|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-924 |
1.64e-96 |
|
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: 308.27 E-value: 1.64e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQALFMASDFRHCVLRLT---ENNSQPLMTKLQWLFGFLEHSQRPAISPEN-FLSASWTPWFSPGT 517
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNlprLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 518 QQDCSEYLKYLLDRLHeeektgtricqklkqssspsppeeppapssTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLS 597
Cdd:cd02664 81 QQDCSEYLRYLLDRLH------------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 598 LAFPppercrrrrlgsvmrpteditarelppptsaqgpgrvgprrqrkhcitedtpptslyiegldskeaggqssqeeri 677
Cdd:cd02664 131 LSFP---------------------------------------------------------------------------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 678 ereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgertcgseg 757
Cdd:cd02664 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 758 srSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLLLRLPL 837
Cdd:cd02664 135 --SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 838 -----------------AGGRGQA------YDLCSVVVHSGVSSESGHYYCYAR-----EGAARPAASLGTADRPEPENQ 889
Cdd:cd02664 213 rveskssesplekkeeeSGDDGELvtrqvhYRLYAVVVHSGYSSESGHYFTYARdqtdaDSTGQECPEPKDAEENDESKN 292
|
490 500 510
....*....|....*....|....*....|....*
gi 2217283940 890 WYLFNDTRVSFSSFESVSNVTSFFPKDTAYVLFYR 924
Cdd:cd02664 293 WYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFYE 327
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-924 |
2.53e-30 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 123.14 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 439 GKIGLINLGNTCYVNSILQALFMASDFRHCVLRLTEN----NSQPLMTKLQWLFGFLEHSQRPAISPENFLSASWTPWFS 514
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTedddDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 515 --PGTQQDCSEYLKYLLDRLhEEEKTGTricqKLKQssspsppeeppapsstSVEKMFGGKIVTRICCLCCLNVSSREEA 592
Cdd:cd02659 81 lnTFEQHDVQEFFRVLFDKL-EEKLKGT----GQEG----------------LIKNLFGGKLVNYIICKECPHESEREEY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 593 FTDLSLAfpppercrrrrlgsvmrpteditarelppptsaqgpgrvgprrqrkhciteDTPPTSLYiEGLDSkeaggqss 672
Cdd:cd02659 140 FLDLQVA---------------------------------------------------VKGKKNLE-ESLDA-------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 673 qeeriereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgert 752
Cdd:cd02659 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 753 cgsegsrsvldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLL 832
Cdd:cd02659 160 ---------------YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLE 224
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 833 LRL------PLAGGRGQAYDLCSVVVHSGV--------SSESGHYYCYAregaarpaaslgtadRPEPENQWYLFNDTRv 898
Cdd:cd02659 225 LDMepytekGLAKKEGDSEKKDSESYIYELhgvlvhsgDAHGGHYYSYI---------------KDRDDGKWYKFNDDV- 288
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2217283940 899 sfssfesvsnVTSF-------------------------FPKDT-AYVLFYR 924
Cdd:cd02659 289 ----------VTPFdpndaeeecfggeetqktydsgpraFKRTTnAYMLFYE 330
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
441-923 |
4.39e-29 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 118.70 E-value: 4.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 441 IGLINLGNTCYVNSILQALFMASDFRHCVLRL-------TENNSQPLMTKLQWLF-GFLEHSQRPAISPENFLSA--SWT 510
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplsedsRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSlgKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 511 PWFSPGTQQDCSEYLKYLLDRLHEEEKTGTricqklkqssspsppeepPAPSSTSVEKMFGGKIVTRICCLCCLNVSSRE 590
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNH------------------STENESLITDLFRGQLKSRLKCLSCGEVSETF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 591 EAFTDLSLafpppercrrrrlgsvmrpteditarelppptsaqgpgrvgprrqrkhcitedtpptslyiegldskeaggq 670
Cdd:pfam00443 143 EPFSDLSL------------------------------------------------------------------------ 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 671 ssqeeriereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpDAAIPSGE 750
Cdd:pfam00443 151 ------------------------------------------------------------------------PIPGDSAE 158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 751 RTCGSEGSRSVLdlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTmrRRKILDDVSIP 830
Cdd:pfam00443 159 LKTASLQICFLQ-----FSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFP 231
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 831 LLLRLplaggrgqaYDLCSVVVHSGVSSES----------------GHYYCYAregaarpaaslgtadRPEPENQWYLFN 894
Cdd:pfam00443 232 LELDL---------SRYLAEELKPKTNNLQdyrlvavvvhsgslssGHYIAYI---------------KAYENNRWYKFD 287
|
490 500
....*....|....*....|....*....
gi 2217283940 895 DTRVSFSSFESVSNvtsffpKDTAYVLFY 923
Cdd:pfam00443 288 DEKVTEVDEETAVL------SSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
442-924 |
9.49e-28 |
|
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: 113.35 E-value: 9.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQALFMasdfrhcvlrltennsqplmtklqwlfgflehsqrpaispenflsaswtpwfspgTQQDC 521
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS-------------------------------------------------------EQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 522 SEYLKYLLDRLHEEEKTGTRICQKLKQSSspsppeeppapssTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSLafp 601
Cdd:cd02257 26 HEFLLFLLDKLHEELKKSSKRTSDSSSLK-------------SLIHDLFGGKLESTIVCLECGHESVSTEPELFLSL--- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 602 ppercrrrrlgsvmrpteditarELPPPtsaqgpgrvgprrqrkhciteDTPPTSLYiegldskeaggqssqeerieree 681
Cdd:cd02257 90 -----------------------PLPVK---------------------GLPQVSLE----------------------- 102
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 682 egkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgertcgsegsrsv 761
Cdd:cd02257 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 762 lDLVNYFLSPEKLTAENRYYCESCaSLQDAEKVVELSQGPCYLILTLLRFSFDlRTMRRRKILDDVSIPLLLRL------ 835
Cdd:cd02257 103 -DCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLspylse 179
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 836 ----PLAGGRGQAYDLCSVVVHSGVSSESGHYYCYAREGaarpaaslgtadrpePENQWYLFNDTRVSFSSFESVSNVTS 911
Cdd:cd02257 180 gekdSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDP---------------SDGKWYKFNDDKVTEVSEEEVLEFGS 244
|
490
....*....|...
gi 2217283940 912 FfpKDTAYVLFYR 924
Cdd:cd02257 245 L--SSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-895 |
3.15e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 104.81 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQALFMASDFRHCVLRL--------------TENNSQPLMTKLQWLFGFLEHSQRPAISPENFLSA 507
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECnstedaelknmppdKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 508 SWtpwFSPGTQQDCSEYLKYLLDRLheEEKTGTRICQKLKQSsspsppeeppapsstsVEKMFGGKIVTRICCLCCLNVS 587
Cdd:cd02668 81 LG---LDTGQQQDAQEFSKLFLSLL--EAKLSKSKNPDLKNI----------------VQDLFRGEYSYVTQCSKCGRES 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 588 SREEAFTDLSLafpppercrrrrlgsvmrpteditarelppptsaqgpgRVGPRRQRKHCITEdtpptslyiegldskea 667
Cdd:cd02668 140 SLPSKFYELEL--------------------------------------QLKGHKTLEECIDE----------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 668 ggqssqeeriereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaip 747
Cdd:cd02668 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 748 sgertcgsegsrsvldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDV 827
Cdd:cd02668 165 --------------------FLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASI 224
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217283940 828 SIPLLLRLP--LAGGRGQ--AYDLCSVVVHSGVSSESGHYYCYAREgaarpaaslgtadrpEPENQWYLFND 895
Cdd:cd02668 225 SFPEILDMGeyLAESDEGsyVYELSGVLIHQGVSAYSGHYIAHIKD---------------EQTGEWYKFND 281
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-923 |
2.47e-18 |
|
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: 86.98 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQALFMASdfrhcvlrltennsqpLMTKLQWLFGFLEHSQRP--AISPENFLSASWT--PWFSPGT 517
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEN----------------LLTCLKDLFESISEQKKRtgVISPKKFITRLKRenELFDNYM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 518 QQDCSEYLKYLLDRLHEE-EKTgtricQKLKQSSSPSPPEEPPAPSSTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDL 596
Cdd:cd02663 65 HQDAHEFLNFLLNEIAEIlDAE-----RKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 597 SLafpppercrrrrlgsvmrpteditarELPPPTSAQgpgrvgprrqrkHCItedtpptslyiegldskeaggqssqeer 676
Cdd:cd02663 140 SI--------------------------DVEQNTSIT------------SCL---------------------------- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 677 iereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgertcgse 756
Cdd:cd02663 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 757 gsRSvldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLLLRLP 836
Cdd:cd02663 154 --RQ-------FSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 837 LAGGRG----QAYDLCSVVVHSGVSSESGHYYCYAREGaarpaaslgtadrpepeNQWYLFNDtrvSFSSFESVSNVTSF 912
Cdd:cd02663 225 NTTDDAenpdRLYELVAVVVHIGGGPNHGHYVSIVKSH-----------------GGWLLFDD---ETVEKIDENAVEEF 284
|
490
....*....|....*
gi 2217283940 913 F----PKDTAYVLFY 923
Cdd:cd02663 285 FgdspNQATAYVLFY 299
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-923 |
1.93e-16 |
|
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: 81.17 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQAL--------FMASdFRH---------CVLRLTENNSQplmtklqwlfGFLEhSQRPAISPENF 504
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLthtpplanYLLS-REHskdccnegfCMMCALEAHVE----------RALA-SSGPGSAPRIF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 505 LSA--SWTPWFSPGTQQDCSEYLKYLLDRLHeeeKTGTRICQKLKQSSSPSPPEeppapssTSVEKMFGGKIVTRICCLC 582
Cdd:cd02661 71 SSNlkQISKHFRIGRQEDAHEFLRYLLDAMQ---KACLDRFKKLKAVDPSSQET-------TLVQQIFGGYLRSQVKCLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 583 CLNVSSREEAFTDLSLafpppercrrrrlgsvmrpteDItarelppptsaqgpgrvgprrqrkhcitedtpptslyiegl 662
Cdd:cd02661 141 CKHVSNTYDPFLDLSL---------------------DI----------------------------------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 663 dskeaggqssqeeriereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthp 742
Cdd:cd02661 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 743 daaipsgertcgsEGSRSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDlrtmRRRK 822
Cdd:cd02661 159 -------------KGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF----RGGK 221
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 823 ILDDVSIPLLLRL-PL---AGGRGQAYDLCSVVVHSGVSSESGHYYCYARegaarpaASLGtadrpepenQWYLFNDTRV 898
Cdd:cd02661 222 INKQISFPETLDLsPYmsqPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVK-------SSNG---------KWYNMDDSKV 285
|
490 500
....*....|....*....|....*
gi 2217283940 899 SFSSFESVSNvtsffpkDTAYVLFY 923
Cdd:cd02661 286 SPVSIETVLS-------QKAYILFY 303
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-924 |
6.87e-16 |
|
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: 78.10 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQALFmasdfrhcvlrltennsqplmtklqwlfgflehsqrpaispenflsaswtpwfspGTQQDC 521
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLS-------------------------------------------------------ADQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 522 SEYLKYLLDRLHeeektgtRIcqklkqssspsppeeppapsstsVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSLAfp 601
Cdd:cd02674 26 QEFLLFLLDGLH-------SI-----------------------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLP-- 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 602 ppercrrrrLGSVMRPTEDITArelppptsaqgpgrvgprrqrKHCITEdtpptslyiegldskeaggqssqeerieree 681
Cdd:cd02674 74 ---------IPSGSGDAPKVTL---------------------EDCLRL------------------------------- 92
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 682 egkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgertcgsegsrsv 761
Cdd:cd02674 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 762 ldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDlrTMRRRKILDDVSIPL--LLRLPLAG 839
Cdd:cd02674 93 ------FTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPLndLDLTPYVD 164
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 840 GRGQA----YDLCsVVVHSGVSSESGHYYCYARegaarpaaslgtadRPEPeNQWYLFNDTRvsfssfesvsnVTSFFP- 914
Cdd:cd02674 165 TRSFTgpfkYDLY-AVVNHYGSLNGGHYTAYCK--------------NNET-NDWYKFDDSR-----------VTKVSEs 217
|
490
....*....|...
gi 2217283940 915 ---KDTAYVLFYR 924
Cdd:cd02674 218 svvSSSAYILFYE 230
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
763-926 |
1.62e-14 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 78.39 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 763 DLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRtmRRRKILDDVSIPlLLRLPLAGGRG 842
Cdd:COG5560 679 DCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRS--FRDKIDDLVEYP-IDDLDLSGVEY 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 843 Q------AYDLcSVVVHSGVSSESGHYYCYAREGAarpaaslgtadrpepENQWYLFNDTRvsfssfesvsnVTSFFPKD 916
Cdd:COG5560 756 MvddprlIYDL-YAVDNHYGGLSGGHYTAYARNFA---------------NNGWYLFDDSR-----------ITEVDPED 808
|
170
....*....|....
gi 2217283940 917 T----AYVLFYRQR 926
Cdd:COG5560 809 SvtssAYVLFYRRK 822
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-598 |
1.16e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 73.18 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQAL--------FMASDFRHC-VLRLTENNSQPL-MTKLQWLFGFLEHSQrpAISPENFLSASWTP 511
Cdd:cd02660 2 GLINLGATCFMNVILQALlhnpllrnYFLSDRHSCtCLSCSPNSCLSCaMDEIFQEFYYSGDRS--PYGPINLLYLSWKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 512 WFSPGT--QQDCSEYLKYLLDRLHEEEKTGTRICQKLKQSSSPsppeeppapsstsVEKMFGGKIVTRICCLCCLNVSSR 589
Cdd:cd02660 80 SRNLAGysQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCI-------------IHQTFSGSLQSSVTCQRCGGVSTT 146
|
....*....
gi 2217283940 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 |
2.58e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 68.89 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQALF-----------MASDFRHCVLRLTEN-NSQplMTKLqwLFGFLEH----------SQRP-- 497
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwryddLENKFPSDVVDPANDlNCQ--LIKL--ADGLLSGryskpaslksENDPyq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 498 -AISPENF--LSASWTPWFSPGTQQDCSEYLKYLLDRLHEEEKTgtricqklkqssspsppeeppaPSSTSVEKMFGGKI 574
Cdd:cd02658 77 vGIKPSMFkaLIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK----------------------NLGLNPNDLFKFMI 134
|
170 180
....*....|....*....|....
gi 2217283940 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 |
5.29e-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: 67.41 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQALFmASDFRHCVLRLTennsqplmtklqwlfgflehsqrpaisPENFLS--ASWTPWFSPGTQQ 519
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS-QTPALRELLSET---------------------------PKELFSqvCRKAPQFKGYQQQ 52
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217283940 520 DCSEYLKYLLDRLheeektgtricqklkqssspsppeeppapsSTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSL 598
Cdd:cd02667 53 DSHELLRYLLDGL------------------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL 101
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
434-598 |
5.57e-12 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 70.28 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 434 AKSDTGKIGLINLGNTCYVNSILQALFMASDFRHCVLRLTENNSQP---LMTKLQWLFGFLEHSQRPAISPENFLSASWT 510
Cdd:COG5077 187 SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGrdsVALALQRLFYNLQTGEEPVDTTELTRSFGWD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 511 PwFSPGTQQDCSEYLKYLLDRLhEEEKTGTRicqklkqssspsppeeppapsstsVEKMFGGKIVTRICCLC-CLNV--- 586
Cdd:COG5077 267 S-DDSFMQHDIQEFNRVLQDNL-EKSMRGTV------------------------VENALNGIFVGKMKSYIkCVNVnye 320
|
170
....*....|..
gi 2217283940 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 |
1.51e-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: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 441 IGLINLGNTCYVNSILQALFMASDFRHCVLRLTENNSQplMTKLQWLFGFLE---HSQRPAISPENFLSA--SWTPWFSP 515
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISS--VEQLQSSFLLNPekyNDELANQAPRRLLNAlrEVNPMYEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 516 GTQQDCSEYLKYLLDRLHEeektgtricqklkqssspsppeeppapsstSVEKMFGGKIVTRICCLCCLNVSSREEAFTD 595
Cdd:cd02671 103 YLQHDAQEVLQCILGNIQE------------------------------LVEKDFQGQLVLRTRCLECETFTERREDFQD 152
|
...
gi 2217283940 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 |
1.11e-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 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: 54.64 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQALFMASDFRHCVLRLTEN------NSQPLMTKLQWLFGFLEHSQRPaISPENFLSASWT--PWF 513
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPArrganqSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLLRMafPQF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217283940 514 SPGT------QQDCSEYLKYLLdrlheeektgTRICQKLKqssspsppeePPAPSSTSVEKMFGGKIVTRICCL 581
Cdd:cd02657 80 AEKQnqggyaQQDAEECWSQLL----------SVLSQKLP----------GAGSKGSFIDQLFGIELETKMKCT 133
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-599 |
2.00e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 46.98 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQALfmASdfrhcvlrltennsqplmtkLQWLFGFLehsqrpaispENFLSaswtpwfspgtQQDC 521
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL--AS--------------------LPSLIEYL----------EEFLE-----------QQDA 37
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217283940 522 SEYLKYLLDRLHeeektgtricQKLKQSsspsppeeppapsstsvekmFGGKIVTRICCLCCLNVSS-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 2217283940 441 IGLINLGNTCYVNSILQALFMASDFRHCVLRLTENN-------------------------SQPLMTKLQWLFGFLEHSQ 495
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKaelasdypterriggrevsrselqrSNQFVYELRSLFNDLIHSN 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2217283940 496 RPAISPENFLSaswtpwFSPGTQQDCSEYLKYLLDRLHEEEKTG 539
Cdd:cd02666 82 TRSVTPSKELA------YLALRQQDVTECIDNVLFQLEVALEPI 119
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
442-532 |
3.51e-05 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 46.72 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 442 GLINLGNTCYVNSILQALFMASD----------FRHCVLRLTENNSQPLMTKLQWLFGFlehsqrPAISPENFLSASWTP 511
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldellddlsKELKVLKNVIRKPEPDLNQEEALKLF------TALWSSKEHKVGWIP 74
|
90 100
....*....|....*....|.
gi 2217283940 512 wfSPGTQQDCSEYLKYLLDRL 532
Cdd:COG5533 75 --PMGSQEDAHELLGKLLDEL 93
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
760-896 |
1.71e-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: 41.20 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 760 SVLDLVNYFLSPEKLtaENrYYCESCASLqdaekvveLSQGPCYLILTLLRFSFDLR-TMRRRKIldDVSIPLLLRLPLa 838
Cdd:cd02662 97 TLEHCLDDFLSTEII--DD-YKCDRCQTV--------IVRLPQILCIHLSRSVFDGRgTSTKNSC--KVSFPERLPKVL- 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217283940 839 ggrgqaYDLCSVvVHSGVSSESGHYYCYAR-----EGAARPAASLGTADRPEPENQWYLFNDT 896
Cdd:cd02662 163 ------YRLRAV-VVHYGSHSSGHYVCYRRkplfsKDKEPGSFVRMREGPSSTSHPWWRISDT 218
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-533 |
3.21e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 41.15 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283940 439 GKIGLINLGNTCYVNSILQALFMASDFR-HCVL----RLTENNSQPLMTKLQWLFGFLEHSQ--RPAISPENFLSA---- 507
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRnFFLLyenyENIKDRKSELVKRLSELIRKIWNPRnfKGHVSPHELLQAvskv 197
|
90 100
....*....|....*....|....*.
gi 2217283940 508 SWTPwFSPGTQQDCSEYLKYLLDRLH 533
Cdd:cd02669 198 SKKK-FSITEQSDPVEFLSWLLNTLH 222
|
|
| COG1365 |
COG1365 |
Predicted ATPase, PP-loop superfamily [General function prediction only]; |
55-97 |
9.61e-03 |
|
Predicted ATPase, PP-loop superfamily [General function prediction only];
Pssm-ID: 440976 Cd Length: 256 Bit Score: 38.88 E-value: 9.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217283940 55 ELPRRVGCQLLHVAGRHHPDVfaEFFSARRVLRLLQGGAGPPG 97
Cdd:COG1365 207 ELSMKYGCPLLREAHKRHPSL--RKFSIQRVLREVRAGVLEPG 247
|
|
| |
