|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
253-654 |
4.91e-70 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 230.79 E-value: 4.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 253 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTehlfpkatngktqlsgkptnssatelslrndraeaceregfcw 332
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSE------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 333 ngrasisrsleliqnKEPSSKHISLCRELHTLFRVMWSGKW-ALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKV 411
Cdd:pfam00443 38 ---------------DSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 412 QQELESEGTTRRILIpfsqrkltkqvlkvVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPERyhciekgfvPLNQ 491
Cdd:pfam00443 103 HEDLNGNHSTENESL--------------ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD---------SAEL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 492 TECLLTEMLAKFTETEALEGRI-YACDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSgRNHREKIGVH 570
Cdd:pfam00443 160 KTASLQICFLQFSKLEELDDEEkYYCDKCGCKQ-----------DAIKQLKISRLPPVLIIHLKRFSYN-RSTWEKLNTE 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 571 VVFDQVLTMEPYCCRDmLSSLDKETFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLNVCSVE-EVCKTQA 649
Cdd:pfam00443 228 VEFPLELDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSA 305
|
....*
gi 1859876153 650 YILFY 654
Cdd:pfam00443 306 YILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-655 |
6.43e-63 |
|
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: 212.23 E-value: 6.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLnldpSKTEHLFPKATNGKTQLSgkptnssatelslrndraeaCEREgfcwn 333
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL----SDRHSCTCLSCSPNSCLS--------------------CAMD----- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 334 grasisrslELIQNKepsskHISLCRELHtlfrvmwsgkwalvSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQ 413
Cdd:cd02660 53 ---------EIFQEF-----YYSGDRSPY--------------GPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 414 ELESEgttrrilipFSQRKLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPERYHCIEKGFVPLNQTE 493
Cdd:cd02660 105 HYGGD---------KNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSGT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 494 CLLTEMLAKFTETEALEGRIYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVF 573
Cdd:cd02660 176 PTLSDCLDRFTRPEKLGDFAYKCSGCGST-----------QEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQF 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 574 DQVLTMEPYC----CRDMLSSLDKETFAYDLSAVVMHHGKgFGSGHYTAYCYNtEGGFWVHCNDSKLNVCSVEEVCKTQA 649
Cdd:cd02660 245 PLELNMTPYTsssiGDTQDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQ-GDGQWFKFDDAMITRVSEEEVLKSQA 322
|
....*.
gi 1859876153 650 YILFYT 655
Cdd:cd02660 323 YLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
395-654 |
1.16e-57 |
|
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: 195.78 E-value: 1.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 395 YDQQDAQEFLCELLHKVQQELESEgttrrilipFSQRKLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLE 474
Cdd:cd02257 20 SEQQDAHEFLLFLLDKLHEELKKS---------SKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 475 FPERyhciekgfvplNQTECLLTEMLAKFTETEALEGriYACDQCNSKRrksnpkplvLSEARKQLMIYRLPQVLRLHLK 554
Cdd:cd02257 91 LPVK-----------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKKK---------KQEATKRLKIKKLPPVLIIHLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 555 RFRWSGRNHREKIGVHVVFDQVLTMEPYCCRD-MLSSLDKETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCND 633
Cdd:cd02257 149 RFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGeKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFND 228
|
250 260
....*....|....*....|....*.
gi 1859876153 634 SKLNVCSVEEV-----CKTQAYILFY 654
Cdd:cd02257 229 DKVTEVSEEEVlefgsLSSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
253-654 |
7.09e-52 |
|
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: 181.71 E-value: 7.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 253 TGLRNLGNTCYMNSILQVLSHlqkfrecflnldpskTEHLfpkatngktqlsgkptnsSATELSLRNDRAeaCEREGFCw 332
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTH---------------TPPL------------------ANYLLSREHSKD--CCNEGFC- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 333 ngrasISRSLEliqnkepssKHISlcrelhtlfRVMWSGKWALVSPF--AMLHSVWsliPAFRGYDQQDAQEFLCELLHK 410
Cdd:cd02661 46 -----MMCALE---------AHVE---------RALASSGPGSAPRIfsSNLKQIS---KHFRIGRQEDAHEFLRYLLDA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 411 VQqelesegttRRILIPFSQRKLTKQVLK---VVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEfperyhcIEKGfv 487
Cdd:cd02661 100 MQ---------KACLDRFKKLKAVDPSSQettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD-------IKGA-- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 488 plnQTeclLTEMLAKFTETEALEGR-IYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFrwsGRNHREK 566
Cdd:cd02661 162 ---DS---LEDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRF---SNFRGGK 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 567 IGVHVVFDQVLTMEPYccrdmLSSLDKETFAYDLSAVVMHHGKGFGSGHYTAYCyNTEGGFWVHCNDSKLNVCSVEEVCK 646
Cdd:cd02661 222 INKQISFPETLDLSPY-----MSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYV-KSSNGKWYNMDDSKVSPVSIETVLS 295
|
....*...
gi 1859876153 647 TQAYILFY 654
Cdd:cd02661 296 QKAYILFY 303
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-654 |
4.25e-45 |
|
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: 162.56 E-value: 4.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 254 GLRNLGNTCYMNSILQVLSHLQKFRECFlnldpsktehlfpkatngktqlSGKPTNssatelslrndraeaceregfcwn 333
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL----------------------SETPKE------------------------ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 334 grasisrsleliqnkepsskhislcrelhtlfrvmwsgkwalvspfaMLHSVWSLIPAFRGYDQQDAQEFLCELLHKvqq 413
Cdd:cd02667 35 -----------------------------------------------LFSQVCRKAPQFKGYQQQDSHELLRYLLDG--- 64
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 414 elesegttrriLIPFsqrkltkqvlkvVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEfpeRYHCIEKgfvplnqtE 493
Cdd:cd02667 65 -----------LRTF------------IDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLP---RSDEIKS--------E 110
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 494 CLLTEMLAKFTETEALEGR-IYACDQCnskrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVV 572
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNnKFACENC--------------TKAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVS 176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 573 FDQVLTMEPYCCRDMLSSLDKETFAYDLSAVVMHHGkGFGSGHYTAYCY------------------NTEG---GFWVHC 631
Cdd:cd02667 177 FPEILDLAPFCDPKCNSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaaDEAGpgsGQWYYI 255
|
410 420
....*....|....*....|...
gi 1859876153 632 NDSKLNVCSVEEVCKTQAYILFY 654
Cdd:cd02667 256 SDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
396-655 |
9.02e-45 |
|
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: 159.76 E-value: 9.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 396 DQQDAQEFLCELLhkvqQELESegttrrilipfsqrkltkqvlkVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEF 475
Cdd:cd02674 21 DQQDAQEFLLFLL----DGLHS----------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 476 PERYHciekgfvplNQTECLLTEMLAKFTETEALEGRIYA-CDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLK 554
Cdd:cd02674 75 PSGSG---------DAPKVTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 555 RFRWSGRNhREKIGVHVVFD-QVLTMEPYCcrdmLSSLDKETFAYDLSAVVMHHGKGFGsGHYTAYCYNTEGGFWVHCND 633
Cdd:cd02674 135 RFSFSRGS-TRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNHYGSLNG-GHYTAYCKNNETNDWYKFDD 208
|
250 260
....*....|....*....|..
gi 1859876153 634 SKLNVCSVEEVCKTQAYILFYT 655
Cdd:cd02674 209 SRVTKVSESSVVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-654 |
6.99e-38 |
|
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: 143.94 E-value: 6.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTEhlfpkatngktqlsgKPTNSSATELSLRndraeaceregFCWN 333
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDD---------------DDNKSVPLALQRL-----------FLFL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 334 GRASISRsleliQNKEPSSKHislcrelhtlfRVMWsgkWALVSPFamlhsvwslipafrgyDQQDAQEFLCELLHKVQQ 413
Cdd:cd02659 58 QLSESPV-----KTTELTDKT-----------RSFG---WDSLNTF----------------EQHDVQEFFRVLFDKLEE 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 414 ELEseGTTRRilipfsqrkltkqvlKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFperyhcieKGFVPlnqte 493
Cdd:cd02659 103 KLK--GTGQE---------------GLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAV--------KGKKN----- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 494 clLTEMLAKFTETEALEG-RIYACDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLKRFRWSG-RNHREKIGVHV 571
Cdd:cd02659 153 --LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFEFDFeTMMRIKINDRF 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 572 VFDQVLTMEPYCCRDMLS------SLDKETFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLNVCSVEEVC 645
Cdd:cd02659 220 EFPLELDMEPYTEKGLAKkegdseKKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAE 298
|
410 420 430
....*....|....*....|....*....|.
gi 1859876153 646 K----------------------TQAYILFY 654
Cdd:cd02659 299 EecfggeetqktydsgprafkrtTNAYMLFY 329
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-655 |
1.59e-37 |
|
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: 142.56 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDpsktehlFPKATNGKTQLSGKPTNSSatelslrndraeaceregfcwn 333
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECN-------STEDAELKNMPPDKPHEPQ---------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 334 grasisrsleliqnkepsskhiSLCRELHTLFRVMWSGKWALVSPFAmlhsvwsLIPAFR--GYDQQDAQEFLCELLHKV 411
Cdd:cd02668 52 ----------------------TIIDQLQLIFAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFSKLFLSLL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 412 QQELESEgttrrilipfsqrkLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEfperyhciekgfvpLNQ 491
Cdd:cd02668 103 EAKLSKS--------------KNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQ--------------LKG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 492 TECLlTEMLAKFTETEALEG-RIYACDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLKRF---RWSGrnHREKI 567
Cdd:cd02668 155 HKTL-EECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFvfdRKTG--AKKKL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 568 GVHVVFDQVLTMEPYCCRDmlsslDKETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDS----------KLN 637
Cdd:cd02668 221 NASISFPEILDMGEYLAES-----DEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEdveempgkplKLG 295
|
410 420
....*....|....*....|....*....
gi 1859876153 638 V-----------CSVEEVCKTQAYILFYT 655
Cdd:cd02668 296 NsedpakprkseIKKGTHSSRTAYMLVYK 324
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-655 |
1.37e-34 |
|
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: 133.59 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 361 LHTLFRVMWSGK--WALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEGTTRRILIPFSQRKLTKQVL 438
Cdd:cd02663 27 LKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 439 KVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPEryhciekgfvplnqtECLLTEMLAKFTETEALEGR-IYACD 517
Cdd:cd02663 107 TWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ---------------NTSITSCLRQFSATETLCGRnKFYCD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 518 QCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSGRNHR-EKIGVHVVFDqvLTMEPYCCRDMLSSLDKEtf 596
Cdd:cd02663 172 ECCSLQ-----------EAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFP--LELRLFNTTDDAENPDRL-- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859876153 597 aYDLSAVVMHHGKGFGSGHYTAYCYNTegGFWVHCND---SKLNVCSVEEV-----CKTQAYILFYT 655
Cdd:cd02663 237 -YELVAVVVHIGGGPNHGHYVSIVKSH--GGWLLFDDetvEKIDENAVEEFfgdspNQATAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-654 |
3.06e-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 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: 106.65 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSktehlfpkatngktqlsgkptnssatelslrndRAEACERegfcwn 333
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPA---------------------------------RRGANQS------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 334 grasisrsleliqnkepsskHISLCRELHTLFRVMwSGKWALVSPFAMLHSVWSLIPAF------RGYDQQDAQEFLCEL 407
Cdd:cd02657 42 --------------------SDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQFaekqnqGGYAQQDAEECWSQL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 408 LHKVQQELESEGTTRRilipfsqrkltkqvlkVVNTIFHGQLLSQVTCI-SCNYKSNTIEPFWDLSLefperyHCIEKGF 486
Cdd:cd02657 101 LSVLSQKLPGAGSKGS----------------FIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQC------HISITTE 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 487 VplnqtECLLTEMLAKFTETEALEGRIYACDQCNSKRRKsnpkplvlsearkqlmIYRLPQVLRLHLKRFRWSGR-NHRE 565
Cdd:cd02657 159 V-----NYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSR----------------ISRLPKYLTVQFVRFFWKRDiQKKA 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 566 KIGVHVVFDQVLTMEPYCCrdmlssldkETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLNVCSVEEVC 645
Cdd:cd02657 218 KILRKVKFPFELDLYELCT---------PSGYYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDIL 288
|
410
....*....|....*.
gi 1859876153 646 KTQ-------AYILFY 654
Cdd:cd02657 289 KLSgggdwhiAYILLY 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
226-654 |
4.81e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 106.52 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 226 PAALPTSRRVPAATLKLRRqpaMAPGVTGLRNLGNTCYMNSILQVLShlqkfrecflnldpsktehlfpkatngktqlsg 305
Cdd:cd02671 1 DQVVPAPQPSSATSCEKRE---NLLPFVGLNNLGNTCYLNSVLQVLY--------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 306 kptnssatelslrndraeaceregFCWNGRASISRSLELIQNKEpssKHISLCRELHTLFrvmwSGKWALVSPFAMLHSV 385
Cdd:cd02671 45 ------------------------FCPGFKHGLKHLVSLISSVE---QLQSSFLLNPEKY----NDELANQAPRRLLNAL 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 386 WSLIPAFRGYDQQDAQEFLCELLHKVQQELESegttrrilipfsqrkltkqvlkvvntIFHGQLLSQVTCISCNYKSNTI 465
Cdd:cd02671 94 REVNPMYEGYLQHDAQEVLQCILGNIQELVEK--------------------------DFQGQLVLRTRCLECETFTERR 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 466 EPFWDLSLEFPERYHCIEKGFVPLNQTECLLTEMLAKFTETEALEGRI-----YACDQCNSkrrksnpkplvLSEARKQL 540
Cdd:cd02671 148 EDFQDISVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIvgedkYFCENCHH-----------YTEAERSL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 541 MIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVFDQVLTMEPYCCRDMLSSLDKETfaYDLSAVVMHHGKGFGSGHYTAYC 620
Cdd:cd02671 217 LFDKLPEVITIHLKCFAANGSEFDCYGGLSKVNTPLLTPLKLSLEEWSTKPKNDV--YRLFAVVMHSGATISSGHYTAYV 294
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1859876153 621 YnteggfWVHCNDSK---------LNVCSVEEVCKTQAYILFY 654
Cdd:cd02671 295 R------WLLFDDSEvkvteekdfLEALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-654 |
5.07e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 106.25 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLdpsktEHLFPKATNGktqlsgkPTNSSATELS-LRNdraeacereGFCw 332
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDL-----ENKFPSDVVD-------PANDLNCQLIkLAD---------GLL- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 333 NGRASISRSLELIQNkePSSKHISlcrelhtlfrvmwsgkwalvsPFaMLHSvwsLI----PAFRGYDQQDAQEFLCELL 408
Cdd:cd02658 59 SGRYSKPASLKSEND--PYQVGIK---------------------PS-MFKA---LIgkghPEFSTMRQQDALEFLLHLI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 409 HKVQQELESEGTTRrilipfsqrkltkqvlkvVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPER----YHCIEK 484
Cdd:cd02658 112 DKLDRESFKNLGLN------------------PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDeateKEEGEL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 485 GFVPLNQTEClltemLAKFTETEALEgriYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFR----WSG 560
Cdd:cd02658 174 VYEPVPLEDC-----LKAYFAPETIE---DFCSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQllenWVP 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 561 RnhreKIGVHVVFDQVLTMEPyccrdmlssldketfaYDLSAVVMHHGKGFGSGHYTAYCY--NTEGGFWVHCNDSKLNV 638
Cdd:cd02658 235 K----KLDVPIDVPEELGPGK----------------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFNDEKVVA 294
|
410
....*....|....*.
gi 1859876153 639 CSVEEVCKTQAYILFY 654
Cdd:cd02658 295 SQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-654 |
2.92e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 104.11 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTehlfpkatnGKTQLSGKPTNSSATELSLRNDRAEAceregfcwn 333
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL---------GDSQSVMKKLQLLQAHLMHTQRRAEA--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 334 grasisrsleliqnkePSSKHISLCRElhtlfrvmwsgkwalvspfamlhsvwsliPAFRGYDQQDAQEFLCELLHKVQQ 413
Cdd:cd02664 63 ----------------PPDYFLEASRP-----------------------------PWFTPGSQQDCSEYLRYLLDRLHT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 414 elesegttrrilipfsqrkltkqvlkVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPeryhciekgfvplnqte 493
Cdd:cd02664 98 --------------------------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP----------------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 494 cLLTEMLAKFTETEALEG-RIYACDQCNSkrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWSGRNH-REKIGVHV 571
Cdd:cd02664 135 -SVQDLLNYFLSPEKLTGdNQYYCEKCAS-----------LQDAEKEMKVTGAPEYLILTLLRFSYDQKTHvREKIMDNV 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 572 VFDQVLTM----------EPYCCRDMLSSLDKE----TFAYDLSAVVMHHGKGFGSGHYtaYCY---------------- 621
Cdd:cd02664 203 SINEVLSLpvrvesksseSPLEKKEEESGDDGElvtrQVHYRLYAVVVHSGYSSESGHY--FTYardqtdadstgqecpe 280
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1859876153 622 ------NTEGGFWVHCNDSKLNVCSVEEV-------CKTQAYILFY 654
Cdd:cd02664 281 pkdaeeNDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
26-87 |
5.62e-24 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 95.41 E-value: 5.62e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1859876153 26 CLECATTESVWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDLYVFCYLCKDYVLNDN 87
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
386-654 |
1.62e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 93.97 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 386 WSLIPAFRGY-----DQQDAQEFLCELLHKVQQELESegttrriliPFsqrkltkqvlkvvntifHGQLLSQVTCISCNY 460
Cdd:cd02662 18 LASLPSLIEYleeflEQQDAHELFQVLLETLEQLLKF---------PF-----------------DGLLASRIVCLQCGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 461 KSN-TIEPFWDLSLEFPERyhciekgfvpLNQTECLLTEMLAKFTETEALEGriYACDQCnskrrksnpkplvlsearkQ 539
Cdd:cd02662 72 SSKvRYESFTMLSLPVPNQ----------SSGSGTTLEHCLDDFLSTEIIDD--YKCDRC-------------------Q 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 540 LMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVFDQVLTmepyccrdmlssldkeTFAYDLSAVVMHHGkGFGSGHYTAY 619
Cdd:cd02662 121 TVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERLP----------------KVLYRLRAVVVHYG-SHSSGHYVCY 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1859876153 620 --------------------CYNTEGGFWVHCNDSKLNVCSVEEVCKT-QAYILFY 654
Cdd:cd02662 184 rrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLEQkSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
251-658 |
3.56e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 98.80 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 251 GVTGLRNLGNTCYMNSILQVLSHLQKFRECFLnldpsktehlfpkatngktqlsgkptnssatelslrndraeaceregf 330
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL------------------------------------------------ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 331 cwngrasiSRSLELIQNKE-PSSKHISLCRELHTLFRVMWSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLH 409
Cdd:COG5560 296 --------SDEYEESINEEnPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLD 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 410 KVQQEL----ESEGTTRRILIPFSQRKL-----------TKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSL- 473
Cdd:COG5560 368 GLHEDLnriiKKPYTSKPDLSPGDDVVVkkkakecwwehLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLp 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 474 ---------------------------------------------------------------------------EFPER 478
Cdd:COG5560 448 lpvsmvwkhtivvfpesgrrqplkieldasstirglkklvdaeygklgcfeikvmciyyggnynmlepadkvllqDIPQT 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 479 YHCIEKG----------------------------FVPLN----------------------------------QTECLL 496
Cdd:COG5560 528 DFVYLYEtndngievpvvhlriekgykskrlfgdpFLQLNvlikasiydklvkefeellvlvemkktdvdlvseQVRLLR 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 497 TEM----------------------------------------------------------------------LAKFTET 506
Cdd:COG5560 608 EESspsswlkleteidtkreeqveeegqmnfndavvisceweekrylslfsydplwtireigaaertitlqdcLNEFSKP 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 507 EAL--EGRIYaCDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRwSGRNHREKIGVHVVF---DQVLTMep 581
Cdd:COG5560 688 EQLglSDSWY-CPGCKEFR-----------QASKQMELWRLPMILIIHLKRFS-SVRSFRDKIDDLVEYpidDLDLSG-- 752
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859876153 582 yccrdMLSSLDKETFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLNVCSVEEVCKTQAYILFYTQRT 658
Cdd:COG5560 753 -----VEYMVDDPRLIYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
254-656 |
1.28e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 89.48 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 254 GLRNLGNTCYMNSILQVLShlqkfrecfLNLdpsktehlfPKATNGKTQLSGkptnssatelSLRNdraeaceregfcwn 333
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA---------LYL---------PKLDELLDDLSK----------ELKV-------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 334 grasisrsleLIQNKEPSSKHISLCRELHtLFRVMWSGKwalvspfamLHSVWSLIPAfrgYDQQDAQEFLCELLHKVQQ 413
Cdd:COG5533 39 ----------LKNVIRKPEPDLNQEEALK-LFTALWSSK---------EHKVGWIPPM---GSQEDAHELLGKLLDELKL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 414 ELESEGTtRRILIPFSqrkltkqvlkvvntifhgqllsqvtciscNYKSNTIEPFWDLSLEFPERyhcieKGFVPLNQTE 493
Cdd:COG5533 96 DLVNSFT-IRIFKTTK-----------------------------DKKKTSTGDWFDIIIELPDQ-----TWVNNLKTLQ 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 494 CLLTEMLAKFTetealegriyacDQCNSKRrKSNPKPLVLSEARKQLMIYRLPQVLRLHLKRFRWSGRNHR------EKI 567
Cdd:COG5533 141 EFIDNMEELVD------------DETGVKA-KENEELEVQAKQEYEVSFVKLPKILTIQLKRFANLGGNQKidtevdEKF 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 568 GVHVVFDQvltmepyccrdmlSSLDKETFAYDLSAVVMHHGkGFGSGHYTAYCynTEGGFWVHCNDSKLNVCSVEEVCKT 647
Cdd:COG5533 208 ELPVKHDQ-------------ILNIVKETYYDLVGFVLHQG-SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINE 271
|
410
....*....|..
gi 1859876153 648 ---QAYILFYTQ 656
Cdd:COG5533 272 kakNAYLYFYER 283
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
251-644 |
2.26e-16 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 83.38 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 251 GVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNLdpsktehlfpkatngktqlsgkPTNSSatelslrndraeaceregf 330
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI----------------------PTDHP------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 331 cwNGRASISRSLEliqnkepsskhislcrelhTLFRVMWSGKwalvSPFAMLHSVWSLI-PAFRGYDQQDAQEFlcellh 409
Cdd:COG5077 231 --RGRDSVALALQ-------------------RLFYNLQTGE----EPVDTTELTRSFGwDSDDSFMQHDIQEF------ 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 410 kvqqelesegttRRILIPFSQRKLTKQVLK-VVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFperyhcieKGFVP 488
Cdd:COG5077 280 ------------NRVLQDNLEKSMRGTVVEnALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--------KGMKN 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 489 LNqteclltEMLAKFTETEALEG-RIYACDQCNskrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWS-GRNHREK 566
Cdd:COG5077 340 LQ-------ESFRRYIQVETLDGdNRYNAEKHG------------LQDAKKGVIFESLPPVLHLQLKRFEYDfERDMMVK 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1859876153 567 IGVHVVFDQVLTMEPYCCRDMLSSLDKEtFAYDLSAVVMHHGKgFGSGHYTAYCYNTEGGFWVHCNDSKLNVCSVEEV 644
Cdd:COG5077 401 INDRYEFPLEIDLLPFLDRDADKSENSD-AVYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
26-72 |
2.57e-15 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 70.47 E-value: 2.57e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1859876153 26 CLECATTESVWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDL 72
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQ 48
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
250-654 |
1.14e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 73.51 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 250 PGVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTEhlfpkaTNGKTQLsgkptnssatelslrndraeacereg 329
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENI------KDRKSEL-------------------------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 330 fcwngrasISRSLELIqnkepssKHISLCRelhtLFRvmwsgkwALVSPFAMLH--SVWSLIPaFRGYDQQDAQEFLCEL 407
Cdd:cd02669 165 --------VKRLSELI-------RKIWNPR----NFK-------GHVSPHELLQavSKVSKKK-FSITEQSDPVEFLSWL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 408 LHKVQQELESEGTTRRILIPFS-QRKLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIePFWDLSLEFPER---YHCIE 483
Cdd:cd02669 218 LNTLHKDLGGSKKPNSSIIHDCfQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLPPPplfKDGNE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 484 KGFVPlnQTecLLTEMLAKFTETEALEgriyacdqcnskrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRwsgRNH 563
Cdd:cd02669 297 ENIIP--QV--PLKQLLKKYDGKTETE----------------------LKDSLKRYLISRLPKYLIFHIKRFS---KNN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 564 --REKIGVHVVFDQVLTMEPYCCRDMLSSLDKETfAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLNVCSV 641
Cdd:cd02669 348 ffKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLST-KYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLP 426
|
410
....*....|...
gi 1859876153 642 EEVCKTQAYILFY 654
Cdd:cd02669 427 QLIFLSESYIQIW 439
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
253-644 |
1.28e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 69.44 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 253 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTEhlfpkatngktqlsgkPTNSSATElslrndraeacEREGfcw 332
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAE----------------LASDYPTE-----------RRIG--- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 333 nGRAsISRSLELIQNKepsskhisLCRELHTLFRVMWSGKWALVSPFAMLhsvwslipAFRGYDQQDAQeflcELLHKVQ 412
Cdd:cd02666 52 -GRE-VSRSELQRSNQ--------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVT----ECIDNVL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 413 QELESEGTTRRILIPFSQRKLTKQVLKVVNTIFHGQLLSQVT-CISCNYKSNTIEPFWDLSLEFPeryhCIEKGFVPLNQ 491
Cdd:cd02666 110 FQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVD----VGKKGREIVVL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 492 TE-CLLTEMLAKFTETEALE-GRIYACDQCN----------SKRRKSNPKPL-VLSEARKQLMIYRLPQVLRLhlkrfRW 558
Cdd:cd02666 186 LEpKDLYDALDRYFDYDSLTkLPQRSQVQAQlaqplqreliSMDRYELPSSIdDIDELIREAIQSESSLVRQA-----QN 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 559 SGRNHREKIgvHVVFDqvltmepyccrdmlsslDKETFAYDLSAVVMHHGKGfGSGHYTAYCYNTEGGFWVHCNDSKLNV 638
Cdd:cd02666 261 ELAELKHEI--EKQFD-----------------DLKSYGYRLHAVFIHRGEA-SSGHYWVYIKDFEENVWRKYNDETVTV 320
|
....*.
gi 1859876153 639 CSVEEV 644
Cdd:cd02666 321 VPASEV 326
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
382-654 |
1.52e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 67.94 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 382 LHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEGTtrriLIPFSQrkltkQVLKVVNTI--FHGQLLSQVTCISCN 459
Cdd:cd02673 18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRT----NVPPSN-----IEIKRLNPLeaFKYTIESSYVCIGCS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 460 YKSNTIEPFWDLSLEFPERYHCIEKgfvplnqtecLLTEMLAKFTETEAlegriyACDQCNSKRRKSNPKplvlsearkq 539
Cdd:cd02673 89 FEENVSDVGNFLDVSMIDNKLDIDE----------LLISNFKTWSPIEK------DCSSCKCESAISSER---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 540 lmIYRLPQVLRLHLKRFRWsgrnhREKIGVHVVfDQVLTMEPYCcrdmlSSLDKetfaYDLSAVVMHHGKGFGSGHYTAY 619
Cdd:cd02673 143 --IMTFPECLSINLKRYKL-----RIATSDYLK-KNEEIMKKYC-----GTDAK----YSLVAVICHLGESPYDGHYIAY 205
|
250 260 270
....*....|....*....|....*....|....*....
gi 1859876153 620 CYN-TEGGFWVHCNDSKLNVCSVEEVCK---TQAYILFY 654
Cdd:cd02673 206 TKElYNGSSWLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
545-654 |
6.47e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 41.77 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859876153 545 LPQVLRLHLKRFRWsGRNHREKIGVHVVFDQVLTMEPYccrdmlssldketfayDLSAVVMHHGKGfGSGHYTAYCYNTE 624
Cdd:cd02665 128 LPPVLTFELSRFEF-NQGRPEKIHDKLEFPQIIQQVPY----------------ELHAVLVHEGQA-NAGHYWAYIYKQS 189
|
90 100 110
....*....|....*....|....*....|....*...
gi 1859876153 625 GGFWVHCNDSKLNVCSVEEVCK--------TQAYILFY 654
Cdd:cd02665 190 RQEWEKYNDISVTESSWEEVERdsfgggrnPSAYCLMY 227
|
|
| |
