|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
298-704 |
1.15e-68 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 227.71 E-value: 1.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 298 TGLQNPCNTCYINSIIQCLFGTTLFRDLFLtkKYRLFLNTNKYPKEVQLSRSIYVLFKKMYLNG-GRAIIPNRFLKMCKK 376
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLL--RISPLSEDSRYNKDINLLCALRDLFKALQKNSkSSSVSPKMFKKSLGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 377 LRPDLNIpDDQQDTQEFLLIVLARIHEelsnenvvkyypdlvsydanalqvnpskyekWYERNVITDGLSPIDHIYRGQL 456
Cdd:pfam00443 79 LNPDFSG-YKQQDAQEFLLFLLDGLHE-------------------------------DLNGNHSTENESLITDLFRGQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 457 ENILKCQRCGNSSYSYSTFYVLSLAIPKLSLYSFTsksrkIKLEDCINLFTGDEELSGDNAWDCPNCRitdskskkeeit 536
Cdd:pfam00443 127 KSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKT-----ASLQICFLQFSKLEELDDEEKYYCDKCG------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 537 sqkkkstifgfhsrsrsksphhhhhhhhssddstknakkrnsKKLTTIKSLDFIVLPPILVIHLSRFYYDLT--KKNSTV 614
Cdd:pfam00443 190 ------------------------------------------CKQDAIKQLKISRLPPVLIIHLKRFSYNRStwEKLNTE 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 615 ITYPLILNI--------ILKNGKVIRYKLYGTVNHSGNLINGHYTSVVNKEKSHEiglnrqvWVTFDDDYIQQHRKDrnn 686
Cdd:pfam00443 228 VEFPLELDLsrylaeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNR-------WYKFDDEKVTEVDEE--- 297
|
410
....*....|....*...
gi 767168212 687 feagkTEMSSDEVYVLFY 704
Cdd:pfam00443 298 -----TAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
299-705 |
1.16e-42 |
|
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: 154.37 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGttlfrdlfltkkyrlflntnkypkevqlsrsiyvlfkkmylnggraiipnrflkmckklr 378
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 379 pdlnipdDQQDTQEFLLIVLARIHeelsnenvvkyypdlvsydanalqvnpskyekwyernvitdglSPIDHIYRGQLEN 458
Cdd:cd02674 21 -------DQQDAQEFLLFLLDGLH-------------------------------------------SIIVDLFQGQLKS 50
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 459 ILKCQRCGNSSYSYSTFYVLSLAIPKLSlysftSKSRKIKLEDCINLFTGDEELSGDNAWDCPNCRitdskskkeeitsq 538
Cdd:cd02674 51 RLTCLTCGKTSTTFEPFTYLSLPIPSGS-----GDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCK-------------- 111
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 539 kkkstifgfhsrsrsksphhhhhhhhssddstknaKKRNSKklttiKSLDFIVLPPILVIHLSRFYYDL--TKKNSTVIT 616
Cdd:cd02674 112 -----------------------------------KKRKAT-----KKLTISRLPKVLIIHLKRFSFSRgsTRKLTTPVT 151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 617 YPL---ILNIILKNG---KVIRYKLYGTVNHSGNLINGHYTSVVNKEksheiglNRQVWVTFDDDYIQqhrkdrnnfEAG 690
Cdd:cd02674 152 FPLndlDLTPYVDTRsftGPFKYDLYAVVNHYGSLNGGHYTAYCKNN-------ETNDWYKFDDSRVT---------KVS 215
|
410
....*....|....*
gi 767168212 691 KTEMSSDEVYVLFYE 705
Cdd:cd02674 216 ESSVVSSSAYILFYE 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
299-705 |
4.93e-39 |
|
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: 144.93 E-value: 4.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGttlfrdlfltkkyrlflntnkypkevqlsrsiyvlfkkmylnggraiipnrflkmckklr 378
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 379 pdlnipdDQQDTQEFLLIVLARIHEELSNENVvkyypdlvsydanalqvnpskyekwyERNVITDGLSPIDHIYRGQLEN 458
Cdd:cd02257 21 -------EQQDAHEFLLFLLDKLHEELKKSSK--------------------------RTSDSSSLKSLIHDLFGGKLES 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 459 ILKCQRCGNSSYSYSTFYVLSLAIPKLSLYsftsksrKIKLEDCINLFTGDEELSGDNAWDCPNCritdskskkeeitsq 538
Cdd:cd02257 68 TIVCLECGHESVSTEPELFLSLPLPVKGLP-------QVSLEDCLEKFFKEEILEGDNCYKCEKK--------------- 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 539 kkkstifgfhsrsrsksphhhhhhhhssddstknaKKRNSKKLTTIKSLdfivlPPILVIHLSRFYYDLT---KKNSTVI 615
Cdd:cd02257 126 -----------------------------------KKQEATKRLKIKKL-----PPVLIIHLKRFSFNEDgtkEKLNTKV 165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 616 TYPLILNI----------ILKNGKVIRYKLYGTVNHSGNLIN-GHYTSVVNKEksheiglNRQVWVTFDDDYIQQHRKDr 684
Cdd:cd02257 166 SFPLELDLspylsegekdSDSDNGSYKYELVAVVVHSGTSADsGHYVAYVKDP-------SDGKWYKFNDDKVTEVSEE- 237
|
410 420
....*....|....*....|.
gi 767168212 685 nnfEAGKTEMSSDEVYVLFYE 705
Cdd:cd02257 238 ---EVLEFGSLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
298-704 |
2.03e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 115.84 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 298 TGLQNPCNTCYINSIIQCLFGTTLFRDLFLTKKYRLFLNTnkypKEVQLSRSIYVLFKKMYLNGGRAIIPNRFLKMCKKL 377
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN----EGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 378 RPDLNIpDDQQDTQEFLLIVLARIHEELSNENVvkyypdlvsydaNALQVNPSKYEKwyernvitdglSPIDHIYRGQLE 457
Cdd:cd02661 78 SKHFRI-GRQEDAHEFLRYLLDAMQKACLDRFK------------KLKAVDPSSQET-----------TLVQQIFGGYLR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 458 NILKCQRCGNSSYSYSTFYVLSLAIPKlslysftSKSrkikLEDCINLFTGDEELSGDNAWDCPNCritdskskkeeits 537
Cdd:cd02661 134 SQVKCLNCKHVSNTYDPFLDLSLDIKG-------ADS----LEDALEQFTKPEQLDGENKYKCERC-------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 538 qKKKSTifgfhsrsrsksphhhhhhhhssddstknAKKRnskkLTTIKSldfivlPPILVIHLSRFYYDLTKKNSTVITY 617
Cdd:cd02661 189 -KKKVK-----------------------------ASKQ----LTIHRA------PNVLTIHLKRFSNFRGGKINKQISF 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 618 PLILNII----LKNGKVIRYKLYGTVNHSGNLIN-GHYTSVVnkeKSheiglNRQVWVTFDDDYIQQHRKDRnnfeagkt 692
Cdd:cd02661 229 PETLDLSpymsQPNDGPLKYKLYAVLVHSGFSPHsGHYYCYV---KS-----SNGKWYNMDDSKVSPVSIET-------- 292
|
410
....*....|..
gi 767168212 693 eMSSDEVYVLFY 704
Cdd:cd02661 293 -VLSQKAYILFY 303
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
299-705 |
2.60e-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: 115.18 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGTTLFRDLFLTKKYRLFlntnkypkeVQLSRsiyvlfKKMYLNGGraiipnrflkmckklr 378
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKELF---------SQVCR------KAPQFKGY---------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 379 pdlnipdDQQDTQEFLLIVLariheelsnenvvkyypdlvsydanalqvnpskyekwyernvitDGLSP-IDHIYRGQLE 457
Cdd:cd02667 50 -------QQQDSHELLRYLL--------------------------------------------DGLRTfIDSIFGGELT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 458 NILKCQRCGNSSYSYstFYVLSLAIPKLSLySFTSKSrkikLEDCINLFTGDEELSGDNAWDCPNCritdskskkeeits 537
Cdd:cd02667 79 STIMCESCGTVSLVY--EPFLDLSLPRSDE-IKSECS----IESCLKQFTEVEILEGNNKFACENC-------------- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 538 qkkkstifgfhsrsrsksphhhhhhhhssddsTKNAKKRNSKKLttiksldfivlPPILVIHLSRFYYDLT---KKNSTV 614
Cdd:cd02667 138 --------------------------------TKAKKQYLISKL-----------PPVLVIHLKRFQQPRSanlRKVSRH 174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 615 ITYPLILNI---------ILKNGKVIRYKLYGTVNHSGNLINGHYTSVV--------------NKEKSHEIGLNRQVWVT 671
Cdd:cd02667 175 VSFPEILDLapfcdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVkvrppqqrlsdltkSKPAADEAGPGSGQWYY 254
|
410 420 430
....*....|....*....|....*....|....
gi 767168212 672 FDDDYIQqhrkdrnnfEAGKTEMSSDEVYVLFYE 705
Cdd:cd02667 255 ISDSDVR---------EVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
299-704 |
8.99e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 111.70 E-value: 8.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGTTLFRDLFLTKKYRLFLNTNKYPKevQLSRSIYVLFKKMYLNGGRA-IIPNRFLKMCKKL 377
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNS--CLSCAMDEIFQEFYYSGDRSpYGPINLLYLSWKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 378 RPDLnIPDDQQDTQEFLLIVLARIHEElsnenvvkyypdlvsydaNALQVNPSKYEKwyERNVItdglspIDHIYRGQLE 457
Cdd:cd02660 80 SRNL-AGYSQQDAHEFFQFLLDQLHTH------------------YGGDKNEANDES--HCNCI------IHQTFSGSLQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 458 NILKCQRCGNSSYSYSTFYVLSLAIPKLSLYSFTSK----SRKIKLEDCINLFTGDEELsGDNAWDCPNCritdskskke 533
Cdd:cd02660 133 SSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGesgvSGTPTLSDCLDRFTRPEKL-GDFAYKCSGC---------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 534 eitsqkkkstifgfhsrsrsksphhhhhhhhssdDSTKNAKKRnskklTTIKSLdfivlPPILVIHLSRFYYDLTK---K 610
Cdd:cd02660 202 ----------------------------------GSTQEATKQ-----LSIKKL-----PPVLCFQLKRFEHSLNKtsrK 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 611 NSTVITYPLILNI-----------ILKNGKV--IRYKLYGTVNHSGNLINGHYTSVVNKEKSHeiglnrqvWVTFDDDYI 677
Cdd:cd02660 238 IDTYVQFPLELNMtpytsssigdtQDSNSLDpdYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQ--------WFKFDDAMI 309
|
410 420 430
....*....|....*....|....*....|..
gi 767168212 678 qqhrkdrnnfeagkTEMSSDEV-----YVLFY 704
Cdd:cd02660 310 --------------TRVSEEEVlksqaYLLFY 327
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
299-705 |
2.52e-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: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGTTLFRDLFLTKK-----YRLFLNTNKYPKEVQLSRSIYVLFKKMYLNGGRAIIPNRFLKm 373
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNstedaELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 374 ckKLRPDLNipdDQQDTQEFLLIVLARIHEELSNenvvkyypdlvsydanalQVNPskyekwyernvitDGLSPIDHIYR 453
Cdd:cd02668 80 --ALGLDTG---QQQDAQEFSKLFLSLLEAKLSK------------------SKNP-------------DLKNIVQDLFR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 454 GQLENILKCQRCGNSSYSYSTFYVLSLAIPKLSlysftsksrkiKLEDCINLFTGDEELSGDNAWDCPNCritdskskke 533
Cdd:cd02668 124 GEYSYVTQCSKCGRESSLPSKFYELELQLKGHK-----------TLEECIDEFLKEEQLTGDNQYFCESC---------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 534 eitsQKKkstifgfhsrsrsksphhhhhhhhssddstKNAKKRnsKKLTTiksldfivLPPILVIHLSRFYYDLT----K 609
Cdd:cd02668 183 ----NSK------------------------------TDATRR--IRLTT--------LPPTLNFQLLRFVFDRKtgakK 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 610 KNSTVITYPLILNI----ILKNGKVIRYKLYGTVNHSGNLIN-GHYTSVVNKEKSHEiglnrqvWVTFDDDYIQ-----Q 679
Cdd:cd02668 219 KLNASISFPEILDMgeylAESDEGSYVYELSGVLIHQGVSAYsGHYIAHIKDEQTGE-------WYKFNDEDVEempgkP 291
|
410 420 430
....*....|....*....|....*....|...
gi 767168212 680 HRKDRNNFEA-------GKTEMSSDEVYVLFYE 705
Cdd:cd02668 292 LKLGNSEDPAkprkseiKKGTHSSRTAYMLVYK 324
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
299-705 |
1.64e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 104.31 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGTTLF---RDLFLTkkyrlfLNTNKYPKEVqlsrsiyvlfkkmylnggraIIPNRFLKMCK 375
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLtclKDLFES------ISEQKKRTGV--------------------ISPKKFITRLK 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 376 KLRPDLNiPDDQQDTQEFLLIVLARIHEELSNENvvKYYPDLVSYDANalqVNPSKYEKWyernvitdglspIDHIYRGQ 455
Cdd:cd02663 55 RENELFD-NYMHQDAHEFLNFLLNEIAEILDAER--KAEKANRKLNNN---NNAEPQPTW------------VHEIFQGI 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 456 LENILKCQRCGNSSYSYSTFYVLSLAIPKLslYSFTSksrkikledCINLFTGDEELSGDNAWDCPNCRitdskSKKEei 535
Cdd:cd02663 117 LTNETRCLTCETVSSRDETFLDLSIDVEQN--TSITS---------CLRQFSATETLCGRNKFYCDECC-----SLQE-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 536 tsqkkkstifgfhsrsrsksphhhhhhhhssddstknAKKRnskklTTIKSLdfivlPPILVIHLSRFYYDLT----KKN 611
Cdd:cd02663 179 -------------------------------------AEKR-----MKIKKL-----PKILALHLKRFKYDEQlnryIKL 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 612 STVITYPLILNIILKNGKV----IRYKLYGTVNHSGNLIN-GHYTSVVnkeKSHEIglnrqvWVTFDDD--------YIQ 678
Cdd:cd02663 212 FYRVVFPLELRLFNTTDDAenpdRLYELVAVVVHIGGGPNhGHYVSIV---KSHGG------WLLFDDEtvekidenAVE 282
|
410 420
....*....|....*....|....*..
gi 767168212 679 QHRKDRNNfeagktemsSDEVYVLFYE 705
Cdd:cd02663 283 EFFGDSPN---------QATAYVLFYQ 300
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
299-708 |
4.48e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 98.10 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGTTLFR-DLFLTKKYRLFLNTNKYPKEVQLsrsiyvLFKKMYLNGGRAIIPNRFLKMcKKL 377
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRnAVYSIPPTEDDDDNKSVPLALQR------LFLFLQLSESPVKTTELTDKT-RSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 378 RPDLNIPDDQQDTQEFLLIVLARIHEELSNENVvkyyPDLvsydanalqvnpskyekwyernvitdglspIDHIYRGQLE 457
Cdd:cd02659 77 GWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQ----EGL------------------------------IKNLFGGKLV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 458 NILKCQRCGNSSYSYSTFYVLSLAIpklslysFTSKSrkikLEDCINLFTGDEELSGDNAWDCPNCritdskskkeeits 537
Cdd:cd02659 123 NYIICKECPHESEREEYFLDLQVAV-------KGKKN----LEESLDAYVQGETLEGDNKYFCEKC-------------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 538 qkkkstifgfhsrsrsksphhhhhhhhssddstknakkrnSKKLTTIKSLDFIVLPPILVIHLSRFYYDLTK----KNST 613
Cdd:cd02659 178 ----------------------------------------GKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETmmriKIND 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 614 VITYPLILNI---------------ILKNGKVIRYKLYGTVNHSGNLINGHYTSVVnKEKSHEiglnrqVWVTFDDDYIQ 678
Cdd:cd02659 218 RFEFPLELDMepytekglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYI-KDRDDG------KWYKFNDDVVT 290
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 767168212 679 QHRKDR---NNFEAGKTEMSSDEV----------YVLFYERMD 708
Cdd:cd02659 291 PFDPNDaeeECFGGEETQKTYDSGprafkrttnaYMLFYERKS 333
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
294-483 |
8.36e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 91.10 E-value: 8.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 294 ELSITGLQNPCNTCYINSIIQCLFGTTLFRDLFLTKKYRLFLNTNKyPKEV--QLSRSIYVLFKKMYLNGGRAIIPNRFL 371
Cdd:COG5560 262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEN-PLGMhgSVASAYADLIKQLYDGNLHAFTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 372 KMCKKLRPDLNiPDDQQDTQEFLLIVLARIHEELSNENVVKYY--PDLvsYDANALQVNPSKYEKWYE-----RNVITDg 444
Cdd:COG5560 341 KTIGSFNEEFS-GYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTskPDL--SPGDDVVVKKKAKECWWEhlkrnDSIITD- 416
|
170 180 190
....*....|....*....|....*....|....*....
gi 767168212 445 lspidhIYRGQLENILKCQRCGNSSYSYSTFYVLSLAIP 483
Cdd:COG5560 417 ------LFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLP 449
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
299-705 |
1.93e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 84.08 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGTTLFRDLFLTKKYRLFLNTNKYPKEVQLSrsiyvLFKKMYLNGGRAIIPNRFLKMCkklR 378
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLL-----QAHLMHTQRRAEAPPDYFLEAS---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 379 PDLNIPDDQQDTQEFLLIVLARIHeelsnenvvkyypdlvsydanalqvnpskyekwyernvitdglSPIDHIYRGQLEN 458
Cdd:cd02664 73 PPWFTPGSQQDCSEYLRYLLDRLH-------------------------------------------TLIEKMFGGKLST 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 459 ILKCQRCGNSSYSYSTFYVLSLAIPklslysftsksrkiKLEDCINLFTGDEELSGDNAWDCPNCRitdskskkeeitsq 538
Cdd:cd02664 110 TIRCLNCNSTSARTERFRDLDLSFP--------------SVQDLLNYFLSPEKLTGDNQYYCEKCA-------------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 539 kkkstifgfhsrsrsksphhhhhhhhssddSTKNAkkrnskklttIKSLDFIVLPPILVIHLSRFYYDLTKKNSTVI--- 615
Cdd:cd02664 162 ------------------------------SLQDA----------EKEMKVTGAPEYLILTLLRFSYDQKTHVREKImdn 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 616 -TYPLILNI-ILKNGKVIR----------------------YKLYGTVNHSG-NLINGHYTS-------------VVNKE 657
Cdd:cd02664 202 vSINEVLSLpVRVESKSSEsplekkeeesgddgelvtrqvhYRLYAVVVHSGySSESGHYFTyardqtdadstgqECPEP 281
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 767168212 658 KSHEIGLNRQVWVTFDDDYIQQhrKDRNNFEAGKTEMSSDEVYVLFYE 705
Cdd:cd02664 282 KDAEENDESKNWYLFNDSRVTF--SSFESVQNVTSRFPKDTPYILFYE 327
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
299-705 |
3.96e-15 |
|
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: 76.98 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGTTLFRDLFLtKKYRLFLNTNKYPK---EVQLSR-------------SIYVLFKKMYLNGg 362
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYD-DLENKFPSDVVDPAndlNCQLIKladgllsgryskpASLKSENDPYQVG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 363 raIIPNRFLKMCKKLRPDLNiPDDQQDTQEFLLIVLARIheelsnenvvkyypdlvsydanalqvnpskyekwyERNVIT 442
Cdd:cd02658 79 --IKPSMFKALIGKGHPEFS-TMRQQDALEFLLHLIDKL-----------------------------------DRESFK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 443 DGLSPIDHIYRGQLENILKCQRCGNSSYSYSTFYVLSLAIPKLSLYSFTSKSRK---IKLEDCINLFTGDEELSGDnawd 519
Cdd:cd02658 121 NLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGELVyepVPLEDCLKAYFAPETIEDF---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 520 CPNCritdskskkeeitsqkkkstifgfhsrsrsksphhhhhhhhssddstknakkrnSKKLTTIKSLDFIVLPPILVIH 599
Cdd:cd02658 197 CSTC------------------------------------------------------KEKTTATKTTGFKTFPDYLVIN 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 600 LSRFYYdltKKNSTV--ITYPLILNIILKNGKvirYKLYGTVNHSGNLIN-GHYTSVVNKEKSHEiglnrQVWVTFDDDY 676
Cdd:cd02658 223 MKRFQL---LENWVPkkLDVPIDVPEELGPGK---YELIAFISHKGTSVHsGHYVAHIKKEIDGE-----GKWVLFNDEK 291
|
410 420
....*....|....*....|....*....
gi 767168212 677 IQQhrkdrnnfeAGKTEMSSDEVYVLFYE 705
Cdd:cd02658 292 VVA---------SQDPPEMKKLGYIYFYQ 311
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
494-706 |
8.76e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 71.84 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 494 SRKIKLEDCINLFTGDEELSGDNAWDCPNCritdskskkeeitsqkkkstifgfhsrsrsksphhhhhhhhssddstkNA 573
Cdd:COG5560 672 ERTITLQDCLNEFSKPEQLGLSDSWYCPGC------------------------------------------------KE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 574 KKRNSKKlttiksLDFIVLPPILVIHLSRFYYDLT--KKNSTVITYP---LILNIIL--KNGKVIRYKLYGTVNHSGNLI 646
Cdd:COG5560 704 FRQASKQ------MELWRLPMILIIHLKRFSSVRSfrDKIDDLVEYPiddLDLSGVEymVDDPRLIYDLYAVDNHYGGLS 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 647 NGHYTSVVNKEKSheiglnrQVWVTFDDDYIQqhRKDRNNFEAGKTemssdevYVLFYER 706
Cdd:COG5560 778 GGHYTAYARNFAN-------NGWYLFDDSRIT--EVDPEDSVTSSA-------YVLFYRR 821
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
299-705 |
2.01e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 64.69 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGTtlfrdlfltKKYRLFLNtnkypkevqlsrsiyvlfkkmylnggraiipnRFLkmckklr 378
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASL---------PSLIEYLE--------------------------------EFL------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 379 pdlnipdDQQDTQEFLLIVLARIHEELSNenvvkyypdlvsydanalqvnpskyekwyernvitdglsPIDhiyrGQLEN 458
Cdd:cd02662 33 -------EQQDAHELFQVLLETLEQLLKF---------------------------------------PFD----GLLAS 62
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 459 ILKCQRCGNSSY-SYSTFYVLSLAIPKLSLYSFTSksrkikLEDCINLFTGDEELSGDNawdCPNCritdskskkeeits 537
Cdd:cd02662 63 RIVCLQCGESSKvRYESFTMLSLPVPNQSSGSGTT------LEHCLDDFLSTEIIDDYK---CDRC-------------- 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 538 qkkkstifgfhsrsrsksphhhhhhhhssddstknakkrnskklttikSLDFIVLPPILVIHLSRFYYDLT---KKNSTV 614
Cdd:cd02662 120 ------------------------------------------------QTVIVRLPQILCIHLSRSVFDGRgtsTKNSCK 151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 615 ITYPLILNIILkngkvirYKLYGTVNHSGNLINGHYTS------VVNKEKSHEIGLNRQV-------WVTFDDDYIQqhR 681
Cdd:cd02662 152 VSFPERLPKVL-------YRLRAVVVHYGSHSSGHYVCyrrkplFSKDKEPGSFVRMREGpsstshpWWRISDTTVK--E 222
|
410 420
....*....|....*....|....
gi 767168212 682 KDRNNFEAGKtemssdEVYVLFYE 705
Cdd:cd02662 223 VSESEVLEQK------SAYMLFYE 240
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
295-704 |
2.65e-10 |
|
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: 62.60 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 295 LSITGLQNPCNTCYINSIIQCLFgttlFRDLFLTKKYRLFlNTNKYPKEVQLSrsiYVLFKKMYLNGGRAIIPNRFLKMC 374
Cdd:cd02671 22 LPFVGLNNLGNTCYLNSVLQVLY----FCPGFKHGLKHLV-SLISSVEQLQSS---FLLNPEKYNDELANQAPRRLLNAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 375 KKLRPDLNiPDDQQDTQEFLLIVLARIHEelsnenvvkyypdLVSYDanalqvnpskyekwyernvitdglspidhiYRG 454
Cdd:cd02671 94 REVNPMYE-GYLQHDAQEVLQCILGNIQE-------------LVEKD------------------------------FQG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 455 QLENILKCQRCGNSSYSYSTFYVLSLAIP-----KLSLYSFTSKSRKIK---LEDCINLFTGDEELSGDNAWDCPNCrit 526
Cdd:cd02671 130 QLVLRTRCLECETFTERREDFQDISVPVQeselsKSEESSEISPDPKTEmktLKWAISQFASVERIVGEDKYFCENC--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 527 dskskkeeitsqkkkstifgfhsrsrsksphhhhhhhhssddstknakkrnSKKLTTIKSLDFIVLPPILVIHLSRF--- 603
Cdd:cd02671 207 ---------------------------------------------------HHYTEAERSLLFDKLPEVITIHLKCFaan 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 604 ------YYDLTKKNSTVITyPLILNIILKNGKVIR--YKLYGTVNHSGNLIN-GHYTSVVNkeksheiglnrqvWVTFDD 674
Cdd:cd02671 236 gsefdcYGGLSKVNTPLLT-PLKLSLEEWSTKPKNdvYRLFAVVMHSGATISsGHYTAYVR-------------WLLFDD 301
|
410 420 430
....*....|....*....|....*....|..
gi 767168212 675 DYIQQHrkDRNNFEA--GKTEMSSDEVYVLFY 704
Cdd:cd02671 302 SEVKVT--EEKDFLEalSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
299-705 |
2.89e-08 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 55.80 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 299 GLQNPCNTCYINSIIQCLFGTTLFRDLFLTkkyrlflNTNKYPKEVQLSRSIYVLFKKMYL---NGGRAIIPNRFLKMCK 375
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKN-------YNPARRGANQSSDNLTNALRDLFDtmdKKQEPVPPIEFLQLLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 376 KLRPDLNIPDD-----QQDTQE---FLLIVLARIHEELSNENvvkyypdlvsydanalqvnpskyekwyernvitdglSP 447
Cdd:cd02657 74 MAFPQFAEKQNqggyaQQDAEEcwsQLLSVLSQKLPGAGSKG------------------------------------SF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 448 IDHIYRGQLENILKCQRCGN-SSYSYSTFYVLSLAIpklslysftsksrKIKLEdCINLFTGDEelsgdnawdcpncrit 526
Cdd:cd02657 118 IDQLFGIELETKMKCTESPDeEEVSTESEYKLQCHI-------------SITTE-VNYLQDGLK---------------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 527 dsKSKKEEITsqkkkstifgfhsrsrsksphhhhhhhHSSDDSTKNAKkrnSKKLTTIKSLdfivlPPILVIHLSRFYY- 605
Cdd:cd02657 168 --KGLEEEIE---------------------------KHSPTLGRDAI---YTKTSRISRL-----PKYLTVQFVRFFWk 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 606 DLTKKNSTV---ITYPLILNI--ILKNGKVirYKLYGTVNHSG-NLINGHYTSVVNKEksheiglNRQVWVTFDDDYIQQ 679
Cdd:cd02657 211 RDIQKKAKIlrkVKFPFELDLyeLCTPSGY--YELVAVITHQGrSADSGHYVAWVRRK-------NDGKWIKFDDDKVSE 281
|
410 420
....*....|....*....|....*.
gi 767168212 680 HRKDRNNFEAGKTEmsSDEVYVLFYE 705
Cdd:cd02657 282 VTEEDILKLSGGGD--WHIAYILLYK 305
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
566-706 |
6.37e-08 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 54.81 E-value: 6.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 566 SDDSTKNAKKRNSKKLTTIKsldfivLPPILVIHLSRFYYDLTK---KNSTVITYPLILNI--ILKNGKVIRYKLYGTVN 640
Cdd:COG5533 159 KENEELEVQAKQEYEVSFVK------LPKILTIQLKRFANLGGNqkiDTEVDEKFELPVKHdqILNIVKETYYDLVGFVL 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767168212 641 HSGNLINGHYTSVVNKEKSheiglnrqvWVTFDDDYIQQhrkdrnNFEAGKTEMSSDEVYVLFYER 706
Cdd:COG5533 233 HQGSLEGGHYIAYVKKGGK---------WEKANDSDVTP------VSEEEAINEKAKNAYLYFYER 283
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
298-419 |
1.98e-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: 50.57 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 298 TGLQNPCNTCYINSIIQCLFGTTLFRDLFLTKKYRLFLNTNKYPKE----------VQLSRSIYV------LFKKMYLNG 361
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTErriggrevsrSELQRSNQFvyelrsLFNDLIHSN 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767168212 362 GRAIIPNRFLKmckklrpdlNIPDDQQDTQEFLLIVLARIHEELSNENVVKYYPDLVS 419
Cdd:cd02666 82 TRSVTPSKELA---------YLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTED 130
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
585-675 |
2.34e-04 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 44.48 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168212 585 KSLDFIVLPPILVIHLSRFYYDLTKKNSTVIT--YPLILNIIL----------KNGKVIRYKLYGTVNHSGNLINGHYTS 652
Cdd:COG5077 371 KGVIFESLPPVLHLQLKRFEYDFERDMMVKINdrYEFPLEIDLlpfldrdadkSENSDAVYVLYGVLVHSGDLHEGHYYA 450
|
90 100
....*....|....*....|...
gi 767168212 653 VVNKEKSHEiglnrqvWVTFDDD 675
Cdd:COG5077 451 LLKPEKDGR-------WYKFDDT 466
|
|
| |
