|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
1.13e-110 |
|
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: 322.41 E-value: 1.13e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAvrylkdyflnpvaagasegplTSALRRFFLEingdnleafsgnakkrhrdyttyNPKGLF 80
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQ---------------------TPALRELLSE-----------------------TPKELF 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 81 GALCSKSSRFSGYHQQDSHELLRCLLDGLQvegkhkeseeknsangkedhTFVDHLFGGQFASTVTCCECGHSSSVLEPF 160
Cdd:cd02667 37 SQVCRKAPQFKGYQQQDSHELLRYLLDGLR--------------------TFIDSIFGGELTSTIMCESCGTVSLVYEPF 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 161 LDVSLPI--PFITAKSLEGCLQAFTKLEVLSGENAWGCDNCTrrKATKRLVIRKAPPVLTVHLKRFAQDMRGRLSKLTGH 238
Cdd:cd02667 97 LDLSLPRsdEIKSECSIESCLKQFTEVEILEGNNKFACENCT--KAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRH 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 239 VAFDELLNLSPFLSTSRDGG------LYRLVGVVEHSGTMKGGHYVAFVRGG-------------SAGDGKENF---WYY 296
Cdd:cd02667 175 VSFPEILDLAPFCDPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltkskPAADEAGPGsgqWYY 254
|
330 340
....*....|....*....|....
gi 300141194 297 ISDSDVRRTTLDQVLRSEAYLLFY 320
Cdd:cd02667 255 ISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1-320 |
4.19e-83 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 253.52 E-value: 4.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRYLKDYFLNPVAAGASEGPLTS-----ALRRFFLEINGdnleafsgNAKKRHrdyttYN 75
Cdd:pfam00443 2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinllcALRDLFKALQK--------NSKSSS-----VS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 76 PKGLFGALCSKSSRFSGYHQQDSHELLRCLLDGLQvegkhkesEEKNSANGKEDHTFVDHLFGGQFASTVTCCECGHSSS 155
Cdd:pfam00443 69 PKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLH--------EDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 156 VLEPFLDVSLPIPFITAKSLEG----CLQAFTKLEVLSGENAWGCDNCTRRK-ATKRLVIRKAPPVLTVHLKRFAQDMRG 230
Cdd:pfam00443 141 TFEPFSDLSLPIPGDSAELKTAslqiCFLQFSKLEELDDEEKYYCDKCGCKQdAIKQLKISRLPPVLIIHLKRFSYNRST 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 231 RlSKLTGHVAFDELLNLSPFLSTSRDGGL-----YRLVGVVEHSGTMKGGHYVAFVRggsagDGKENFWYYISDSDVRRT 305
Cdd:pfam00443 221 W-EKLNTEVEFPLELDLSRYLAEELKPKTnnlqdYRLVAVVVHSGSLSSGHYIAYIK-----AYENNRWYKFDDEKVTEV 294
|
330
....*....|....*.
gi 300141194 306 TLD-QVLRSEAYLLFY 320
Cdd:pfam00443 295 DEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
3.54e-79 |
|
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: 243.34 E-value: 3.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRYLKDYFLNPVAAGASEGPLTSALRRFFLEINGDNLEAFSGNAKKRHRDyttynpkglf 80
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSS---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 81 gALCSKSSRFSGYHQQDSHELLRCLLDGLqvegkHKESEEKNSANGKEDH-----TFVDHLFGGQFASTVTCCECGHSSS 155
Cdd:cd02661 73 -NLKQISKHFRIGRQEDAHEFLRYLLDAM-----QKACLDRFKKLKAVDPssqetTLVQQIFGGYLRSQVKCLNCKHVSN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 156 VLEPFLDVSLPIPfiTAKSLEGCLQAFTKLEVLSGENAWGCDNCTRR-KATKRLVIRKAPPVLTVHLKRFAQDMRGRLSK 234
Cdd:cd02661 147 TYDPFLDLSLDIK--GADSLEDALEQFTKPEQLDGENKYKCERCKKKvKASKQLTIHRAPNVLTIHLKRFSNFRGGKINK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 235 ltgHVAFDELLNLSPFLSTSRDGGL-YRLVGVVEHSGT-MKGGHYVAFVRggsAGDGKenfWYYISDSDVRRTTLDQVLR 312
Cdd:cd02661 225 ---QISFPETLDLSPYMSQPNDGPLkYKLYAVLVHSGFsPHSGHYYCYVK---SSNGK---WYNMDDSKVSPVSIETVLS 295
|
....*...
gi 300141194 313 SEAYLLFY 320
Cdd:cd02661 296 QKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1-320 |
2.40e-73 |
|
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: 226.60 E-value: 2.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAvrylkdyflnpvaagasegpltsalrrffleingdnleafsgnakkrhrdyttynpkglf 80
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 81 galcskssrfsgyHQQDSHELLRCLLDGLQVEGKhkeSEEKNSANGKEDHTFVDHLFGGQFASTVTCCECGHSS--SVLE 158
Cdd:cd02257 21 -------------EQQDAHEFLLFLLDKLHEELK---KSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESvsTEPE 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 159 PFLDVSLPIPFITAKSLEGCLQAFTKLEVLSGENAWGCDNCTRRKATKRLVIRKAPPVLTVHLKRFAQDMRGRLSKLTGH 238
Cdd:cd02257 85 LFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 239 VAFDELLNLSPFLSTSRDG-------GLYRLVGVVEHSGTMK-GGHYVAFVRggsagDGKENFWYYISDSDVRRTTLDQV 310
Cdd:cd02257 165 VSFPLELDLSPYLSEGEKDsdsdngsYKYELVAVVVHSGTSAdSGHYVAYVK-----DPSDGKWYKFNDDKVTEVSEEEV 239
|
330
....*....|....*
gi 300141194 311 LR-----SEAYLLFY 320
Cdd:cd02257 240 LEfgslsSSAYILFY 254
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
2.58e-66 |
|
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: 207.91 E-value: 2.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAvrylkdyflnpvaagasegpltsalrrffleingdnleafsgnakkrhrdyttynpkglf 80
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 81 galcskssrfsgyHQQDSHELLRCLLDGLqvegkhkeseeknsangkedHTFVDHLFGGQFASTVTCCECGHSSSVLEPF 160
Cdd:cd02674 21 -------------DQQDAQEFLLFLLDGL--------------------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 161 LDVSLPIPFITAK----SLEGCLQAFTKLEVLSGENAWGCDNC-TRRKATKRLVIRKAPPVLTVHLKRFAQDmRGRLSKL 235
Cdd:cd02674 68 TYLSLPIPSGSGDapkvTLEDCLRLFTKEETLDGDNAWKCPKCkKKRKATKKLTISRLPKVLIIHLKRFSFS-RGSTRKL 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 236 TGHVAFD-ELLNLSPFLSTSRDGG--LYRLVGVVEHSGTMKGGHYVAFVRGGSAGDgkenfWYYISDSDVRRTTLDQVLR 312
Cdd:cd02674 147 TTPVTFPlNDLDLTPYVDTRSFTGpfKYDLYAVVNHYGSLNGGHYTAYCKNNETND-----WYKFDDSRVTKVSESSVVS 221
|
....*...
gi 300141194 313 SEAYLLFY 320
Cdd:cd02674 222 SSAYILFY 229
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
3.09e-65 |
|
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: 208.38 E-value: 3.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRYLKDYFLNPVAAGASEGP-----LTSALRRFFleingdnlEAFSGNAKKrhrdyTTYN 75
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCspnscLSCAMDEIF--------QEFYYSGDR-----SPYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 76 PKGLFGALCSKSSRFSGYHQQDSHELLRCLLDGLqvegkHKESEEKNSANGKEDHT--FVDHLFGGQFASTVTCCECGHS 153
Cdd:cd02660 69 PINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQL-----HTHYGGDKNEANDESHCncIIHQTFSGSLQSSVTCQRCGGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 154 SSVLEPFLDVSLPIPFITAKS-------------LEGCLQAFTKLEVLsGENAWGCDNC-TRRKATKRLVIRKAPPVLTV 219
Cdd:cd02660 144 STTVDPFLDLSLDIPNKSTPSwalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCgSTQEATKQLSIKKLPPVLCF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 220 HLKRFAQDMRGRLSKLTGHVAFDELLNLSPFLSTSR----------DGGLYRLVGVVEHSGTMKGGHYVAFVRGGsagdg 289
Cdd:cd02660 223 QLKRFEHSLNKTSRKIDTYVQFPLELNMTPYTSSSIgdtqdsnsldPDYTYDLFAVVVHKGTLDTGHYTAYCRQG----- 297
|
330 340 350
....*....|....*....|....*....|.
gi 300141194 290 kENFWYYISDSDVRRTTLDQVLRSEAYLLFY 320
Cdd:cd02660 298 -DGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-311 |
1.07e-54 |
|
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: 181.30 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRYLKDYFLN--PVAAGASEGPLTSALRRFFLEINgdnleaFSgnakkrHRDYTTYNPKG 78
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSipPTEDDDDNKSVPLALQRLFLFLQ------LS------ESPVKTTELTD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 79 LFGALCSKSSrfSGYHQQDSHELLRCLLDGLqvEGKHKESEEKNSangkedhtfVDHLFGGQFASTVTCCECGHSSSVLE 158
Cdd:cd02659 72 KTRSFGWDSL--NTFEQHDVQEFFRVLFDKL--EEKLKGTGQEGL---------IKNLFGGKLVNYIICKECPHESEREE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 159 PFLDVSLPI-PFitaKSLEGCLQAFTKLEVLSGENAWGCDNC-TRRKATKRLVIRKAPPVLTVHLKRFAQDM-RGRLSKL 235
Cdd:cd02659 139 YFLDLQVAVkGK---KNLEESLDAYVQGETLEGDNKYFCEKCgKKVDAEKGVCFKKLPPVLTLQLKRFEFDFeTMMRIKI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 236 TGHVAFDELLNLSPFLSTSRDGG------------LYRLVGVVEHSGTMKGGHYVAFVRggsagDGKENFWYYISDSDVR 303
Cdd:cd02659 216 NDRFEFPLELDMEPYTEKGLAKKegdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIK-----DRDDGKWYKFNDDVVT 290
|
....*...
gi 300141194 304 RTTLDQVL 311
Cdd:cd02659 291 PFDPNDAE 298
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
6.54e-44 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 150.59 E-value: 6.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRYLKDYflnpvaagasegpltsalrrffleingdnLEAFSGnakkrhrdyttynpkglf 80
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-----------------------------LEEFLE------------------ 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 81 galcskssrfsgyhQQDSHELLRCLLDGLQVEgkhkeseeknsangkedhtfVDHLFGGQFASTVTCCECGHSSSV-LEP 159
Cdd:cd02662 34 --------------QQDAHELFQVLLETLEQL--------------------LKFPFDGLLASRIVCLQCGESSKVrYES 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 160 FLDVSLPIPF---ITAKSLEGCLQAFTKLEVLSGenaWGCDNCtrrkatkRLVIRKAPPVLTVHLKRFAQDMRGRLSKLT 236
Cdd:cd02662 80 FTMLSLPVPNqssGSGTTLEHCLDDFLSTEIIDD---YKCDRC-------QTVIVRLPQILCIHLSRSVFDGRGTSTKNS 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 237 GHVAFDELLNlspflstsrdGGLYRLVGVVEHSGTMKGGHYVAFVRGGSAGDGKENF---------------WYYISDSD 301
Cdd:cd02662 150 CKVSFPERLP----------KVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKDKEPGsfvrmregpsstshpWWRISDTT 219
|
330 340
....*....|....*....|
gi 300141194 302 VRRTTLDQVL-RSEAYLLFY 320
Cdd:cd02662 220 VKEVSESEVLeQKSAYMLFY 239
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-302 |
1.09e-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: 141.79 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSvmqnllavrYLKDYFLNpvaagasegpltSALRRFFLEIN-GDNLEAFSGNAKKRHRDYTT------ 73
Cdd:cd02668 1 GLKNLGATCYVNS---------FLQLWFMN------------LEFRKAVYECNsTEDAELKNMPPDKPHEPQTIidqlql 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 74 ------------YNPKGLFGALcskssRFSGYHQQDSHELLRCLLDGLQVE-GKHKESEEKNsangkedhtFVDHLFGGQ 140
Cdd:cd02668 60 ifaqlqfgnrsvVDPSGFVKAL-----GLDTGQQQDAQEFSKLFLSLLEAKlSKSKNPDLKN---------IVQDLFRGE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 141 FASTVTCCECGHSSSVLEPFLDVSLPIPfiTAKSLEGCLQAFTKLEVLSGENAWGCDNCTRRK-ATKRLVIRKAPPVLTV 219
Cdd:cd02668 126 YSYVTQCSKCGRESSLPSKFYELELQLK--GHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTdATRRIRLTTLPPTLNF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 220 HLKRFAQDMR-GRLSKLTGHVAFDELLNLSPFLSTSRDGG-LYRLVGVVEHSGT-MKGGHYVAFVRGGSAGDgkenfWYY 296
Cdd:cd02668 204 QLLRFVFDRKtGAKKKLNASISFPEILDMGEYLAESDEGSyVYELSGVLIHQGVsAYSGHYIAHIKDEQTGE-----WYK 278
|
....*.
gi 300141194 297 ISDSDV 302
Cdd:cd02668 279 FNDEDV 284
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
2.36e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 140.14 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLlavrylkdYFLNpvaagasegpLTSALRRFFleingdnlEAFSGNAKKrhrdYTTYNPKGLF 80
Cdd:cd02663 1 GLENFGNTCYCNSVLQAL--------YFEN----------LLTCLKDLF--------ESISEQKKR----TGVISPKKFI 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 81 GALCSKSSRFSGYHQQDSHELLRCLLDGL-----QVEGKHKESEEKNSANGKED-HTFVDHLFGGQFASTVTCCECGHSS 154
Cdd:cd02663 51 TRLKRENELFDNYMHQDAHEFLNFLLNEIaeildAERKAEKANRKLNNNNNAEPqPTWVHEIFQGILTNETRCLTCETVS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 155 SVLEPFLDVSLPIPfiTAKSLEGCLQAFTKLEVLSGENAWGCDNC-TRRKATKRLVIRKAPPVLTVHLKRFAQDMR-GRL 232
Cdd:cd02663 131 SRDETFLDLSIDVE--QNTSITSCLRQFSATETLCGRNKFYCDECcSLQEAEKRMKIKKLPKILALHLKRFKYDEQlNRY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 233 SKLTGHVAFDELLNLSpflSTSRDGG----LYRLVGVVEHSG-TMKGGHYVAFVRGGsagdgkeNFWY--------YISD 299
Cdd:cd02663 209 IKLFYRVVFPLELRLF---NTTDDAEnpdrLYELVAVVVHIGgGPNHGHYVSIVKSH-------GGWLlfddetveKIDE 278
|
330 340
....*....|....*....|.
gi 300141194 300 SDVRRTTLDQVLRSEAYLLFY 320
Cdd:cd02663 279 NAVEEFFGDSPNQATAYVLFY 299
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
5.85e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 140.03 E-value: 5.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLlavrylkdYFlnpvAAGasegpLTSALRRFF-LEINGDNLEA-FSGNAKKRHRDYTTYNPKG 78
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVL--------YF----CPG-----FKHGLKHLVsLISSVEQLQSsFLLNPEKYNDELANQAPRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 79 LFGALCSKSSRFSGYHQQDSHELLRCLLDGLQvegkhkeseeknsangkedhTFVDHLFGGQFASTVTCCECGHSSSVLE 158
Cdd:cd02671 89 LLNALREVNPMYEGYLQHDAQEVLQCILGNIQ--------------------ELVEKDFQGQLVLRTRCLECETFTERRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 159 PFLDVSLPI-----------------PFITAKSLEGCLQAFTKLEVLSGENAWGCDNCTR-RKATKRLVIRKAPPVLTVH 220
Cdd:cd02671 149 DFQDISVPVqeselskseesseispdPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHyTEAERSLLFDKLPEVITIH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 221 LKRFAQ-----DMRGRLSKLTGHVAfdELLNLSPF-LSTSRDGGLYRLVGVVEHSG-TMKGGHYVAFVRggsagdgkenf 293
Cdd:cd02671 229 LKCFAAngsefDCYGGLSKVNTPLL--TPLKLSLEeWSTKPKNDVYRLFAVVMHSGaTISSGHYTAYVR----------- 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 300141194 294 WYYISDSDVRRTTLDQVLR---------SEAYLLFY 320
Cdd:cd02671 296 WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
1.53e-32 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 122.99 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRYLKDYFL--NPVAAGASEGPLTSALRRF-FLEIngdnleafsgnakkrHRDYTTYNPK 77
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLslNLPRLGDSQSVMKKLQLLQaHLMH---------------TQRRAEAPPD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 78 GLFGAlcSKSSRFSGYHQQDSHELLRCLLDGLqvegkhkeseeknsangkedHTFVDHLFGGQFASTVTCCECGHSSSVL 157
Cdd:cd02664 66 YFLEA--SRPPWFTPGSQQDCSEYLRYLLDRL--------------------HTLIEKMFGGKLSTTIRCLNCNSTSART 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 158 EPFLDVSLPIPfitakSLEGCLQAFTKLEVLSGENAWGCDNCTRRK-ATKRLVIRKAPPVLTVHLKRFAQDMRGRL-SKL 235
Cdd:cd02664 124 ERFRDLDLSFP-----SVQDLLNYFLSPEKLTGDNQYYCEKCASLQdAEKEMKVTGAPEYLILTLLRFSYDQKTHVrEKI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 236 TGHVAFDELLNLsPFLSTSRDGGL---------------------YRLVGVVEHSGT-MKGGHYVAFVRGGSAGDGKENF 293
Cdd:cd02664 199 MDNVSINEVLSL-PVRVESKSSESplekkeeesgddgelvtrqvhYRLYAVVVHSGYsSESGHYFTYARDQTDADSTGQE 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 300141194 294 ---------------WYYISDSDVRRTT---LDQVL---RSE-AYLLFY 320
Cdd:cd02664 278 cpepkdaeendesknWYLFNDSRVTFSSfesVQNVTsrfPKDtPYILFY 326
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
7.13e-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 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: 115.12 E-value: 7.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRYLKD----YFLNPVAAGASEGPLTSALRRFFleingDNLEafsgnaKKRhrdyTTYNP 76
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalknYNPARRGANQSSDNLTNALRDLF-----DTMD------KKQ----EPVPP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 77 KGLFGALCSKSSRFS------GYHQQDSHELLRCLLDGLQVEGKHKESEEKnsangkedhtFVDHLFGGQFASTVTCCEC 150
Cdd:cd02657 66 IEFLQLLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKGS----------FIDQLFGIELETKMKCTES 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 151 GHSSSV-LEPFL------DVSLPIPFITAKSLEGCLQAFTKLEVLSGENAwgcdnctrrKATKRLVIRKAPPVLTVHLKR 223
Cdd:cd02657 136 PDEEEVsTESEYklqchiSITTEVNYLQDGLKKGLEEEIEKHSPTLGRDA---------IYTKTSRISRLPKYLTVQFVR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 224 FA-QDMRGRLSKLTGHVAFDELLNLSPFLSTSrdgGLYRLVGVVEHSG-TMKGGHYVAFVRggSAGDGKenfWYYISDSD 301
Cdd:cd02657 207 FFwKRDIQKKAKILRKVKFPFELDLYELCTPS---GYYELVAVITHQGrSADSGHYVAWVR--RKNDGK---WIKFDDDK 278
|
330 340
....*....|....*....|....*.
gi 300141194 302 VRRTTLDQVLRSE-------AYLLFY 320
Cdd:cd02657 279 VSEVTEEDILKLSgggdwhiAYILLY 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1-311 |
1.17e-29 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 119.20 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRYL-KDYFLNPVAAGASEGPLTSALRRFFLEINgdnleafsgnaKKRHRDYTTYNPKGl 79
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFrKDVYGIPTDHPRGRDSVALALQRLFYNLQ-----------TGEEPVDTTELTRS- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 80 FGAlcsksSRFSGYHQQDSHELLRCLLDGLqvEGKHKESEEKNSANGkedhtfvdhLFGGQFASTVTCCECGHSSSVLEP 159
Cdd:COG5077 263 FGW-----DSDDSFMQHDIQEFNRVLQDNL--EKSMRGTVVENALNG---------IFVGKMKSYIKCVNVNYESARVED 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 160 FLDVSLPIPfiTAKSLEGCLQAFTKLEVLSGENAWGCDNCTRRKATKRLVIRKAPPVLTVHLKRFAQDM-RGRLSKLTGH 238
Cdd:COG5077 327 FWDIQLNVK--GMKNLQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDFeRDMMVKINDR 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300141194 239 VAFDELLNLSPFLSTSRD-----GGLYRLVGVVEHSGTMKGGHYVAFVRggsagDGKENFWYYISDSDVRRTTLDQVL 311
Cdd:COG5077 405 YEFPLEIDLLPFLDRDADksensDAVYVLYGVLVHSGDLHEGHYYALLK-----PEKDGRWYKFDDTRVTRATEKEVL 477
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
2.31e-26 |
|
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: 105.87 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAV-----RYLKDY--FLNPVAAGASEgpLTSALRRFfleinGDNLeaFSGNAKKRHRDYTT 73
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIpsfqwRYDDLEnkFPSDVVDPAND--LNCQLIKL-----ADGL--LSGRYSKPASLKSE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 74 YNP--KGL----FGALCSKS-SRFSGYHQQDSHELLRCLLDGLQVEGKHKESEEKNSangkedhtfvdhLFGGQFASTVT 146
Cdd:cd02658 72 NDPyqVGIkpsmFKALIGKGhPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPND------------LFKFMIEDRLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 147 CCECGHSSSVLEPFLDVSLPIPF--ITAK----------SLEGCLQAFTKLEVLsgENAWgCDNCTRRKATKRLVIRKAP 214
Cdd:cd02658 140 CLSCKKVKYTSELSEILSLPVPKdeATEKeegelvyepvPLEDCLKAYFAPETI--EDFC-STCKEKTTATKTTGFKTFP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 215 PVLTVHLKRFAQDMRGRLSKLTGHVAFDELLnlspflstsrDGGLYRLVGVVEHSGT-MKGGHYVAFVRGGSAGDGKenf 293
Cdd:cd02658 217 DYLVINMKRFQLLENWVPKKLDVPIDVPEEL----------GPGKYELIAFISHKGTsVHSGHYVAHIKKEIDGEGK--- 283
|
330 340
....*....|....*....|....*..
gi 300141194 294 WYYISDSDVRRTTLDQVLRSEAYLLFY 320
Cdd:cd02658 284 WVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1-320 |
3.56e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 102.19 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLlaVRYLKDYflNPVAagaseGPLTSALRRFFLEINGDNleafsgnaKKRHRDYTTYNPKGLF 80
Cdd:COG5533 1 GLPNLGNTCFMNSVLQIL--ALYLPKL--DELL-----DDLSKELKVLKNVIRKPE--------PDLNQEEALKLFTALW 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 81 GALCSKSSR-FSGYHQQDSHELLRCLLDGLQVEGKHKESEEKNSANGKEDHTFVDHLFggqfastvtccecghsssvlep 159
Cdd:COG5533 64 SSKEHKVGWiPPMGSQEDAHELLGKLLDELKLDLVNSFTIRIFKTTKDKKKTSTGDWF---------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 160 flDVSLPIPFITA----KSLEGCLQAFTKLeVLSGENAWGCDN---CTRRKATKRLVIRKAPPVLTVHLKRFAQDMRGRl 232
Cdd:COG5533 122 --DIIIELPDQTWvnnlKTLQEFIDNMEEL-VDDETGVKAKENeelEVQAKQEYEVSFVKLPKILTIQLKRFANLGGNQ- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 233 sKLTGHVafDELLNLSpfLSTSRDGGL-----YRLVGVVEHSGTMKGGHYVAFVRggsagdgKENFWYYISDSDVR---R 304
Cdd:COG5533 198 -KIDTEV--DEKFELP--VKHDQILNIvketyYDLVGFVLHQGSLEGGHYIAYVK-------KGGKWEKANDSDVTpvsE 265
|
330
....*....|....*.
gi 300141194 305 TTLDQVLRSEAYLLFY 320
Cdd:COG5533 266 EEAINEKAKNAYLYFY 281
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
153-320 |
1.52e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 101.11 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 153 SSSVLEPFLDVSLPIPFITaksLEGCLQAFTKLEVLSGENAWGCDNCT-RRKATKRLVIRKAPPVLTVHLKRFAQDMRGR 231
Cdd:COG5560 658 SYDPLWTIREIGAAERTIT---LQDCLNEFSKPEQLGLSDSWYCPGCKeFRQASKQMELWRLPMILIIHLKRFSSVRSFR 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 232 --LSKLTGHVAFDelLNLSPFLSTSRDGGL-YRLVGVVEHSGTMKGGHYVAFVRggsagDGKENFWYYISDSDVRRTTLD 308
Cdd:COG5560 735 dkIDDLVEYPIDD--LDLSGVEYMVDDPRLiYDLYAVDNHYGGLSGGHYTAYAR-----NFANNGWYLFDDSRITEVDPE 807
|
170
....*....|..
gi 300141194 309 QVLRSEAYLLFY 320
Cdd:COG5560 808 DSVTSSAYVLFY 819
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1-168 |
6.26e-22 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 96.49 E-value: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRYLKDYFL-----------NPVAAGASegpLTSALRRFFLEINGDNLEAFSgnakkrhr 69
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLsdeyeesineeNPLGMHGS---VASAYADLIKQLYDGNLHAFT-------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 70 dyttynPKGLFGALCSKSSRFSGYHQQDSHELLRCLLDGLQ---------------------VEGKHKESEEKNSANGKE 128
Cdd:COG5560 336 ------PSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHedlnriikkpytskpdlspgdDVVVKKKAKECWWEHLKR 409
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300141194 129 DHTFVDHLFGGQFASTVTCCECGHSSSVLEPFLDVSLPIP 168
Cdd:COG5560 410 NDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLP 449
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2-320 |
2.09e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 66.01 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 2 LVNLGNTCFFNSVMQNLlavrylkdyflnpvaagasegpltSALRRFFLEINGDNleafsgnakkrhrdyttynpkglfg 81
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL------------------------SSIGKINTEFDNDD------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 82 alcskssrfsgyhQQDSHE----LLRCLLDGLQVEGKHKESEEKNsangkedhtfVDHL-----FGGQFASTVTCCECGH 152
Cdd:cd02673 33 -------------QQDAHEflltLLEAIDDIMQVNRTNVPPSNIE----------IKRLnpleaFKYTIESSYVCIGCSF 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 153 SSSV--LEPFLDVSL-PIPFITAKSLEGCLQAFTKLEVLsgenawgCDNCTRRKATKRLVIRKAPPVLTVHLKRFaqdmr 229
Cdd:cd02673 90 EENVsdVGNFLDVSMiDNKLDIDELLISNFKTWSPIEKD-------CSSCKCESAISSERIMTFPECLSINLKRY----- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 230 gRLSKLTGHVAFDELLNLSPFLSTSrdgGLYRLVGVVEHSG-TMKGGHYVAFVRGgsagDGKENFWYYISDSDVRRTTLD 308
Cdd:cd02673 158 -KLRIATSDYLKKNEEIMKKYCGTD---AKYSLVAVICHLGeSPYDGHYIAYTKE----LYNGSSWLYCSDDEIRPVSKN 229
|
330
....*....|....*
gi 300141194 309 QVL---RSEAYLLFY 320
Cdd:cd02673 230 DVStnaRSSGYLIFY 244
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
103-295 |
3.65e-12 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 65.75 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 103 RCLLDGLqvegkHKESEEKNSaNGKEDHTFVDHLFGGQFASTVTCCECGHSS---SVLePFLDVSLPIPFITAK------ 173
Cdd:pfam13423 104 RFLLDQL-----SSEENSTPP-NPSPAESPLEQLFGIDAETTIRCSNCGHESvreSST-HVLDLIYPRKPSSNNkkppnq 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 174 SLEGCLQAFTKLEVLSgeNAWgCDNCtRRKAT--KRLVIRKAPPVLTVHLKRFAQDMRgRLSKLTGHVAFDELLNLSPFL 251
Cdd:pfam13423 177 TFSSILKSSLERETTT--KAW-CEKC-KRYQPleSRRTVRNLPPVLSLNAALTNEEWR-QLWKTPGWLPPEIGLTLSDDL 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 300141194 252 STSRDGGLYRLVGVV---EHSGTmkGGHYVAFVRGGS--AGDGKENFWY 295
Cdd:pfam13423 252 QGDNEIVKYELRGVVvhiGDSGT--SGHLVSFVKVADseLEDPTESQWY 298
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
1.81e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 58.48 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRYLKDYFL---NPVAAGASEGPLTSALRRFFLEIngdnleaFSGNAKKRHrdyttYNPK 77
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLlyeNYENIKDRKSELVKRLSELIRKI-------WNPRNFKGH-----VSPH 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 78 GLFGALCSKSS-RFSGYHQQDSHE----LLRCLLDGLQVEGKHKES-------------EEKNSANGKEDHTfvDHLFGG 139
Cdd:cd02669 189 ELLQAVSKVSKkKFSITEQSDPVEflswLLNTLHKDLGGSKKPNSSiihdcfqgkvqieTQKIKPHAEEEGS--KDKFFK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 140 QFASTVTccecghsssVLEPF----LDVSLPIPFITAKS--------LEGCLQAFT-KLEVLSGENawgcdnctrrkaTK 206
Cdd:cd02669 267 DSRVKKT---------SVSPFllltLDLPPPPLFKDGNEeniipqvpLKQLLKKYDgKTETELKDS------------LK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 207 RLVIRKAPPVLTVHLKRFaqdmrgrlSKLTGH-------VAF-DELLNLSPFL-STSRDGGL---YRLVGVVEHSGTMKG 274
Cdd:cd02669 326 RYLISRLPKYLIFHIKRF--------SKNNFFkeknptiVNFpIKNLDLSDYVhFDKPSLNLstkYNLVANIVHEGTPQE 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 300141194 275 -GHYVAFVRggsagDGKENFWYYISDSDVRRTTLDQVLRSEAYLLFY 320
Cdd:cd02669 398 dGTWRVQLR-----HKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
94-320 |
1.79e-08 |
|
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: 54.07 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 94 HQQDSHELLRCLLDGLQVE----------GKHKESEEKNSANGKEDHTFVDHLFGGQFASTVTCCECGHSSSVLepfldV 163
Cdd:cd02670 22 EQQDPEEFFNFITDKLLMPllepkvdiihGGKKDQDDDKLVNERLLQIPVPDDDDGGGITLEQCLEQYFNNSVF-----A 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 164 SLPIPFITakslegCLQAFTKLEvlsgenawgcdnctrRKATKRLviRKAPPVLTVHLKRFAQDMRGRLSK--LTGHVAF 241
Cdd:cd02670 97 KAPSCLII------CLKRYGKTE---------------GKAQKMF--KKILIPDEIDIPDFVADDPRACSKcqLECRVCY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 242 DELLNlspflstSRDGGLYRLV--GVVEHSGT-MKGGHYVAFVRGGSAG------DGKENFWYYISDSDVRRTTL----- 307
Cdd:cd02670 154 DDKDF-------SPTCGKFKLSlcSAVCHRGTsLETGHYVAFVRYGSYSltetdnEAYNAQWVFFDDMADRDGVSngfni 226
|
250
....*....|....
gi 300141194 308 -DQVLRSEAYLLFY 320
Cdd:cd02670 227 pAARLLEDPYMLFY 240
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-320 |
2.77e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 51.34 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 1 GLVNLGNTCFFNSVMQNLLAVRylkdyflnpvaagasegpltsALRRFFLEINGDNLEAFS---------GNAKKRHR-- 69
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIK---------------------PLRDLVLNFDESKAELASdypterrigGREVSRSElq 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 70 --DYTTYNPKGLF------GALCSKSSRFSGY---HQQDSHELLRCLLDGLQVEGKHKESEEKNSA--NGKEDHTFVDHL 136
Cdd:cd02666 62 rsNQFVYELRSLFndlihsNTRSVTPSKELAYlalRQQDVTECIDNVLFQLEVALEPISNAFAGPDteDDKEQSDLIKRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 137 FGGQFASTVTCCECGHSSSVLEPF-LDVSLPI----------PFITAKSLEGCL------QAFTKL-----------EVL 188
Cdd:cd02666 142 FSGKTKQQLVPESMGNQPSVRTKTeRFLSLLVdvgkkgreivVLLEPKDLYDALdryfdyDSLTKLpqrsqvqaqlaQPL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 189 SGENAWgCDNCTRRKATKRL--VIRKAPPVLTVHLKRFAQDMRGRLSKLTGHvaFDELLNLSpflstsrdgglYRLVGVV 266
Cdd:cd02666 222 QRELIS-MDRYELPSSIDDIdeLIREAIQSESSLVRQAQNELAELKHEIEKQ--FDDLKSYG-----------YRLHAVF 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 267 EHSGTMKGGHYVAFVRggsagDGKENFWYYISDSDVRR-TTLDQVLRSEA-----YLLFY 320
Cdd:cd02666 288 IHRGEASSGHYWVYIK-----DFEENVWRKYNDETVTVvPASEVFLFTLGntatpYFLVY 342
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
95-320 |
1.69e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 48.32 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 95 QQDSHELLRCLLDGLQVEGKHKESEekNSANGKEDHTFVDhLFGGQFaSTVTCCEcGHSSSVLEPFLDvsLPIPFITAKS 174
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEA--ISPGEKSKNPMVQ-LFYGTF-LTEGVLE-GKPFCNCETFGQ--YPLQVNGYGN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 175 LEGCLQAFT---KLEVLSGENAwgcdnctrRKATKRLVIRKAPPVLTVHLKRFAQDmRGRLSKLTGHVAFDELLNLSPfl 251
Cdd:cd02665 95 LHECLEAAMfegEVELLPSDHS--------VKSGQERWFTELPPVLTFELSRFEFN-QGRPEKIHDKLEFPQIIQQVP-- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300141194 252 stsrdgglYRLVGVVEHSGTMKGGHYVAFVRggsagDGKENFWYYISDSDVRRTTLDQVLR--------SEAYLLFY 320
Cdd:cd02665 164 --------YELHAVLVHEGQANAGHYWAYIY-----KQSRQEWEKYNDISVTESSWEEVERdsfgggrnPSAYCLMY 227
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-320 |
5.54e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 40.96 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 123 SANGKEDHTFVDHLFGGQFASTVTCCECghSSSVLEPFLDVSLPIPFITAKSL---EGCLQAFTKLEVlsGENAWGCDNC 199
Cdd:cd02672 66 STLIQNFTRFLLETISQDQLGTPFSCGT--SRNSVSLLYTLSLPLGSTKTSKEstfLQLLKRSLDLEK--VTKAWCDTCC 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300141194 200 TRRKATKRLVIRKAPP----VLTVHLKRFAQDMRGRLSKLT------GHVAFDELLNLSPFLSTSRDGG-LYRLVG-VVE 267
Cdd:cd02672 142 KYQPLEQTTSIRHLPDilllVLVINLSVTNGEFDDINVVLPsgkvmqNKVSPKAIDHDKLVKNRGQESIyKYELVGyVCE 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 300141194 268 HSGTMKGGHYVAFVRGGSAgDGKENFWYYISDSDVRRTTLDqvlrseAYLLFY 320
Cdd:cd02672 222 INDSSRGQHNVVFVIKVNE-ESTHGRWYLFNDFLVTPVSEL------AYILLY 267
|
|
| |
