|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
227-570 |
1.24e-83 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 263.92 E-value: 1.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 227 IGLTNLGNTCYMNCVLQCLFACKDLTIPMLQGrgllQNINTKNPLGTGGKITSAFFSLLQSVLLNHGQRSISPRNFLEIV 306
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI----SPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 307 QSLNRDFSIDGQCDAQEFLNFFLDKLHEDLNSNasrspiapltedqlsareelplshfshiewnlHLRSNKSIVVNNFVG 386
Cdd:pfam00443 77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGN--------------------------------HSTENESLITDLFRG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 387 QLCSRTQCMTCGRTSTTFAPFTSLAIPIDDVSHV---VSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLP 463
Cdd:pfam00443 125 QLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAElktASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 464 EYLIIQIQRFKISVMGRKKIDTPLGLSLQIPSKMLVPPSFQSGIGYIPsNYNLFAFICHYGQLENGHYISDVLF--NNEW 541
Cdd:pfam00443 205 PVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-DYRLVAVVVHSGSLSSGHYIAYIKAyeNNRW 283
|
330 340
....*....|....*....|....*....
gi 347834304 542 CHIDDSIVRTVGGITDLREDfsSSYILFY 570
Cdd:pfam00443 284 YKFDDEKVTEVDEETAVLSS--SAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-571 |
4.84e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 249.13 E-value: 4.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFAckdltipmlqgrgllqnintknplgtggkitsaffsllqsvllnhgqrsisprnfleivq 307
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 308 slnrdfsidGQCDAQEFLNFFLDKLHedlnsnasrspiapltedqlsareelplshfshiewnlhlrsnkSIVVNNFVGQ 387
Cdd:cd02674 21 ---------DQQDAQEFLLFLLDGLH--------------------------------------------SIIVDLFQGQ 47
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 388 LCSRTQCMTCGRTSTTFAPFTSLAIPIDDVS---HVVSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLPE 464
Cdd:cd02674 48 LKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdaPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPK 127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 465 YLIIQIQRFKISVMGRKKIDTPLGLSLQIPskmLVPPSFQSGIGYIPSNYNLFAFICHYGQLENGHYISDVLFN--NEWC 542
Cdd:cd02674 128 VLIIHLKRFSFSRGSTRKLTTPVTFPLNDL---DLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNetNDWY 204
|
330 340
....*....|....*....|....*....
gi 347834304 543 HIDDSIVRTVGGITdlrEDFSSSYILFYK 571
Cdd:cd02674 205 KFDDSRVTKVSESS---VVSSSAYILFYE 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
228-571 |
9.70e-55 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 186.15 E-value: 9.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFACkdltipmlqgrgllqnintknplgtggkitsaffsllqsvllnhgqrsisprnfleivq 307
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 308 slnrdfsidgQCDAQEFLNFFLDKLHEDLNSNASRSPiapltedqlsareelplshfshiewnlHLRSNKSIVVNNFVGQ 387
Cdd:cd02257 22 ----------QQDAHEFLLFLLDKLHEELKKSSKRTS---------------------------DSSSLKSLIHDLFGGK 64
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 388 LCSRTQCMTCGRTSTTFAPFTSLAIPIDDVS-HVVSLQECLLKFSAPELLQGHDGWHCPVCKVQRsAKKVIMISKLPEYL 466
Cdd:cd02257 65 LESTIVCLECGHESVSTEPELFLSLPLPVKGlPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQE-ATKRLKIKKLPPVL 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 467 IIQIQRFKI-SVMGRKKIDTPLGLSLQI-PSKMLVPPSFQSGIGYIPSNYNLFAFICHYGQLEN-GHYISDVL--FNNEW 541
Cdd:cd02257 144 IIHLKRFSFnEDGTKEKLNTKVSFPLELdLSPYLSEGEKDSDSDNGSYKYELVAVVVHSGTSADsGHYVAYVKdpSDGKW 223
|
330 340 350
....*....|....*....|....*....|..
gi 347834304 542 CHIDDSIVRTVG--GITDLREDFSSSYILFYK 571
Cdd:cd02257 224 YKFNDDKVTEVSeeEVLEFGSLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
226-570 |
4.45e-41 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 150.89 E-value: 4.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 226 PIGLTNLGNTCYMNCVLQCLFACKDLTIPMLqGRGLLQNINTKNPlgtggKITSAFFSLLQSVLLNHGqRSISPRNFLEI 305
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLL-SREHSKDCCNEGF-----CMMCALEAHVERALASSG-PGSAPRIFSSN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 306 VQSLNRDFSIDGQCDAQEFLNFFLDKLHedlnsNASRSPIAPLTEDQLSAREelplshfshiewnlhlrsnKSIVVNNFV 385
Cdd:cd02661 74 LKQISKHFRIGRQEDAHEFLRYLLDAMQ-----KACLDRFKKLKAVDPSSQE-------------------TTLVQQIFG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 386 GQLCSRTQCMTCGRTSTTFAPFTSLAIPIDDVShvvSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLPEY 465
Cdd:cd02661 130 GYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD---SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 466 LIIQIQRFKISVMGR--KKIDTPLGLSLQipskmlvppSFQSGIGYIPSNYNLFAFICHYGQLEN-GHYISDV-LFNNEW 541
Cdd:cd02661 207 LTIHLKRFSNFRGGKinKQISFPETLDLS---------PYMSQPNDGPLKYKLYAVLVHSGFSPHsGHYYCYVkSSNGKW 277
|
330 340
....*....|....*....|....*....
gi 347834304 542 CHIDDSIVRTVGGITDLREDfssSYILFY 570
Cdd:cd02661 278 YNMDDSKVSPVSIETVLSQK---AYILFY 303
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
228-414 |
1.40e-37 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 148.88 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFACKDLTIPMLQgRGLLQNINTKNPLGTGGKITSAFFSLLQSVllnHGQR--SISPRNFLEI 305
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLS-DEYEESINEENPLGMHGSVASAYADLIKQL---YDGNlhAFTPSGFKKT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 306 VQSLNRDFSIDGQCDAQEFLNFFLDKLHEDLNsnasRSPIAPLTED-QLSAREELPLSHFSHIEWNLHLRSNKSIVVNNF 384
Cdd:COG5560 343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLN----RIIKKPYTSKpDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLF 418
|
170 180 190
....*....|....*....|....*....|
gi 347834304 385 VGQLCSRTQCMTCGRTSTTFAPFTSLAIPI 414
Cdd:COG5560 419 QGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-571 |
1.36e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 139.04 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLfackdLTIPMLQgRGLLQNINTKNPLGTGGK--ITSAFFSLLQSVLLNHGQRSISPRNFLEI 305
Cdd:cd02660 2 GLINLGATCFMNVILQAL-----LHNPLLR-NYFLSDRHSCTCLSCSPNscLSCAMDEIFQEFYYSGDRSPYGPINLLYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 306 VQSLNRDFSIDGQCDAQEFLNFFLDKLHEDlnsnasrspiapltedqlSAREELPLSHFSHIewnlhlrsnKSIVVNNFV 385
Cdd:cd02660 76 SWKHSRNLAGYSQQDAHEFFQFLLDQLHTH------------------YGGDKNEANDESHC---------NCIIHQTFS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 386 GQLCSRTQCMTCGRTSTTFAPFTSLAIPIDD------------VSHVVSLQECLLKFSAPELLqGHDGWHCPVCKVQRSA 453
Cdd:cd02660 129 GSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNkstpswalgesgVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 454 KKVIMISKLPEYLIIQIQRFKISVMG-RKKIDTPLglslQIPSKMLVPPSFQSGIGYIPSN--------YNLFAFICHYG 524
Cdd:cd02660 208 TKQLSIKKLPPVLCFQLKRFEHSLNKtSRKIDTYV----QFPLELNMTPYTSSSIGDTQDSnsldpdytYDLFAVVVHKG 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 347834304 525 QLENGHYISDV-LFNNEWCHIDDSIVRTVGGITDLREDfssSYILFYK 571
Cdd:cd02660 284 TLDTGHYTAYCrQGDGQWFKFDDAMITRVSEEEVLKSQ---AYLLFYH 328
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-571 |
2.47e-29 |
|
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: 118.19 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFackdlTIPMLQGR----GLLQNINTKNP----------LGTG---GKiTSAFFSLLQSVll 290
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLF-----SIPSFQWRyddlENKFPSDVVDPandlncqlikLADGllsGR-YSKPASLKSEN-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 291 NHGQRSISPRNFLEIVQSLNRDFSIDGQCDAQEFLNFFLDKLHEDLNSNASRSPIAPLtedqlsareelplshFSHIEwn 370
Cdd:cd02658 73 DPYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPNDLF---------------KFMIE-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 371 lhlrsnksivvnnfvgqlcSRTQCMTCGRTSTTFAP--FTSLAIPIDDVSHV---------VSLQECLLKFSAPELLQGH 439
Cdd:cd02658 136 -------------------DRLECLSCKKVKYTSELseILSLPVPKDEATEKeegelvyepVPLEDCLKAYFAPETIEDF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 440 dgwhCPVCKVQRSAKKVIMISKLPEYLIIQIQRFKISVMGR-KKIDTPlglsLQIPsKMLVPPsfqsgigyipsNYNLFA 518
Cdd:cd02658 197 ----CSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVpKKLDVP----IDVP-EELGPG-----------KYELIA 256
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347834304 519 FICHYG-QLENGHYISD-----------VLFNnewchiDDSIVRTVggitDLREDFSSSYILFYK 571
Cdd:cd02658 257 FISHKGtSVHSGHYVAHikkeidgegkwVLFN------DEKVVASQ----DPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-571 |
2.99e-29 |
|
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: 117.80 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFACKDLTIpmlqgrgllqnintknplgtggkitsafFSLLQSVLLNHGQRS--ISPRNFLEI 305
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLTC----------------------------LKDLFESISEQKKRTgvISPKKFITR 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 306 VQSLNRDFSIDGQCDAQEFLNFFLDKLHEDLNsnasrspiapltEDQLSAREELPLSHFSHIEWNlhlrsnKSIVVNNFV 385
Cdd:cd02663 53 LKRENELFDNYMHQDAHEFLNFLLNEIAEILD------------AERKAEKANRKLNNNNNAEPQ------PTWVHEIFQ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 386 GQLCSRTQCMTCGRTSTTFAPFTSLAIpidDVSHVVSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLPEY 465
Cdd:cd02663 115 GILTNETRCLTCETVSSRDETFLDLSI---DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 466 LIIQIQRFKIS--VMGRKKidtplgLSLQIP-SKMLVPPSFQSGIGYIPSNYNLFAFICHYGQLEN-GHYISDVLFNNEW 541
Cdd:cd02663 192 LALHLKRFKYDeqLNRYIK------LFYRVVfPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNhGHYVSIVKSHGGW 265
|
330 340 350
....*....|....*....|....*....|....*
gi 347834304 542 CHIDDSIVRTV--GGITDLREDFSSS---YILFYK 571
Cdd:cd02663 266 LLFDDETVEKIdeNAVEEFFGDSPNQataYVLFYQ 300
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-570 |
2.62e-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: 114.41 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFACKDLTipmlqgrgllqnintknplgtggkitsaffSLLQSvllnhgqrsiSPRNFLEIVQ 307
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALR------------------------------ELLSE----------TPKELFSQVC 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 308 SLNRDFSIDGQCDAQEFLNFFLDKLhedlnsnasRSPIapltedqlsareelplshfshiewnlhlrsnKSIvvnnFVGQ 387
Cdd:cd02667 41 RKAPQFKGYQQQDSHELLRYLLDGL---------RTFI-------------------------------DSI----FGGE 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 388 LCSRTQCMTCGRTSTTFAPFTSLAIPI-DDVSHVVSLQECLLKFSAPELLQGHDGWHCPVCKvqrSAKKVIMISKLPEYL 466
Cdd:cd02667 77 LTSTIMCESCGTVSLVYEPFLDLSLPRsDEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 467 IIQIQRFKisvmgrkkidtplGLSLQIPSKMLVPPSFQSGIGYIP--------------SNYNLFAFICHYGQLENGHYI 532
Cdd:cd02667 154 VIHLKRFQ-------------QPRSANLRKVSRHVSFPEILDLAPfcdpkcnssedkssVLYRLYGVVEHSGTMRSGHYV 220
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347834304 533 SDVLFNNE-----------------------WCHIDDSIVRTVGGITDLRedfSSSYILFY 570
Cdd:cd02667 221 AYVKVRPPqqrlsdltkskpaadeagpgsgqWYYISDSDVREVSLEEVLK---SEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
227-574 |
8.85e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 114.28 E-value: 8.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 227 IGLTNLGNTCYMNCVLQCLFackdlTIPMLQgRGLLQNINTKNPLGTGGKITsaffsLLQSVLLnHGQRSISPR---NFL 303
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLY-----MTPEFR-NAVYSIPPTEDDDDNKSVPL-----ALQRLFL-FLQLSESPVkttELT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 304 EIVQSLNRDfSIDG--QCDAQEFLNFFLDKLhedlnsnasrspiapltEDQLSAREElplshfshiewnlhlrsnKSIVV 381
Cdd:cd02659 71 DKTRSFGWD-SLNTfeQHDVQEFFRVLFDKL-----------------EEKLKGTGQ------------------EGLIK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 382 NNFVGQLCSRTQCMTCGRTSTTFAPFTSLAIpidDVSHVVSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISK 461
Cdd:cd02659 115 NLFGGKLVNYIICKECPHESEREEYFLDLQV---AVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 462 LPEYLIIQIQRFK--ISVMGRKKIDT----PLGLSLQ--IPSKMLVPPSFQSGIGYIPSNYNLFAFICHYGQLENGHY-- 531
Cdd:cd02659 192 LPPVLTLQLKRFEfdFETMMRIKINDrfefPLELDMEpyTEKGLAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYys 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 347834304 532 -ISDVLfNNEWCHIDDSIV-------------------RTVGGITDLREDFSSSYILFYKRSS 574
Cdd:cd02659 272 yIKDRD-DGKWYKFNDDVVtpfdpndaeeecfggeetqKTYDSGPRAFKRTTNAYMLFYERKS 333
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-571 |
2.37e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 112.97 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFACKDLTIPMLqgRGLLQNINTKNPLGTGgkitsafFSLLQSVLLNHGQRSISPRN-FLEiv 306
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVL--SLNLPRLGDSQSVMKK-------LQLLQAHLMHTQRRAEAPPDyFLE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 307 QSLNRDFSIDGQCDAQEFLNFFLDKLHedlnsnasrspiapltedqlsareelplshfshiewnlhlrsnkSIVVNNFVG 386
Cdd:cd02664 70 ASRPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------------TLIEKMFGG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 387 QLCSRTQCMTCGRTSTTFAPFTSLaipidDVShVVSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLPEYL 466
Cdd:cd02664 106 KLSTTIRCLNCNSTSARTERFRDL-----DLS-FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 467 IIQIQRFKIS--VMGRKKI----DTPLGLSLQIPSKM----------LVPPSFQSGIGYIPSNYNLFAFICHYG-QLENG 529
Cdd:cd02664 180 ILTLLRFSYDqkTHVREKImdnvSINEVLSLPVRVESkssesplekkEEESGDDGELVTRQVHYRLYAVVVHSGySSESG 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347834304 530 HYIS----------------------DVLFNNEWCHIDDSIV-----RTVGGITDLredFSS--SYILFYK 571
Cdd:cd02664 260 HYFTyardqtdadstgqecpepkdaeENDESKNWYLFNDSRVtfssfESVQNVTSR---FPKdtPYILFYE 327
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-571 |
4.31e-25 |
|
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: 106.35 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFACKDL-------TIPMLQGRGLLQNINTKNPLGTGGKITSAFfsllqsVLLNHGQRS-ISP 299
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFrkavyecNSTEDAELKNMPPDKPHEPQTIIDQLQLIF------AQLQFGNRSvVDP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 300 RNFLEIVQSLNRDfsidgQCDAQEFLNFFLdklhedlnsnasrspiapltedqlsareelplshfSHIEWNLHLRSN--- 376
Cdd:cd02668 75 SGFVKALGLDTGQ-----QQDAQEFSKLFL-----------------------------------SLLEAKLSKSKNpdl 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 377 KSIVVNNFVGQLCSRTQCMTCGRTSTTFAPFTSLAIPIDDVShvvSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKV 456
Cdd:cd02668 115 KNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK---TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 457 IMISKLPEYLIIQIQRF---KISvMGRKKIDTPLGLSLQI-PSKMLVPPSFQSgigyipSNYNLFAFICHYGQLEN-GHY 531
Cdd:cd02668 192 IRLTTLPPTLNFQLLRFvfdRKT-GAKKKLNASISFPEILdMGEYLAESDEGS------YVYELSGVLIHQGVSAYsGHY 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 532 ISDV--LFNNEWCHIDDSIVRTVGG------------------ITDLREDFSSSYILFYK 571
Cdd:cd02668 265 IAHIkdEQTGEWYKFNDEDVEEMPGkplklgnsedpakprkseIKKGTHSSRTAYMLVYK 324
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
228-572 |
6.77e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 99.11 E-value: 6.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFACKD-----LTIPMLQGRGLLQNINTKNPLGTGGKITSAFFSLLQsvllnhgqrsisprnf 302
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldelLDDLSKELKVLKNVIRKPEPDLNQEEALKLFTALWS---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 303 lEIVQSLNRDFSIDGQCDAQEFLNFFLDKLHEDL-NSNASRspIAPLTEDQLSareelplshfshiewnlHLRSNKSIVV 381
Cdd:COG5533 65 -SKEHKVGWIPPMGSQEDAHELLGKLLDELKLDLvNSFTIR--IFKTTKDKKK-----------------TSTGDWFDII 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 382 NNFVGQlcsrtqcmTCGRTSTTFAPFtslaipIDDVSHVVSlQECLLKFSApellqgHDGWHcpvckVQRSAKKVIMISK 461
Cdd:COG5533 125 IELPDQ--------TWVNNLKTLQEF------IDNMEELVD-DETGVKAKE------NEELE-----VQAKQEYEVSFVK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 462 LPEYLIIQIQRFKISVMGRK---KIDTPLGLSLQIPSKMLVPPSFQsgigyipsnYNLFAFICHYGQLENGHYISDVLFN 538
Cdd:COG5533 179 LPKILTIQLKRFANLGGNQKidtEVDEKFELPVKHDQILNIVKETY---------YDLVGFVLHQGSLEGGHYIAYVKKG 249
|
330 340 350
....*....|....*....|....*....|....
gi 347834304 539 NEWCHIDDSIVRTVGGITDLREDFSSSYILFYKR 572
Cdd:COG5533 250 GKWEKANDSDVTPVSEEEAINEKAKNAYLYFYER 283
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
209-571 |
4.59e-22 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 97.66 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 209 LANPKKVDSSLSYENYQP-IGLTNLGNTCYMNCVLQCLFACKdltipmlqgrGLLQNIntKNPLGTGGKITSaffslLQS 287
Cdd:cd02671 6 APQPSSATSCEKRENLLPfVGLNNLGNTCYLNSVLQVLYFCP----------GFKHGL--KHLVSLISSVEQ-----LQS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 288 V-LLNH-----GQRSISPRNFLEIVQSLNRDFSIDGQCDAQEFLNFFLDKLHEdlnsnasrspiapltedqlsareelpl 361
Cdd:cd02671 69 SfLLNPekyndELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE--------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 362 shfshiewnlhlrsnksIVVNNFVGQLCSRTQCMTCGRTSTTFAPFTSLAIPI----------------DDVSHVVSLQE 425
Cdd:cd02671 122 -----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVqeselskseesseispDPKTEMKTLKW 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 426 CLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLPEYLIIQIQRFKISVM------GRKKIDTPlglsLQIPSKMlv 499
Cdd:cd02671 185 AISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSefdcygGLSKVNTP----LLTPLKL-- 258
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 347834304 500 pPSFQSGIGYIPSNYNLFAFICHYG-QLENGHYISDVlfnnEWCHIDDSIVRTV------GGITDLREDFSSSYILFYK 571
Cdd:cd02671 259 -SLEEWSTKPKNDVYRLFAVVMHSGaTISSGHYTAYV----RWLLFDDSEVKVTeekdflEALSPNTSSTSTPYLLFYK 332
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
421-574 |
1.82e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 95.72 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 421 VSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLPEYLIIQIQRFKISVMGRKKIDTPLGLSL-QIPSKMLV 499
Cdd:COG5560 675 ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIdDLDLSGVE 754
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347834304 500 PPSFQSGIGyipsnYNLFAFICHYGQLENGHYISDV--LFNNEWCHIDDSIVRTVGGITDLRedfSSSYILFYKRSS 574
Cdd:COG5560 755 YMVDDPRLI-----YDLYAVDNHYGGLSGGHYTAYArnFANNGWYLFDDSRITEVDPEDSVT---SSAYVLFYRRKS 823
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-571 |
2.23e-19 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 88.93 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFAckdltIPMLQGRGLLQNINTKNPLGTGGKITSAFFSLLQSvlLNHGQRSISPRNFLEIVQ 307
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRS-----VPELRDALKNYNPARRGANQSSDNLTNALRDLFDT--MDKKQEPVPPIEFLQLLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 308 SLNRDFSIDG------QCDAQEFLNFFLDKLHEDLnsnasrspiapltedqlsareELPLSHFSHIEwnlhlrsnksivv 381
Cdd:cd02657 74 MAFPQFAEKQnqggyaQQDAEECWSQLLSVLSQKL---------------------PGAGSKGSFID------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 382 NNFVGQLCSRTQCM-TCGRTSTTFAPFTSLAIPIDDVSHVVSLQECLLKFSAPELLQGHDgwhcpvcKVQRSAK--KVIM 458
Cdd:cd02657 120 QLFGIELETKMKCTeSPDEEEVSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSP-------TLGRDAIytKTSR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 459 ISKLPEYLIIQIQRF--------KISVMgrKKIDTPLGLSlqipskmLVPPSFQSGIgyipsnYNLFAFICHYGQ-LENG 529
Cdd:cd02657 193 ISRLPKYLTVQFVRFfwkrdiqkKAKIL--RKVKFPFELD-------LYELCTPSGY------YELVAVITHQGRsADSG 257
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 347834304 530 HYISDVLF--NNEWCHIDDS---------IVRTVGGitdlrEDFSSSYILFYK 571
Cdd:cd02657 258 HYVAWVRRknDGKWIKFDDDkvsevteedILKLSGG-----GDWHIAYILLYK 305
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-570 |
6.84e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 71.63 E-value: 6.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 228 GLTNLGNTCYMNCVLQCLFACKDLTIpmlqgrgllqnintknplgtggkitsaffsllqsvllnhgqrsisprnFLEivq 307
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIE------------------------------------------------YLE--- 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 308 slnrdfSIDGQCDAQEFLNFFLDKLHedlnsNASRSPIAPLTEDQLSAReelplshfsHIEWNLHLRSNksivvnnfvgq 387
Cdd:cd02662 30 ------EFLEQQDAHELFQVLLETLE-----QLLKFPFDGLLASRIVCL---------QCGESSKVRYE----------- 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 388 lcsrtqCMTCgrtsttfapfTSLAIPIDDVSHVVSLQECLLKFSAPELLqghDGWHCPVCKvqrsakkvIMISKLPEYLI 467
Cdd:cd02662 79 ------SFTM----------LSLPVPNQSSGSGTTLEHCLDDFLSTEII---DDYKCDRCQ--------TVIVRLPQILC 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 468 IQIQRfkiSVMgrkkidTPLGLSLQIPSKMLVPPSFQSGIgyipsnYNLFAFICHYGQLENGHYIS-------------- 533
Cdd:cd02662 132 IHLSR---SVF------DGRGTSTKNSCKVSFPERLPKVL------YRLRAVVVHYGSHSSGHYVCyrrkplfskdkepg 196
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 347834304 534 --------DVLFNNEWCHIDDSIVRTVgGITDLREDfSSSYILFY 570
Cdd:cd02662 197 sfvrmregPSSTSHPWWRISDTTVKEV-SESEVLEQ-KSAYMLFY 239
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
227-578 |
1.21e-11 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 67.97 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 227 IGLTNLGNTCYMNCVLQCLFACKDLtipmlqgRGLLQNINTKNPlgtGGKITSAFfsLLQSVLLNHgQRSISPRNFLEIV 306
Cdd:COG5077 194 VGLRNQGATCYMNSLLQSLFFIAKF-------RKDVYGIPTDHP---RGRDSVAL--ALQRLFYNL-QTGEEPVDTTELT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 307 QSLNRDfSIDG--QCDAQEFLNFFLDKLHEdlnsNASRSPIapltEDQLSareelplshfshiewnlhlrsnksivvNNF 384
Cdd:COG5077 261 RSFGWD-SDDSfmQHDIQEFNRVLQDNLEK----SMRGTVV----ENALN---------------------------GIF 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 385 VGQLCSRTQCMTCGRTSTTFAPFTSLAIpidDVSHVVSLQECLLKFSAPELLQGHDGWHCPVCKVQrSAKKVIMISKLPE 464
Cdd:COG5077 305 VGKMKSYIKCVNVNYESARVEDFWDIQL---NVKGMKNLQESFRRYIQVETLDGDNRYNAEKHGLQ-DAKKGVIFESLPP 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 465 YLIIQIQRFKISV---MGRK---KIDTPLGLSLqipSKMLVPPSFQSGigYIPSNYNLFAFICHYGQLENGHYIS--DVL 536
Cdd:COG5077 381 VLHLQLKRFEYDFerdMMVKindRYEFPLEIDL---LPFLDRDADKSE--NSDAVYVLYGVLVHSGDLHEGHYYAllKPE 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347834304 537 FNNEWCHIDDSIVRTVGGITDLREDF-------------------SSSYILFYKRSSLLEE 578
Cdd:COG5077 456 KDGRWYKFDDTRVTRATEKEVLEENFggdhpykdkirdhsgikrfMSAYMLVYLRKSMLDD 516
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-571 |
6.92e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 64.65 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 213 KKVDSSLSYENYQP--IGLTNLGNTCYMNCVLQCLFACKDLtipmlqgRG-LLQNINTKNPLGTGGKITSAFFSLLQSvL 289
Cdd:cd02669 104 PKLSRDLDGKPYLPgfVGLNNIKNNDYANVIIQALSHVKPI-------RNfFLLYENYENIKDRKSELVKRLSELIRK-I 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 290 LNHG--QRSISPRNFLEIVQSL-NRDFSIDGQCDAQEFLNFFLDKLHEDLNSNasrspIAPLTedqlsareelplSHFSH 366
Cdd:cd02669 176 WNPRnfKGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGGS-----KKPNS------------SIIHD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 367 -IEWNLHLRSNKSIVVNNFVGQLCSRTQCMTCGRTSTTFAPFTSLAIPI----DDVSHVVSLQECLLKfsapELLQGHDG 441
Cdd:cd02669 239 cFQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVSPFLLLTLDLPPpplfKDGNEENIIPQVPLK----QLLKKYDG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 442 WHCPVCKVQRsakKVIMISKLPEYLIIQIQRF-KISVMGRKKIDTplglsLQIPSKML-----VPPSFQSGIgyIPSNYN 515
Cdd:cd02669 315 KTETELKDSL---KRYLISRLPKYLIFHIKRFsKNNFFKEKNPTI-----VNFPIKNLdlsdyVHFDKPSLN--LSTKYN 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347834304 516 LFAFICHYGQ-LENGHYISDVLFN--NEWCHIDDSIVrtvggiTDLREDF---SSSYILFYK 571
Cdd:cd02669 385 LVANIVHEGTpQEDGTWRVQLRHKstNKWFEIQDLNV------KEVLPQLiflSESYIQIWE 440
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
309-570 |
2.78e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 57.92 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 309 LNRDFSIDGQCDAQEFLNFFLDKLHEDLNSNASRSPIAPLTEDQLSAREELPLShfshIEwnlhlrsnksivvnnfvgql 388
Cdd:cd02673 24 INTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLEAFKYT----IE-------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 389 cSRTQCMTCGRTSTTFAPFTSLAIPIDDVSHVV--SLQECLLKFSAPELLqghdgwhCPVCKVQrSAKKVIMISKLPEYL 466
Cdd:cd02673 80 -SSYVCIGCSFEENVSDVGNFLDVSMIDNKLDIdeLLISNFKTWSPIEKD-------CSSCKCE-SAISSERIMTFPECL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 467 IIQIQRFKISvmgrkkidTPLGLSLQIPSKMLVPpsFQSGIGyipsNYNLFAFICHYGQL-ENGHYIS---DVLFNNEWC 542
Cdd:cd02673 151 SINLKRYKLR--------IATSDYLKKNEEIMKK--YCGTDA----KYSLVAVICHLGESpYDGHYIAytkELYNGSSWL 216
|
250 260
....*....|....*....|....*...
gi 347834304 543 HIDDSIVRTVGGITDLREDFSSSYILFY 570
Cdd:cd02673 217 YCSDDEIRPVSKNDVSTNARSSGYLIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
226-552 |
3.45e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 49.41 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 226 PIGLTNLGNTCYMNCVLQCLFACKDLtipmlqgRGLLQNINTKNPLGTGGKITS--------AFFSLLQSVLLNHGQRSI 297
Cdd:cd02666 1 PAGLDNIGNTCYLNSLLQYFFTIKPL-------RDLVLNFDESKAELASDYPTErriggrevSRSELQRSNQFVYELRSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 298 sprnFLEIVQSLNR---------DFSIDGQcDAQEFLNFFLDKLheDLNSNASRSPIAPLTEDQLSAREELPLSHFShie 368
Cdd:cd02666 74 ----FNDLIHSNTRsvtpskelaYLALRQQ-DVTECIDNVLFQL--EVALEPISNAFAGPDTEDDKEQSDLIKRLFS--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 369 wnlhLRSNKSIVVNNFVGQLCSRTQcMTcgRTSTTFAPFTSLAIPIDDVSHVVSLQECLL-------KFSAPELLQghdg 441
Cdd:cd02666 144 ----GKTKQQLVPESMGNQPSVRTK-TE--RFLSLLVDVGKKGREIVVLLEPKDLYDALDryfdydsLTKLPQRSQ---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347834304 442 whcpVCKVQRSAKKVIMISKLPEYLIIQIQRfkISVMGRKKIDTPLGLSLQIPSKMLVPPSFQSGI--GYIPSNYNLFAF 519
Cdd:cd02666 213 ----VQAQLAQPLQRELISMDRYELPSSIDD--IDELIREAIQSESSLVRQAQNELAELKHEIEKQfdDLKSYGYRLHAV 286
|
330 340 350
....*....|....*....|....*....|....*.
gi 347834304 520 ICHYGQLENGHY---ISDvLFNNEWCHIDDSIVRTV 552
Cdd:cd02666 287 FIHRGEASSGHYwvyIKD-FEENVWRKYNDETVTVV 321
|
|
| |
