|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-922 |
2.68e-97 |
|
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: 310.19 E-value: 2.68e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQALFMASDFRHCVLRLT---ENNSQPLMTKLQWLFGFLEHSQRPAISPEN-FLSASWTPWFSPGT 517
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNlprLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 518 QQDCSEYLKYLLDRLHeeektgtricqklkqssspslpeeppapssTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLS 597
Cdd:cd02664 81 QQDCSEYLRYLLDRLH------------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 598 LAFPppercrrrrlgsvmrptgditaqellptasaqgpgrvgprrqrkhcitgdtpptsldiegldskeaggqssqeekv 677
Cdd:cd02664 131 LSFP---------------------------------------------------------------------------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 678 erdeegkeegtekeeageeeeestrgeeereeeeeveekveketekeaeqekeedslgagshldatipsgeqmcgsegsr 757
Cdd:cd02664 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 758 SVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPRYLILTLLRFSFDLRTMRRRKILDDISIPLLLRLPL-- 835
Cdd:cd02664 135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVrv 214
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 836 ---------------AGGRGQA------YDLCSVVVHSGVSSESGHYYCYAR-----EGAARPAPSLGTADRPEPENQWY 889
Cdd:cd02664 215 eskssesplekkeeeSGDDGELvtrqvhYRLYAVVVHSGYSSESGHYFTYARdqtdaDSTGQECPEPKDAEENDESKNWY 294
|
490 500 510
....*....|....*....|....*....|...
gi 1622865576 890 LFNDTRVSFSSFESVSNVTSFFPKDTAYVLFYR 922
Cdd:cd02664 295 LFNDSRVTFSSFESVQNVTSRFPKDTPYILFYE 327
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-922 |
2.50e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 128.91 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 439 GKIGLINLGNTCYVNSILQALFMASDFRHCVLRLTEN----NSQPLMTKLQWLFGFLEHSQRPAISPENFLSASWTPWFS 514
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTedddDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 515 --PGTQQDCSEYLKYLLDRLheEEKtgtricqklkqssSPSLPEEPpapsstSVEKMFGGKIVTRICCLCCLNVSSREEA 592
Cdd:cd02659 81 lnTFEQHDVQEFFRVLFDKL--EEK-------------LKGTGQEG------LIKNLFGGKLVNYIICKECPHESEREEY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 593 FTDLSLAfpppercrrrrlgsVMrptgditaqellptasaqgpgrvgprrqrkhcitgdtpptsldiegldskeaGGQSS 672
Cdd:cd02659 140 FLDLQVA--------------VK----------------------------------------------------GKKNL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 673 QEekverdeegkeegtekeeageeeeestrgeeereeeeeveekveketekeaeqekeedSLGAgshldatipsgeqmcg 752
Cdd:cd02659 154 EE----------------------------------------------------------SLDA---------------- 159
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 753 segsrsvldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPRYLILTLLRFSFDLRTMRRRKILDDISIPLLLR 832
Cdd:cd02659 160 -------------YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 833 L------PLAGGRGQAYDLCSVVVHSGV--------SSESGHYYCYAregaarpapslgtadRPEPENQWYLFNDTRvsf 898
Cdd:cd02659 227 MepytekGLAKKEGDSEKKDSESYIYELhgvlvhsgDAHGGHYYSYI---------------KDRDDGKWYKFNDDV--- 288
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1622865576 899 ssfesvsnVTSF-------------------------FPKDT-AYVLFYR 922
Cdd:cd02659 289 --------VTPFdpndaeeecfggeetqktydsgpraFKRTTnAYMLFYE 330
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
441-921 |
1.32e-30 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 123.32 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 441 IGLINLGNTCYVNSILQALFMASDFRHCVLRL-------TENNSQPLMTKLQWLF-GFLEHSQRPAISPENFLSA--SWT 510
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplsedsRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSlgKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 511 PWFSPGTQQDCSEYLKYLLDRLHEEektgtricqklkqsSSPSLPEEPPAPsstsVEKMFGGKIVTRICCLCCLNVSSRE 590
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHED--------------LNGNHSTENESL----ITDLFRGQLKSRLKCLSCGEVSETF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 591 EAFTDLslafpppercrrrrlgsvmrptgditaqellptasaqgpgrvgprrqrkhcitgdtpptSLDIEGlDSKEAGGQ 670
Cdd:pfam00443 143 EPFSDL-----------------------------------------------------------SLPIPG-DSAELKTA 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 671 SSQEEKVErdeegkeegtekeeageeeeestrgeeereeeeeveekveketekeaeqekeedslgagshldatipsgeqm 750
Cdd:pfam00443 163 SLQICFLQ------------------------------------------------------------------------ 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 751 cgsegsrsvldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPRYLILTLLRFSFDLRTmrRRKILDDISIPLL 830
Cdd:pfam00443 171 ---------------FSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLE 233
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 831 LRLplaggrgqaYDLCSVVVHSGVSSES----------------GHYYCYAregaarpapslgtadRPEPENQWYLFNDT 894
Cdd:pfam00443 234 LDL---------SRYLAEELKPKTNNLQdyrlvavvvhsgslssGHYIAYI---------------KAYENNRWYKFDDE 289
|
490 500
....*....|....*....|....*..
gi 1622865576 895 RVSFSSFESVSNvtsffpKDTAYVLFY 921
Cdd:pfam00443 290 KVTEVDEETAVL------SSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
442-922 |
8.74e-30 |
|
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: 119.12 E-value: 8.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQALFMasdfrhcvlrltennsqplmtklqwlfgflehsqrpaispenflsaswtpwfspgTQQDC 521
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS-------------------------------------------------------EQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 522 SEYLKYLLDRLHEEEKTGTRICQKLKQSSSPslpeeppapsstsVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSLafp 601
Cdd:cd02257 26 HEFLLFLLDKLHEELKKSSKRTSDSSSLKSL-------------IHDLFGGKLESTIVCLECGHESVSTEPELFLSL--- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 602 ppercrrrrlgsvmrptgditaqellptasaqgpgrvgprrqrkhcitgdtpptSLDIEGLDSKeaggqssqeekverde 681
Cdd:cd02257 90 ------------------------------------------------------PLPVKGLPQV---------------- 99
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 682 egkeegtekeeageeeeestrgeeereeeeeveekveketekeaeqekeedslgagshldatipsgeqmcgsegsrSVLD 761
Cdd:cd02257 100 ----------------------------------------------------------------------------SLED 103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 762 LVNYFLSPEKLTAENRYYCESCaSLQDAEKVVELSQGPRYLILTLLRFSFDlRTMRRRKILDDISIPLLLRL-------- 833
Cdd:cd02257 104 CLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLspylsege 181
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 834 --PLAGGRGQAYDLCSVVVHSGVSSESGHYYCYAREGaarpapslgtadrpePENQWYLFNDTRVSFSSFESVSNVTSFf 911
Cdd:cd02257 182 kdSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDP---------------SDGKWYKFNDDKVTEVSEEEVLEFGSL- 245
|
490
....*....|.
gi 1622865576 912 pKDTAYVLFYR 922
Cdd:cd02257 246 -SSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-893 |
4.24e-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: 107.51 E-value: 4.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQALFMASDFRHCVLRL--------------TENNSQPLMTKLQWLFGFLEHSQRPAISPENFLSA 507
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECnstedaelknmppdKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 508 SWtpwFSPGTQQDCSEYLKYLLDRLHEeektgtricqKLKQSSSPSLpeeppapsSTSVEKMFGGKIVTRICCLCCLNVS 587
Cdd:cd02668 81 LG---LDTGQQQDAQEFSKLFLSLLEA----------KLSKSKNPDL--------KNIVQDLFRGEYSYVTQCSKCGRES 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 588 SREEAFTDLSLafpppercrrrrlgsvmrptgditaqellptasaqgpgRVGPRRQRKHCITGdtpptsldiegldskea 667
Cdd:cd02668 140 SLPSKFYELEL--------------------------------------QLKGHKTLEECIDE----------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 668 ggqssqeekverdeegkeegtekeeageeeeestrgeeereeeeeveekveketekeaeqekeedslgagshldatipsg 747
Cdd:cd02668 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 748 eqmcgsegsrsvldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPRYLILTLLRFSFDLRTMRRRKILDDISI 827
Cdd:cd02668 165 ------------------FLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISF 226
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 828 PLLLRLP--LAGGRGQ--AYDLCSVVVHSGVSSESGHYYCYAREgaarpaPSLGTadrpepenqWYLFND 893
Cdd:cd02668 227 PEILDMGeyLAESDEGsyVYELSGVLIHQGVSAYSGHYIAHIKD------EQTGE---------WYKFND 281
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-921 |
6.22e-21 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 94.68 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQALFMASdfrhcvlrltennsqpLMTKLQWLFGFLEHSQRP--AISPENFLSASWT--PWFSPGT 517
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEN----------------LLTCLKDLFESISEQKKRtgVISPKKFITRLKRenELFDNYM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 518 QQDCSEYLKYLLDRLHEE-EKTgtricQKLKQSSSPSLPEEPPAPSSTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDL 596
Cdd:cd02663 65 HQDAHEFLNFLLNEIAEIlDAE-----RKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 597 SLafpppercrrrrlgsvmrptgditaqellptasaqgpgrvgprrqrkhcitgdtpptslDIEgldskeaggQSSqeek 676
Cdd:cd02663 140 SI-----------------------------------------------------------DVE---------QNT---- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 677 verdeegkeegtekeeageeeeestrgeeereeeeeveekveketekeaeqekeedslgagshldatipsgeqmcgsegs 756
Cdd:cd02663 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 757 rSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPRYLILTLLRFSFDLRTMRRRKILDDISIPLLLRLPLA 836
Cdd:cd02663 148 -SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLFNT 226
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 837 GGRG----QAYDLCSVVVHSGVSSESGHYYCYAREGaarpapslgtadrpepeNQWYLFNDtrvSFSSFESVSNVTSFF- 911
Cdd:cd02663 227 TDDAenpdRLYELVAVVVHIGGGPNHGHYVSIVKSH-----------------GGWLLFDD---ETVEKIDENAVEEFFg 286
|
490
....*....|...
gi 1622865576 912 ---PKDTAYVLFY 921
Cdd:cd02663 287 dspNQATAYVLFY 299
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-921 |
6.83e-19 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 88.49 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQAL--------FMASdFRH---------CVLRLTENNSQplmtklqwlfGFLEhSQRPAISPENF 504
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLthtpplanYLLS-REHskdccnegfCMMCALEAHVE----------RALA-SSGPGSAPRIF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 505 LSA--SWTPWFSPGTQQDCSEYLKYLLDRLHeeeKTGTRICQKLKQssspslpEEPPAPSSTSVEKMFGGKIVTRICCLC 582
Cdd:cd02661 71 SSNlkQISKHFRIGRQEDAHEFLRYLLDAMQ---KACLDRFKKLKA-------VDPSSQETTLVQQIFGGYLRSQVKCLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 583 CLNVSSREEAFTDLSLafpppercrrrrlgsvmrptgditaqellptasaqgpgrvgprrqrkhcitgdtpptslDIEGL 662
Cdd:cd02661 141 CKHVSNTYDPFLDLSL-----------------------------------------------------------DIKGA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 663 DSKEaggqssqeekverdeegkeegtekeeageeeeestrgeeereeeeeveekveketekeaeqekeeDSLgagshlda 742
Cdd:cd02661 162 DSLE-----------------------------------------------------------------DAL-------- 168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 743 tipsgEQmcgsegsrsvldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPRYLILTLLRFSFDlrtmRRRKIL 822
Cdd:cd02661 169 -----EQ----------------FTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF----RGGKIN 223
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 823 DDISIPLLLRL-PL---AGGRGQAYDLCSVVVHSGVSSESGHYYCYARegaarpapslgtadrpEPENQWYLFNDTRVSF 898
Cdd:cd02661 224 KQISFPETLDLsPYmsqPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVK----------------SSNGKWYNMDDSKVSP 287
|
490 500
....*....|....*....|...
gi 1622865576 899 SSFESVSNvtsffpkDTAYVLFY 921
Cdd:cd02661 288 VSIETVLS-------QKAYILFY 303
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-922 |
1.35e-17 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 83.11 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQALFmasdfrhcvlrltennsqplmtklqwlfgflehsqrpaispenflsaswtpwfspGTQQDC 521
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLS-------------------------------------------------------ADQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 522 SEYLKYLLDRLHeeektgtricqklkqssspSLpeeppapsstsVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSLAfp 601
Cdd:cd02674 26 QEFLLFLLDGLH-------------------SI-----------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLP-- 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 602 ppercrrrrLGSVMRPTGDITAQellptasaqgpgrvgprrqrkHCITGdtpptsldiegldskeaggqssqeekverde 681
Cdd:cd02674 74 ---------IPSGSGDAPKVTLE---------------------DCLRL------------------------------- 92
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 682 egkeegtekeeageeeeestrgeeereeeeeveekveketekeaeqekeedslgagshldatipsgeqmcgsegsrsvld 761
Cdd:cd02674 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 762 lvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPRYLILTLLRFSFDlrTMRRRKILDDISIPL--LLRLPLAGGR 839
Cdd:cd02674 93 ----FTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPLndLDLTPYVDTR 166
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 840 GQA----YDLCsVVVHSGVSSESGHYYCYARegaarpapslgtadRPEPeNQWYLFNDTRvsfssfesvsnVTSFFP--- 912
Cdd:cd02674 167 SFTgpfkYDLY-AVVNHYGSLNGGHYTAYCK--------------NNET-NDWYKFDDSR-----------VTKVSEssv 219
|
490
....*....|.
gi 1622865576 913 -KDTAYVLFYR 922
Cdd:cd02674 220 vSSSAYILFYE 230
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
336-924 |
2.41e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 81.08 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 336 TFQHSHEAFHLLLPHIPRMVASLVKEDSNSGTSCLEQLSELVHCMVfRFPGFPDLYEPVMEAIkdlhVPNEDrikQLLGQ 415
Cdd:COG5560 179 AFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLT-RLELFEDRSVLLLSKI----TRNPD---WLVDS 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 416 DAWTSQKSelagfyprlmAKSDTGKIGLINLGNTCYVNSILQALFMASDFRHCVL------RLTENNSQPLMTKLQWLFG 489
Cdd:COG5560 251 IVDDHNRS----------INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLsdeyeeSINEENPLGMHGSVASAYA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 490 FL---EHSQR-PAISPENFLS--ASWTPWFSPGTQQDCSEYLKYLLDRLHEEEktgTRICQKlKQSSSPSL-PEEPPAPS 562
Cdd:COG5560 321 DLikqLYDGNlHAFTPSGFKKtiGSFNEEFSGYDQQDSQEFIAFLLDGLHEDL---NRIIKK-PYTSKPDLsPGDDVVVK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 563 STSVEK--------------MFGGKIVTRICCLCCLNVSSREEAFTDLSLA-------------FPPPERCRRRRLGSVM 615
Cdd:COG5560 397 KKAKECwwehlkrndsiitdLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPlpvsmvwkhtivvFPESGRRQPLKIELDA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 616 RPTgdITAQELLPTASAQGPG----------RVGPRR---QRKHCITGDTPPT------SLDIEGLD------SKEAGGQ 670
Cdd:COG5560 477 SST--IRGLKKLVDAEYGKLGcfeikvmciyYGGNYNmlePADKVLLQDIPQTdfvylyETNDNGIEvpvvhlRIEKGYK 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 671 SSQ----------------------EEKVERDEEGKEEGTEKEEAGEEEEESTRGEEEREEEEEVEEKVEKETEKEAEQE 728
Cdd:COG5560 555 SKRlfgdpflqlnvlikasiydklvKEFEELLVLVEMKKTDVDLVSEQVRLLREESSPSSWLKLETEIDTKREEQVEEEG 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 729 KEED-------------SLGAGSHLDATIPSGEQMCGSEgSRSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVEL 795
Cdd:COG5560 635 QMNFndavvisceweekRYLSLFSYDPLWTIREIGAAER-TITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMEL 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 796 SQGPRYLILTLLRFSFDLRtmRRRKILDDISIPlLLRLPLAGGRGQ------AYDLcSVVVHSGVSSESGHYYCYAREGA 869
Cdd:COG5560 714 WRLPMILIIHLKRFSSVRS--FRDKIDDLVEYP-IDDLDLSGVEYMvddprlIYDL-YAVDNHYGGLSGGHYTAYARNFA 789
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622865576 870 arpapslgtadrpepENQWYLFNDTRvsfssfesvsnVTSFFPKDT----AYVLFYRQR 924
Cdd:COG5560 790 ---------------NNGWYLFDDSR-----------ITEVDPEDSvtssAYVLFYRRK 822
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-598 |
1.31e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 76.26 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQAL--------FMASDFRHC-VLRLTENNSQPL-MTKLQWLFGFLEHSQrpAISPENFLSASWTP 511
Cdd:cd02660 2 GLINLGATCFMNVILQALlhnpllrnYFLSDRHSCtCLSCSPNSCLSCaMDEIFQEFYYSGDRS--PYGPINLLYLSWKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 512 WFSPGT--QQDCSEYLKYLLDRLHEEEKTGTRICQKLKQSSSPslpeeppapsstsVEKMFGGKIVTRICCLCCLNVSSR 589
Cdd:cd02660 80 SRNLAGysQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCI-------------IHQTFSGSLQSSVTCQRCGGVSTT 146
|
....*....
gi 1622865576 590 EEAFTDLSL 598
Cdd:cd02660 147 VDPFLDLSL 155
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-598 |
5.19e-13 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 71.20 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQALF-----------MASDFRHCVLRLTEN-NSQplMTKLqwLFGFLEH----------SQRP-- 497
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwryddLENKFPSDVVDPANDlNCQ--LIKL--ADGLLSGryskpaslksENDPyq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 498 -AISPENF--LSASWTPWFSPGTQQDCSEYLKYLLDRLHEEEKTgtricqklKQSSSPSlpeeppapsstsveKMFGGKI 574
Cdd:cd02658 77 vGIKPSMFkaLIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK--------NLGLNPN--------------DLFKFMI 134
|
170 180
....*....|....*....|....
gi 1622865576 575 VTRICCLCCLNVSSREEAFTDLSL 598
Cdd:cd02658 135 EDRLECLSCKKVKYTSELSEILSL 158
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-598 |
3.39e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 68.18 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQALFmASDFRHCVLRLTennsqplmtklqwlfgflehsqrpaisPENFLS--ASWTPWFSPGTQQ 519
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS-QTPALRELLSET---------------------------PKELFSqvCRKAPQFKGYQQQ 52
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622865576 520 DCSEYLKYLLDRLheeektgtricqklkqssspslpeeppapsSTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSL 598
Cdd:cd02667 53 DSHELLRYLLDGL------------------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL 101
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
434-598 |
5.55e-12 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 70.28 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 434 AKSDTGKIGLINLGNTCYVNSILQALFMASDFRHCVLRLTENNSQP---LMTKLQWLFGFLEHSQRPAISPENFLSASWT 510
Cdd:COG5077 187 SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGrdsVALALQRLFYNLQTGEEPVDTTELTRSFGWD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 511 PwFSPGTQQDCSEYLKYLLDRLhEEEKTGTRicqklkqssspslpeeppapsstsVEKMFGGKIVTRICCLC-CLNV--- 586
Cdd:COG5077 267 S-DDSFMQHDIQEFNRVLQDNL-EKSMRGTV------------------------VENALNGIFVGKMKSYIkCVNVnye 320
|
170
....*....|..
gi 1622865576 587 SSREEAFTDLSL 598
Cdd:COG5077 321 SARVEDFWDIQL 332
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
441-598 |
1.71e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 66.84 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 441 IGLINLGNTCYVNSILQALFMASDFRHCVLRLTENNSQplMTKLQWLFGFLE---HSQRPAISPENFLSA--SWTPWFSP 515
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISS--VEQLQSSFLLNPekyNDELANQAPRRLLNAlrEVNPMYEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 516 GTQQDCSEYLKYLLDRLHEeektgtricqklkqssspslpeeppapsstSVEKMFGGKIVTRICCLCCLNVSSREEAFTD 595
Cdd:cd02671 103 YLQHDAQEVLQCILGNIQE------------------------------LVEKDFQGQLVLRTRCLECETFTERREDFQD 152
|
...
gi 1622865576 596 LSL 598
Cdd:cd02671 153 ISV 155
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-581 |
4.27e-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 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: 59.27 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQALFMASDFRHCVLRLTEN------NSQPLMTKLQWLFGFLEHSQRPaISPENFLSASWT--PWF 513
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPArrganqSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLLRMafPQF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622865576 514 SpgTQQDCSEYLKylldrlHEEEKTGTRICQKLKQSSspslpeEPPAPSSTSVEKMFGGKIVTRICCL 581
Cdd:cd02657 80 A--EKQNQGGYAQ------QDAEECWSQLLSVLSQKL------PGAGSKGSFIDQLFGIELETKMKCT 133
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-599 |
5.66e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 48.90 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQALfmASdfrhcvlrltennsqplmtkLQWLFGFLehsqrpaispENFLSaswtpwfspgtQQDC 521
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL--AS--------------------LPSLIEYL----------EEFLE-----------QQDA 37
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622865576 522 SEYLKYLLDRLHeeektgtricqklKQSSSPslpeeppapsstsvekmFGGKIVTRICCLCCLNVSS-REEAFTDLSLA 599
Cdd:cd02662 38 HELFQVLLETLE-------------QLLKFP-----------------FDGLLASRIVCLQCGESSKvRYESFTMLSLP 86
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
441-539 |
2.74e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 47.49 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 441 IGLINLGNTCYVNSILQALFMASDFRHCVLRLTENN-------------------------SQPLMTKLQWLFGFLEHSQ 495
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKaelasdypterriggrevsrselqrSNQFVYELRSLFNDLIHSN 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622865576 496 RPAISPENFLSaswtpwFSPGTQQDCSEYLKYLLDRLHEEEKTG 539
Cdd:cd02666 82 TRSVTPSKELA------YLALRQQDVTECIDNVLFQLEVALEPI 119
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
442-532 |
3.50e-05 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 46.72 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 442 GLINLGNTCYVNSILQALFMASD----------FRHCVLRLTENNSQPLMTKLQWLFGFlehsqrPAISPENFLSASWTP 511
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldellddlsKELKVLKNVIRKPEPDLNQEEALKLF------TALWSSKEHKVGWIP 74
|
90 100
....*....|....*....|.
gi 1622865576 512 wfSPGTQQDCSEYLKYLLDRL 532
Cdd:COG5533 75 --PMGSQEDAHELLGKLLDEL 93
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-582 |
4.10e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 47.31 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 439 GKIGLINLGNTCYVNSILQALFMASDFR-HCVL----RLTENNSQPLMTKLQWLFGFLEHSQ--RPAISPENFLSA---- 507
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRnFFLLyenyENIKDRKSELVKRLSELIRKIWNPRnfKGHVSPHELLQAvskv 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 508 SWTPwFSPGTQQDCSEYLKYLLDRLH--------EEEKTGTRICQ-KLKQSSSPSLPEEPPAPSSTSVEKMFGGKIVTRI 578
Cdd:cd02669 198 SKKK-FSITEQSDPVEFLSWLLNTLHkdlggskkPNSSIIHDCFQgKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS 276
|
....
gi 1622865576 579 CCLC 582
Cdd:cd02669 277 PFLL 280
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
758-894 |
3.51e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 40.43 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865576 758 SVLDLVNYFLSPEKLtaENrYYCESCAslqdaEKVVELsqgPRYLILTLLRFSFDLR-TMRRRKIldDISIPLLLRLPLa 836
Cdd:cd02662 97 TLEHCLDDFLSTEII--DD-YKCDRCQ-----TVIVRL---PQILCIHLSRSVFDGRgTSTKNSC--KVSFPERLPKVL- 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622865576 837 ggrgqaYDLCSVvVHSGVSSESGHYYCYAR-----EGAARPAPSLGTADRPEPENQWYLFNDT 894
Cdd:cd02662 163 ------YRLRAV-VVHYGSHSSGHYVCYRRkplfsKDKEPGSFVRMREGPSSTSHPWWRISDT 218
|
|
| COG1365 |
COG1365 |
Predicted ATPase, PP-loop superfamily [General function prediction only]; |
55-97 |
9.59e-03 |
|
Predicted ATPase, PP-loop superfamily [General function prediction only];
Pssm-ID: 440976 Cd Length: 256 Bit Score: 38.88 E-value: 9.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622865576 55 ELPRRVGCQLLHVAGRHHPDVfaEFFSARRVLRLLQGGAGPPG 97
Cdd:COG1365 207 ELSMKYGCPLLREAHKRHPSL--RKFSIQRVLREVRAGVLEPG 247
|
|
| |
