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1-313 |
1.29e-54 |
|
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: 178.45 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTkqfctevllkqidappfseiqqllallihsrrpeltpravlastrppgfapgyQQDSSE 80
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFSE-----------------------------------------------------QQDAHE 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 81 FLSYLLDRLHEQEKKILNGNVTQQHNTSalissngsgtiatnstktLVQKTFEGQLSVGCLCTVCNSTNHTTETFRSLDL 160
Cdd:cd02257 28 FLLFLLDKLHEELKKSSKRTSDSSSLKS------------------LIHDLFGGKLESTIVCLECGHESVSTEPELFLSL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 161 SFPEDSDlsaagdGTHSVQKLLDYFCSSEKLVGENQYFCDRCRqLRDCERSVTVAVPPQNLILTIKHFRYDQSrNLRAKL 240
Cdd:cd02257 90 PLPVKGL------PQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 241 MNKILHNEDISLT------ITDEAGHCRQLHYRNYAVVVHYGTSMDSGHYYTYAQDG-TGTWFKFNDNYVTECTTSELQN 313
Cdd:cd02257 162 NTKVSFPLELDLSpylsegEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPsDGKWYKFNDDKVTEVSEEEVLE 241
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1-309 |
1.05e-47 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 162.23 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFcTEVLLKQIDAPPFSEIQQ-----------LLALLIHSRRPELTPRAVLASTR--P 67
Cdd:pfam00443 2 GLVNLGNTCYMNSVLQSLFSIPPF-RDYLLRISPLSEDSRYNKdinllcalrdlFKALQKNSKSSSVSPKMFKKSLGklN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 68 PGFAPGYQQDSSEFLSYLLDRLHEqekkILNGNVTQQhNTSalissngsgtiatnstktLVQKTFEGQLSVGCLCTVCNS 147
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHE----DLNGNHSTE-NES------------------LITDLFRGQLKSRLKCLSCGE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 148 TNHTTETFRSLDLSFPEDSDLSAagdgTHSVQKLLDYFCSSEKLVGENQYFCDRCRQLRDCERSVTVAVPPQNLILTIKH 227
Cdd:pfam00443 138 VSETFEPFSDLSLPIPGDSAELK----TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 228 FRYDqsRNLRAKLMNKILHNEDISLTITDEAGHCRQLH----YRNYAVVVHYGTSmDSGHYYTYAQDGT-GTWFKFNDNY 302
Cdd:pfam00443 214 FSYN--RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNnlqdYRLVAVVVHSGSL-SSGHYIAYIKAYEnNRWYKFDDEK 290
|
....*..
gi 157014223 303 VTECTTS 309
Cdd:pfam00443 291 VTEVDEE 297
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-306 |
3.14e-43 |
|
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: 150.50 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFCTEVLLKQ-------IDAPPFSEIQQLLALLIHSRRPELTPRAVLASTR--PPGFA 71
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREhskdccnEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKqiSKHFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 72 PGYQQDSSEFLSYLLDRLHeqekkilngnvtqqhnTSALISSNGSGTIATNS-TKTLVQKTFEGQLSVGCLCTVCNSTNH 150
Cdd:cd02661 83 IGRQEDAHEFLRYLLDAMQ----------------KACLDRFKKLKAVDPSSqETTLVQQIFGGYLRSQVKCLNCKHVSN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 151 TTETFrsLDLSFpedsDLSAAGdgthSVQKLLDYFCSSEKLVGENQYFCDRCRQLRDCERSVTVAVPPQNLILTIKHFRY 230
Cdd:cd02661 147 TYDPF--LDLSL----DIKGAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 231 DQsrnlraklMNKIlhNEDIS----LTITD-----EAGHCRqlhYRNYAVVVHYGTSMDSGHYYTYAQDGTGTWFKFNDN 301
Cdd:cd02661 217 FR--------GGKI--NKQISfpetLDLSPymsqpNDGPLK---YKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDS 283
|
....*
gi 157014223 302 YVTEC 306
Cdd:cd02661 284 KVSPV 288
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-313 |
9.03e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 136.65 E-value: 9.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTkqfctevllkqidappfseiqqllallihsrrpeltpravlastrppgfapgyQQDSSE 80
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSAD-----------------------------------------------------QQDAQE 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 81 FLSYLLDRLHeqekkilngnvtqqhntsalissngsgtiatnstkTLVQKTFEGQLSVGCLCTVCNSTNHTTETFRSLDL 160
Cdd:cd02674 28 FLLFLLDGLH-----------------------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSL 72
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 161 SFPEDSDLSAAGdgthSVQKLLDYFCSSEKLVGENQYFCDRCRQLRDCERSVTVAVPPQNLILTIKHFRYDQSRnlRAKL 240
Cdd:cd02674 73 PIPSGSGDAPKV----TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGS--TRKL 146
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157014223 241 MNKILHN-EDISLT-ITDEAGHCRQLHYRNYAVVVHYGTsMDSGHYYTYAQDG-TGTWFKFNDNYVTECTTSELQN 313
Cdd:cd02674 147 TTPVTFPlNDLDLTpYVDTRSFTGPFKYDLYAVVNHYGS-LNGGHYTAYCKNNeTNDWYKFDDSRVTKVSESSVVS 221
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-311 |
4.03e-38 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 137.77 E-value: 4.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFCTEVL--LKQIDAPPFSEI----QQLLALLIHSRRPELTPRaVLASTRPPGFAP-- 72
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYsiPPTEDDDDNKSVplalQRLFLFLQLSESPVKTTE-LTDKTRSFGWDSln 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 73 -GYQQDSSEFLSYLLDRLHEQEKKilngnvTQQHNtsalissngsgtiatnstktLVQKTFEGQLS--VGCLCtvCNSTN 149
Cdd:cd02659 83 tFEQHDVQEFFRVLFDKLEEKLKG------TGQEG--------------------LIKNLFGGKLVnyIICKE--CPHES 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 150 HTTETFrsldlsfpedSDLSAAGDGTHSVQKLLDYFCSSEKLVGENQYFCDRCRQLRDCERSVTVAVPPQNLILTIKHFR 229
Cdd:cd02659 135 EREEYF----------LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 230 YDQSRNLRAKL---------------MNKILHNEDISLTITDEAghcrQLHYRNYAVVVHYGTSmDSGHYYTYAQDGT-G 293
Cdd:cd02659 205 FDFETMMRIKIndrfefpleldmepyTEKGLAKKEGDSEKKDSE----SYIYELHGVLVHSGDA-HGGHYYSYIKDRDdG 279
|
330
....*....|....*...
gi 157014223 294 TWFKFNDNYVTECTTSEL 311
Cdd:cd02659 280 KWYKFNDDVVTPFDPNDA 297
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-313 |
3.48e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 129.80 E-value: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQAL------------------------------AMTKQFCTevlLKQIDAP-PFSEIQQLLALLI 49
Cdd:cd02660 2 GLINLGATCFMNVILQALlhnpllrnyflsdrhsctclscspnsclscAMDEIFQE---FYYSGDRsPYGPINLLYLSWK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 50 HSRRpeltpravLAstrppgfapGY-QQDSSEFLSYLLDRLHEQEKKILNGNVTqqhntsalissngsgtiaTNSTKTLV 128
Cdd:cd02660 79 HSRN--------LA---------GYsQQDAHEFFQFLLDQLHTHYGGDKNEAND------------------ESHCNCII 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 129 QKTFEGQLSVGCLCTVCNSTNHTTETFRSLDLSFPEDSDLSAA-----GDGTHSVQKLLDYFCSSEKLvGENQYFCDRCR 203
Cdd:cd02660 124 HQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWAlgesgVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 204 QLRDCERSVTVAVPPQNLILTIKHFRYdQSRNLRAKL-----------MNKILHNEDISLTITDEAGhcRQLHYRNYAVV 272
Cdd:cd02660 203 STQEATKQLSIKKLPPVLCFQLKRFEH-SLNKTSRKIdtyvqfplelnMTPYTSSSIGDTQDSNSLD--PDYTYDLFAVV 279
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 157014223 273 VHYGTsMDSGHYYTYAQDGTGTWFKFNDNYVTECTTSELQN 313
Cdd:cd02660 280 VHKGT-LDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLK 319
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-312 |
5.79e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 121.37 E-value: 5.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFCTEVLL-------------KQIDAPPFSEIQQL---LALLIHSRRPELTPRAVLAS 64
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstedaelknmpPDKPHEPQTIIDQLqliFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 65 TrppGFAPGYQQDSSEFLSYLLDRLHEQEKKILNGNVtqqhntsalissngsgtiatnstKTLVQKTFEGQLSVGCLCTV 144
Cdd:cd02668 81 L---GLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDL-----------------------KNIVQDLFRGEYSYVTQCSK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 145 CNSTNHTTETFRSLDLSFpedsdlsaagDGTHSVQKLLDYFCSSEKLVGENQYFCDRCRQLRDCERSVTVAVPPQNLILT 224
Cdd:cd02668 135 CGRESSLPSKFYELELQL----------KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 225 IKHFRYDQSRNLRAKLMNKILHNEDISLTITDEAGHCRQLHYRNYAVVVHYGTSMDSGHYYTYAQDG-TGTWFKFNDNYV 303
Cdd:cd02668 205 LLRFVFDRKTGAKKKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEqTGEWYKFNDEDV 284
|
....*....
gi 157014223 304 TECTTSELQ 312
Cdd:cd02668 285 EEMPGKPLK 293
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-313 |
1.14e-30 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 117.03 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAmtkqfctevllkqidappFSEIQQLLALLIHSRRpELTPRAVLASTRP---------PGFA 71
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY------------------FENLLTCLKDLFESIS-EQKKRTGVISPKKfitrlkrenELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 72 PGYQQDSSEFLSYLLDRLHEqekkilngnVTQQHNTSALISSNGSGTIATNSTKTLVQKTFEGQLSVGCLCTVCNSTNHT 151
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIAE---------ILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 152 TETFrsLDLSFpedsDLsaagDGTHSVQKLLDYFCSSEKLVGENQYFCDRCRQLRDCERSVTVAVPPQNLILTIKHFRYD 231
Cdd:cd02663 133 DETF--LDLSI----DV----EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 232 QSRNLRAKLMNKILHNEDISL-TITDEAGHCRQLhYRNYAVVVHYGTSMDSGHYYTYAQDgTGTWFKFNDNYVTECTTSE 310
Cdd:cd02663 203 EQLNRYIKLFYRVVFPLELRLfNTTDDAENPDRL-YELVAVVVHIGGGPNHGHYVSIVKS-HGGWLLFDDETVEKIDENA 280
|
...
gi 157014223 311 LQN 313
Cdd:cd02663 281 VEE 283
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-310 |
1.12e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 111.32 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFcTEVLLKqidappfseiqqllallihsrrpelTPRAVLASTR--PPGFAPGYQQDS 78
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPAL-RELLSE-------------------------TPKELFSQVCrkAPQFKGYQQQDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 79 SEFLSYLLDRLheqekkilngnvtqqhntsalissngsgtiatnstKTLVQKTFEGQLSVGCLCTVCNSTNHTTETFrsL 158
Cdd:cd02667 55 HELLRYLLDGL-----------------------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPF--L 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 159 DLSFPEDSDLsaagDGTHSVQKLLDYFCSSEKLVGENQYFCDRCRQLRdceRSVTVAVPPQNLILTIKHFRYDQSRNLRa 238
Cdd:cd02667 98 DLSLPRSDEI----KSECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLR- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 239 KLMNKILHNE--DISLTITDEAGHCR---QLHYRNYAVVVHYGTsMDSGHYYTYAQD----------------------G 291
Cdd:cd02667 170 KVSRHVSFPEilDLAPFCDPKCNSSEdksSVLYRLYGVVEHSGT-MRSGHYVAYVKVrppqqrlsdltkskpaadeagpG 248
|
330
....*....|....*....
gi 157014223 292 TGTWFKFNDNYVTECTTSE 310
Cdd:cd02667 249 SGQWYYISDSDVREVSLEE 267
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-314 |
1.79e-24 |
|
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: 101.12 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFCTEV--LLKQIDAppfSEIQQLLALLIHSRRPEL----TPRAVLASTRP--PGFAP 72
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLkhLVSLISS---VEQLQSSFLLNPEKYNDElanqAPRRLLNALREvnPMYEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 73 GYQQDSSEFLSYLLDRLHEqekkilngnvtqqhntsalissngsgtiatnstktLVQKTFEGQLSVGCLCTVCNSTNHTT 152
Cdd:cd02671 103 YLQHDAQEVLQCILGNIQE-----------------------------------LVEKDFQGQLVLRTRCLECETFTERR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 153 ETFRSLDLSFPEDSDLSAAGDGTHS---------VQKLLDYFCSSEKLVGENQYFCDRCRQLRDCERSVTVAVPPQNLIL 223
Cdd:cd02671 148 EDFQDISVPVQESELSKSEESSEISpdpktemktLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 224 TIKHFRYDQSRNLRAKLMNKIlhNEDISLTIT---DEAGHCRQLH-YRNYAVVVHYGTSMDSGHYYTYAQdgtgtWFKFN 299
Cdd:cd02671 228 HLKCFAANGSEFDCYGGLSKV--NTPLLTPLKlslEEWSTKPKNDvYRLFAVVMHSGATISSGHYTAYVR-----WLLFD 300
|
330
....*....|....*
gi 157014223 300 DNYVTECTTSELQNI 314
Cdd:cd02671 301 DSEVKVTEEKDFLEA 315
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-303 |
1.46e-21 |
|
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: 92.77 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFCTevLLKQIDAPPFSEIQ--------QLL----ALLIH-SRRPELTPRAVLAST-- 65
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQW--RYDDLENKFPSDVVdpandlncQLIkladGLLSGrYSKPASLKSENDPYQvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 66 -RP-----------PGFAPGYQQDSSEFLSYLLDRLHEQEKKILNGNVtqqhntsalissngsgtiaTNSTKTLVQKTFE 133
Cdd:cd02658 79 iKPsmfkaligkghPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNP-------------------NDLFKFMIEDRLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 134 gqlsvgclCTVCNSTNHTTETFRSLDLSFPEDsDLSAAGDG--THSVQKL---LDYFCSSEKLvgenQYFCDRCRQLRDC 208
Cdd:cd02658 140 --------CLSCKKVKYTSELSEILSLPVPKD-EATEKEEGelVYEPVPLedcLKAYFAPETI----EDFCSTCKEKTTA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 209 ERSVTVAVPPQNLILTIKHFRYDQsrNLRAKlmnKIlhneDISLTITDEAGHCRqlhYRNYAVVVHYGTSMDSGHYYTY- 287
Cdd:cd02658 207 TKTTGFKTFPDYLVINMKRFQLLE--NWVPK---KL----DVPIDVPEELGPGK---YELIAFISHKGTSVHSGHYVAHi 274
|
330
....*....|....*...
gi 157014223 288 --AQDGTGTWFKFNDNYV 303
Cdd:cd02658 275 kkEIDGEGKWVLFNDEKV 292
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1-314 |
1.06e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 87.16 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQ----------ALAMTKQFCTEVLLKQI--DAPP--FSEIQQLLALLIHSRRPEltpravLASTR 66
Cdd:COG5533 1 GLPNLGNTCFMNSVLQilalylpkldELLDDLSKELKVLKNVIrkPEPDlnQEEALKLFTALWSSKEHK------VGWIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 67 PpgfaPGYQQDSSEFLSYLLDRLHEQEkkilngnvtqqhntsalissngSGTIATNSTKTLVQKtfegqlsvgclctvcn 146
Cdd:COG5533 75 P----MGSQEDAHELLGKLLDELKLDL----------------------VNSFTIRIFKTTKDK---------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 147 sTNHTTETFRSLDLSFPEDSdlsaAGDGTHSVQKLLD---YFCSSEKLV--GENQYFCDRCRQLrdcERSVTVAVPpqnL 221
Cdd:COG5533 113 -KKTSTGDWFDIIIELPDQT----WVNNLKTLQEFIDnmeELVDDETGVkaKENEELEVQAKQE---YEVSFVKLP---K 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 222 ILTIKHFRYDQSrNLRAKLMNKIlhNEDISLTI-TDEAGHCRQ-LHYRNYAVVVHYGtSMDSGHYYTYAQDGtGTWFKFN 299
Cdd:COG5533 182 ILTIQLKRFANL-GGNQKIDTEV--DEKFELPVkHDQILNIVKeTYYDLVGFVLHQG-SLEGGHYIAYVKKG-GKWEKAN 256
|
330
....*....|....*
gi 157014223 300 DNYVTECTTSELQNI 314
Cdd:COG5533 257 DSDVTPVSEEEAINE 271
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1-310 |
1.56e-19 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 89.16 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFCTEVLLKQIDAP-PFSEIQQLLALLIHSRRPELTPRAVLASTRPPG---FAPGYQQ 76
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPrGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGwdsDDSFMQH 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 77 DSSEFLSYLLDRLhEQEKKilngnvtqqhntsalissngsgtiatnstKTLVQKTFEGQLsVGCLCTVCNSTNHTTETFR 156
Cdd:COG5077 275 DIQEFNRVLQDNL-EKSMR-----------------------------GTVVENALNGIF-VGKMKSYIKCVNVNYESAR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 157 SLDLSfpedsDLSAAGDGTHSVQKLLDYFCSSEKLVGENQYFCDRcRQLRDCERSVTVAVPPQNLILTIKHFRYDQSRNL 236
Cdd:COG5077 324 VEDFW-----DIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDM 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157014223 237 RAKLMNKILHNEDISLT--ITDEAGHCRQLH--YRNYAVVVHYGtSMDSGHYYTYAQDGT-GTWFKFNDNYVTECTTSE 310
Cdd:COG5077 398 MVKINDRYEFPLEIDLLpfLDRDADKSENSDavYVLYGVLVHSG-DLHEGHYYALLKPEKdGRWYKFDDTRVTRATEKE 475
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-311 |
5.06e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 78.56 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFcTEVLLKQIDappfseiqqllallihsrrpeltpravlastrppgfapgyQQDSSE 80
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSL-IEYLEEFLE----------------------------------------QQDAHE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 81 FLSYLLDRLHEQekkilngnvtqqhntsalissngsgtiatnstktlVQKTFEGQLSVGCLCTVCNSTNHTT-ETFRSLD 159
Cdd:cd02662 40 LFQVLLETLEQL-----------------------------------LKFPFDGLLASRIVCLQCGESSKVRyESFTMLS 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 160 LSFPEDSDLSaagdgTHSVQKLLDYFCSSEKLVGenqYFCDRCRQLrdcersvtVAVPPQNLILTIKHFRYDqSRNLRAK 239
Cdd:cd02662 85 LPVPNQSSGS-----GTTLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFD-GRGTSTK 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 240 LMNKILHNEDIsltitdeaghcRQLHYRNYAVVVHYGtSMDSGHYYTY---------------------AQDGTGTWFKF 298
Cdd:cd02662 148 NSCKVSFPERL-----------PKVLYRLRAVVVHYG-SHSSGHYVCYrrkplfskdkepgsfvrmregPSSTSHPWWRI 215
|
330
....*....|...
gi 157014223 299 NDNYVTECTTSEL 311
Cdd:cd02662 216 SDTTVKEVSESEV 228
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-310 |
1.82e-14 |
|
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: 72.91 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFCTEVLlkQIDAPPFSE--------------------------IQQLLAL---LIHS 51
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVL--NFDESKAELasdypterriggrevsrselqrsnqfVYELRSLfndLIHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 52 RRPELTPRAVLAstrppgFAPGYQQDSSEFLSYLLDRLHEQEKKILNGNVtqqhntsalissnGSGTIATNSTKTLVQKT 131
Cdd:cd02666 81 NTRSVTPSKELA------YLALRQQDVTECIDNVLFQLEVALEPISNAFA-------------GPDTEDDKEQSDLIKRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 132 FEG---QLSVGCLCTVCNSTNHTTETFRSLDLSFPEDSDLSAAGDGTHSVQKLLD-YFC--SSEKLVGENQYFCD----R 201
Cdd:cd02666 142 FSGktkQQLVPESMGNQPSVRTKTERFLSLLVDVGKKGREIVVLLEPKDLYDALDrYFDydSLTKLPQRSQVQAQlaqpL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 202 CRQLRDCERsvtvaVPPQNLILTIKHFRYD--QSRNLRAKLMNKILhnEDISLTITDEAGHCRQLHYRNYAVVVHYGTSm 279
Cdd:cd02666 222 QRELISMDR-----YELPSSIDDIDELIREaiQSESSLVRQAQNEL--AELKHEIEKQFDDLKSYGYRLHAVFIHRGEA- 293
|
330 340 350
....*....|....*....|....*....|..
gi 157014223 280 DSGHYYTYAQDGT-GTWFKFNDNYVTECTTSE 310
Cdd:cd02666 294 SSGHYWVYIKDFEeNVWRKYNDETVTVVPASE 325
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-308 |
3.52e-14 |
|
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: 71.59 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALamtkQFCTEVLLK------------QIDAPPFSEIQQLLALLIHSRRPeLTPRAVLASTRP- 67
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL----RSVPELRDAlknynparrganQSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLLRMa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 68 -PGFAP-----GY-QQDSSEFLSYLLDRLheqeKKILNGNVTQQHNTSALISSNGSGTIATNSTKTLVQKTFEGQLSVGC 140
Cdd:cd02657 76 fPQFAEkqnqgGYaQQDAEECWSQLLSVL----SQKLPGAGSKGSFIDQLFGIELETKMKCTESPDEEEVSTESEYKLQC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 141 LCTVCNSTNHTTEtfrSLDLSFPEDsdlsaagdgthsVQKLldyfcsSEKLVGENQYfcdrcrqlrdcERSVTVAVPPQN 220
Cdd:cd02657 152 HISITTEVNYLQD---GLKKGLEEE------------IEKH------SPTLGRDAIY-----------TKTSRISRLPKY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 221 LILTIKHFRYDQSRNLRAKLMNKIL--HNEDISlTITDEAGhcrqlHYRNYAVVVHYGTSMDSGHYYTYA-QDGTGTWFK 297
Cdd:cd02657 200 LTVQFVRFFWKRDIQKKAKILRKVKfpFELDLY-ELCTPSG-----YYELVAVITHQGRSADSGHYVAWVrRKNDGKWIK 273
|
330
....*....|.
gi 157014223 298 FNDNYVTECTT 308
Cdd:cd02657 274 FDDDKVSEVTE 284
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-307 |
1.76e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 70.43 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQFCTEVLLKQIDAPPF---SEIQQLLALLI----HSR------RP-ELTPRAVLASTR 66
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKdrkSELVKRLSELIrkiwNPRnfkghvSPhELLQAVSKVSKK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 67 PpgFAPGYQQDSSEFLSYLLDRLHEQEKKILNGNvtqqhntSALISSNGSGTIATNSTKTLVQKTFEGQLSVGCLCTVCN 146
Cdd:cd02669 201 K--FSITEQSDPVEFLSWLLNTLHKDLGGSKKPN-------SSIIHDCFQGKVQIETQKIKPHAEEEGSKDKFFKDSRVK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 147 STNHTTETFRSLDL-SFPEDSDLSAAGDGTH-SVQKLLD-YFCSSEKLVGENqyfcdRCRQLrdcersvtVAVPPQNLIL 223
Cdd:cd02669 272 KTSVSPFLLLTLDLpPPPLFKDGNEENIIPQvPLKQLLKkYDGKTETELKDS-----LKRYL--------ISRLPKYLIF 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 224 TIKHF---RYDQSRNlrAKLMNKILHNEDISLTIT-DEAGHCRQLHYRNYAVVVHYGTSMDSGHYYTY-AQDGTGTWFKF 298
Cdd:cd02669 339 HIKRFsknNFFKEKN--PTIVNFPIKNLDLSDYVHfDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQlRHKSTNKWFEI 416
|
....*....
gi 157014223 299 NDNYVTECT 307
Cdd:cd02669 417 QDLNVKEVL 425
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1-165 |
8.23e-12 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 66.06 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALAMTKQ----FCTEVLLKQIDAPPFSEIQQLLALLIHSRRPEL-TPRavLASTRPPGFA---- 71
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWElrdyFLSDEYEESINEENPLGMHGSVASAYADLIKQLyDGN--LHAFTPSGFKktig 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 72 ------PGY-QQDSSEFLSYLLDRLHEQEKKILNGNVTQQ------HNTSALISSNGSGTIATNSTKTLVQKTFEGQLSV 138
Cdd:COG5560 345 sfneefSGYdQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKpdlspgDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKS 424
|
170 180
....*....|....*....|....*..
gi 157014223 139 GCLCTVCNSTNHTTETFRSLDLSFPED 165
Cdd:COG5560 425 TLTCPGCGSVSITFDPFMDLTLPLPVS 451
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
175-305 |
5.21e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 60.28 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 175 THSVQKLLDYFCSSEKLVGENQYFCDRCRQLRDCERSVTVAVPPQNLILTIKHFRYDQS-RNLRAKLMNKILHNEDISLT 253
Cdd:COG5560 674 TITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSfRDKIDDLVEYPIDDLDLSGV 753
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 157014223 254 ITDEAGhcRQLHYRNYAVVVHYGtSMDSGHYYTYAQD-GTGTWFKFNDNYVTE 305
Cdd:COG5560 754 EYMVDD--PRLIYDLYAVDNHYG-GLSGGHYTAYARNfANNGWYLFDDSRITE 803
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-312 |
9.12e-07 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 49.09 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 1 GLVNLGNTCYMNSVVQALamtkqfctevllkqidappFSEiqqllallihsrrpeltpravlastrppgfapgyQQDSSE 80
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSL-------------------FSQ----------------------------------QQDVSE 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 81 FLSYLLDRL----------HEQEKKILNGNVTQQHNTSalissngsgtiatnstktLVQKTFEGQLSvgCLCTVCNSTNH 150
Cdd:cd02665 28 FTHLLLDWLedafqaaaeaISPGEKSKNPMVQLFYGTF------------------LTEGVLEGKPF--CNCETFGQYPL 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 151 TTETFRSLDLSFpEDSDLSAAGDGTHSVQklldyfcsSEKLVGENQYfcdrcrqlrdcersvtVAVPPqnlILTIKHFRY 230
Cdd:cd02665 88 QVNGYGNLHECL-EAAMFEGEVELLPSDH--------SVKSGQERWF----------------TELPP---VLTFELSRF 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 231 DQSRNLRAKLMNKILHNEDIsltitdeaghcRQLHYRNYAVVVHYGTSmDSGHYYTYAQDGT-GTWFKFNDNYVTECTTS 309
Cdd:cd02665 140 EFNQGRPEKIHDKLEFPQII-----------QQVPYELHAVLVHEGQA-NAGHYWAYIYKQSrQEWEKYNDISVTESSWE 207
|
...
gi 157014223 310 ELQ 312
Cdd:cd02665 208 EVE 210
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2-311 |
3.58e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 38.28 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 2 LVNLGNTCYMNSVVQALAMTKQFCTEvllkqidappfseiqqllallihsrrpeltpravlastrppgFAPGYQQDSSEF 81
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSIGKINTE------------------------------------------FDNDDQQDAHEF 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 82 LSYLLDRLHEQEKKILNGNVTQQHNTSALISSNgsgtiatnSTKTLVQKTFegqlsvgcLCTVC--NSTNHTTETFRSL- 158
Cdd:cd02673 40 LLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLE--------AFKYTIESSY--------VCIGCsfEENVSDVGNFLDVs 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014223 159 --DLSFPEDSDLSAAGDGTHSVQKLldyfCSSEKlvgenqyfcdrCRQLRDCERSVTVavpPQNLILTIKHF--RYDQSR 234
Cdd:cd02673 104 miDNKLDIDELLISNFKTWSPIEKD----CSSCK-----------CESAISSERIMTF---PECLSINLKRYklRIATSD 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157014223 235 NLRaklmnkilHNEDISLTITDEAGHcrqlhYRNYAVVVHYGTSMDSGHYYTYAQDGTG--TWFKFNDNYVTECTTSEL 311
Cdd:cd02673 166 YLK--------KNEEIMKKYCGTDAK-----YSLVAVICHLGESPYDGHYIAYTKELYNgsSWLYCSDDEIRPVSKNDV 231
|
|
| |
