|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
250-651 |
2.21e-70 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 231.56 E-value: 2.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 250 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSTSehlfpqatngkaqlsgrpasssaaelsvrsvraqgcepqglcw 329
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSE------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 330 ssgasisrsleliqnKEPSSKHISLCHELHTLFRVMWSGKW-ALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKV 408
Cdd:pfam00443 38 ---------------DSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 409 QQELESEGSTRRILIpfsqrkltkqvlkvVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPERyhciekgfvPLNQ 488
Cdd:pfam00443 103 HEDLNGNHSTENESL--------------ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD---------SAEL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 489 TECLLTEMLAKFTETEALEGRI-YACDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSgRNHREKIGVH 567
Cdd:pfam00443 160 KTASLQICFLQFSKLEELDDEEkYYCDKCGCKQ-----------DAIKQLKISRLPPVLIIHLKRFSYN-RSTWEKLNTE 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 568 VIFDQVLTMEPYCCRDmLSSLDKETFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVE-EVCKTQA 646
Cdd:pfam00443 228 VEFPLELDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSA 305
|
....*
gi 38259220 647 YILFY 651
Cdd:pfam00443 306 YILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-652 |
4.16e-62 |
|
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: 210.31 E-value: 4.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNldpstsehlfpqatngkaqlsgrpasssaaelsvrsvraQGCEPQGLCWS 330
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLS---------------------------------------DRHSCTCLSCS 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 331 SGASISRSLELIqnkepsskhislCHELHTlfrvmwSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQ 410
Cdd:cd02660 43 PNSCLSCAMDEI------------FQEFYY------SGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 411 ElesegSTRRILIPFSqrklTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPERYHCIEKGFVPLNQTE 490
Cdd:cd02660 105 H-----YGGDKNEAND----ESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSGT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 491 CLLTEMLAKFTETEALEGRIYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVIF 570
Cdd:cd02660 176 PTLSDCLDRFTRPEKLGDFAYKCSGCGST-----------QEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQF 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 571 DQVLTMEPYC----CRDMLSSLDKETFAYDLSAVVMHHGKgFGSGHYTAYCYNtEGGFWVHCNDSKLDVCSVEEVCKTQA 646
Cdd:cd02660 245 PLELNMTPYTsssiGDTQDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQ-GDGQWFKFDDAMITRVSEEEVLKSQA 322
|
....*.
gi 38259220 647 YILFYT 652
Cdd:cd02660 323 YLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
392-651 |
2.61e-58 |
|
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: 197.32 E-value: 2.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 392 YDQQDAQEFLCELLHKVQQELESEGSTRRILipfsqrkltKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLE 471
Cdd:cd02257 20 SEQQDAHEFLLFLLDKLHEELKKSSKRTSDS---------SSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 472 FPERyhciekgfvplNQTECLLTEMLAKFTETEALEGriYACDQCNSKRrksnpkplvLSEARKQLMIYRLPQVLRLHLK 551
Cdd:cd02257 91 LPVK-----------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKKK---------KQEATKRLKIKKLPPVLIIHLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 552 RFRWSGRNHREKIGVHVIFDQVLTMEPYCCRD-MLSSLDKETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCND 630
Cdd:cd02257 149 RFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGeKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFND 228
|
250 260
....*....|....*....|....*.
gi 38259220 631 SKLDVCSVEEV-----CKTQAYILFY 651
Cdd:cd02257 229 DKVTEVSEEEVlefgsLSSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
250-651 |
1.03e-48 |
|
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: 173.23 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 250 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPStsehlfpqatngkaqlsgrpasssaaelsvrsvraQGCEPQGLCw 329
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHS-----------------------------------KDCCNEGFC- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 330 ssgasISRSLEliqnkepssKHISlchelhtlfRVMWSGKWALVSPF--AMLHSVWsliPAFRGYDQQDAQEFLCELLHK 407
Cdd:cd02661 46 -----MMCALE---------AHVE---------RALASSGPGSAPRIfsSNLKQIS---KHFRIGRQEDAHEFLRYLLDA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 408 VQqelesegstRRILIPFSQRKLTKQVLK---VVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEfperyhcIEKGfv 484
Cdd:cd02661 100 MQ---------KACLDRFKKLKAVDPSSQettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD-------IKGA-- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 485 plnQTeclLTEMLAKFTETEALEGR-IYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFrwsGRNHREK 563
Cdd:cd02661 162 ---DS---LEDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRF---SNFRGGK 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 564 IGVHVIFDQVLTMEPYccrdmLSSLDKETFAYDLSAVVMHHGKGFGSGHYTAYCyNTEGGFWVHCNDSKLDVCSVEEVCK 643
Cdd:cd02661 222 INKQISFPETLDLSPY-----MSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYV-KSSNGKWYNMDDSKVSPVSIETVLS 295
|
....*...
gi 38259220 644 TQAYILFY 651
Cdd:cd02661 296 QKAYILFY 303
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
352-651 |
5.10e-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: 162.17 E-value: 5.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 352 ISLCHELHTLFrvmwsgkwaLVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKvqqelesegstrriLIPFsqrklt 431
Cdd:cd02667 18 LSQTPALRELL---------SETPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDG--------------LRTF------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 432 kqvlkvVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEfpeRYHCIEKgfvplnqtECLLTEMLAKFTETEALEGR-I 510
Cdd:cd02667 69 ------IDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLP---RSDEIKS--------ECSIESCLKQFTEVEILEGNnK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 511 YACDQCnskrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVIFDQVLTMEPYCCRDMLSSLDK 590
Cdd:cd02667 132 FACENC--------------TKAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 591 ETFAYDLSAVVMHHGkGFGSGHYTAYCY------------------NTEG---GFWVHCNDSKLDVCSVEEVCKTQAYIL 649
Cdd:cd02667 198 SSVLYRLYGVVEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaaDEAGpgsGQWYYISDSDVREVSLEEVLKSEAYLL 276
|
..
gi 38259220 650 FY 651
Cdd:cd02667 277 FY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
393-652 |
1.78e-44 |
|
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: 158.99 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 393 DQQDAQEFLCELLhkvqQELESegstrrilipfsqrkltkqvlkVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEF 472
Cdd:cd02674 21 DQQDAQEFLLFLL----DGLHS----------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 473 PERYHciekgfvplNQTECLLTEMLAKFTETEALEGRIYA-CDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLK 551
Cdd:cd02674 75 PSGSG---------DAPKVTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 552 RFRWSGRNhREKIGVHVIFD-QVLTMEPYCcrdmLSSLDKETFAYDLSAVVMHHGKGFGsGHYTAYCYNTEGGFWVHCND 630
Cdd:cd02674 135 RFSFSRGS-TRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNHYGSLNG-GHYTAYCKNNETNDWYKFDD 208
|
250 260
....*....|....*....|..
gi 38259220 631 SKLDVCSVEEVCKTQAYILFYT 652
Cdd:cd02674 209 SRVTKVSESSVVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-653 |
4.00e-40 |
|
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: 150.10 E-value: 4.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNL------DPSTSEHLFPQATNGKAQLSGRPAsssaaelsvrsvraqgcep 324
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIppteddDDNKSVPLALQRLFLFLQLSESPV------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 325 qglcwssgasisrsleliQNKEPSSKHislchelhtlfRVMWsgkWALVSPFamlhsvwslipafrgyDQQDAQEFLCEL 404
Cdd:cd02659 65 ------------------KTTELTDKT-----------RSFG---WDSLNTF----------------EQHDVQEFFRVL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 405 LHKVQQELESEGstrrilipfsQRKLtkqvlkvVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFperyhcieKGFV 484
Cdd:cd02659 97 FDKLEEKLKGTG----------QEGL-------IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAV--------KGKK 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 485 PlnqteclLTEMLAKFTETEALEG-RIYACDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLKRFRWSG-RNHRE 562
Cdd:cd02659 152 N-------LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFEFDFeTMMRI 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 563 KIGVHVIFDQVLTMEPYCCRDMLS------SLDKETFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVC 636
Cdd:cd02659 214 KINDRFEFPLELDMEPYTEKGLAKkegdseKKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPF 292
|
410 420 430
....*....|....*....|....*....|....*....
gi 38259220 637 SVEEVCK----------------------TQAYILFYTR 653
Cdd:cd02659 293 DPNDAEEecfggeetqktydsgprafkrtTNAYMLFYER 331
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-652 |
2.33e-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: 142.17 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLdPSTsehlfpQATNGKAQLSGRPASSSaaelsvrsvraqgcepqglcws 330
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEC-NST------EDAELKNMPPDKPHEPQ---------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 331 sgasisrsleliqnkepsskhiSLCHELHTLFRVMWSGKWALVSPFAmlhsvwsLIPAFR--GYDQQDAQEFLCELLHKV 408
Cdd:cd02668 52 ----------------------TIIDQLQLIFAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFSKLFLSLL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 409 QQELESEgstrrilipfsqrkLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEfperyhciekgfvpLNQ 488
Cdd:cd02668 103 EAKLSKS--------------KNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQ--------------LKG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 489 TECLlTEMLAKFTETEALEG-RIYACDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLKRF---RWSGrnHREKI 564
Cdd:cd02668 155 HKTL-EECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFvfdRKTG--AKKKL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 565 GVHVIFDQVLTMEPYCCRDmlsslDKETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLD---------- 634
Cdd:cd02668 221 NASISFPEILDMGEYLAES-----DEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEempgkplklg 295
|
410 420
....*....|....*....|....*....
gi 38259220 635 -----------VCSVEEVCKTQAYILFYT 652
Cdd:cd02668 296 nsedpakprksEIKKGTHSSRTAYMLVYK 324
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
358-652 |
3.47e-35 |
|
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: 135.13 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 358 LHTLFRVMWSGK--WALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEGSTRRILIPFSQRKLTKQVL 435
Cdd:cd02663 27 LKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 436 KVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPEryhciekgfvplnqtECLLTEMLAKFTETEALEGR-IYACD 514
Cdd:cd02663 107 TWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ---------------NTSITSCLRQFSATETLCGRnKFYCD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 515 QCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSGRNHR-EKIGVHVIFDqvLTMEPYCCRDMLSSLDKEtf 593
Cdd:cd02663 172 ECCSLQ-----------EAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFP--LELRLFNTTDDAENPDRL-- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38259220 594 aYDLSAVVMHHGKGFGSGHYTAYCYNTegGFWVHCND---SKLDVCSVEEV-----CKTQAYILFYT 652
Cdd:cd02663 237 -YELVAVVVHIGGGPNHGHYVSIVKSH--GGWLLFDDetvEKIDENAVEEFfgdspNQATAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-651 |
2.42e-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: 107.03 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPStsehlfpqatngkaqlsgrpasssaaelsvrsvRAQGCEPqglcws 330
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPA---------------------------------RRGANQS------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 331 sgasisrsleliqnkepsskHISLCHELHTLFRVMwSGKWALVSPFAMLHSVWSLIPAF------RGYDQQDAQEFLCEL 404
Cdd:cd02657 42 --------------------SDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQFaekqnqGGYAQQDAEECWSQL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 405 LHKVQQELESEGSTRRilipfsqrkltkqvlkVVNTIFHGQLLSQVTCI-SCNYKSNTIEPFWDLSLefperyHCIEKGF 483
Cdd:cd02657 101 LSVLSQKLPGAGSKGS----------------FIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQC------HISITTE 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 484 VplnqtECLLTEMLAKFTETEALEGRIYACDQCNSKRRKsnpkplvlsearkqlmIYRLPQVLRLHLKRFRWSGR-NHRE 562
Cdd:cd02657 159 V-----NYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSR----------------ISRLPKYLTVQFVRFFWKRDiQKKA 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 563 KIGVHVIFDQVLTMEPYCCrdmlssldkETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVEEVC 642
Cdd:cd02657 218 KILRKVKFPFELDLYELCT---------PSGYYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDIL 288
|
410
....*....|....*.
gi 38259220 643 KTQ-------AYILFY 651
Cdd:cd02657 289 KLSgggdwhiAYILLY 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
246-651 |
6.25e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 103.43 E-value: 6.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 246 APGVTGLRNLGNTCYMNSILQVLSHLQKFREcflNLdpstsEHLFpqatngkaqlsgrpasssaaelsvrsvraqgcepq 325
Cdd:cd02671 21 LLPFVGLNNLGNTCYLNSVLQVLYFCPGFKH---GL-----KHLV----------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 326 glcwSSGASISrsleliqnkepssKHISLCHELHTLFrvmwSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELL 405
Cdd:cd02671 58 ----SLISSVE-------------QLQSSFLLNPEKY----NDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCIL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 406 HKVQQELESegstrrilipfsqrkltkqvlkvvntIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPERYHCIEKGFVP 485
Cdd:cd02671 117 GNIQELVEK--------------------------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 486 LNQTECLLTEMLAKFTETEALEGRI-----YACDQCNSkrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWSGRNH 560
Cdd:cd02671 171 ISPDPKTEMKTLKWAISQFASVERIvgedkYFCENCHH-----------YTEAERSLLFDKLPEVITIHLKCFAANGSEF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 561 REKIGVHVIFDQVLTMEPYCCRDMLSSLDKETfaYDLSAVVMHHGKGFGSGHYTAYCYnteggfWVHCNDSK-------- 632
Cdd:cd02671 240 DCYGGLSKVNTPLLTPLKLSLEEWSTKPKNDV--YRLFAVVMHSGATISSGHYTAYVR------WLLFDDSEvkvteekd 311
|
410 420
....*....|....*....|
gi 38259220 633 -LDVCSVEEVCKTQAYILFY 651
Cdd:cd02671 312 fLEALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-651 |
1.00e-23 |
|
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: 102.57 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLdpsTSEHLFPQATNGKAQLSgrpassSAAELSVRSVRAqgcepqglcws 330
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSL---NLPRLGDSQSVMKKLQL------LQAHLMHTQRRA----------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 331 sGASISRSLELiqnkepsskhislchelhtlfrvmwsgkwalvspfamlhsvwSLIPAFRGYDQQDAQEFLCELLHKVQQ 410
Cdd:cd02664 61 -EAPPDYFLEA------------------------------------------SRPPWFTPGSQQDCSEYLRYLLDRLHT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 411 elesegstrrilipfsqrkltkqvlkVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPeryhciekgfvplnqte 490
Cdd:cd02664 98 --------------------------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP----------------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 491 cLLTEMLAKFTETEALEG-RIYACDQCNSkrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWSGRNH-REKIGVHV 568
Cdd:cd02664 135 -SVQDLLNYFLSPEKLTGdNQYYCEKCAS-----------LQDAEKEMKVTGAPEYLILTLLRFSYDQKTHvREKIMDNV 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 569 IFDQVLTM----------EPYCCRDMLSSLDKE----TFAYDLSAVVMHHGKGFGSGHYtaYCY---------------- 618
Cdd:cd02664 203 SINEVLSLpvrvesksseSPLEKKEEESGDDGElvtrQVHYRLYAVVVHSGYSSESGHY--FTYardqtdadstgqecpe 280
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 38259220 619 ------NTEGGFWVHCNDSKLDVCSVEEV-------CKTQAYILFY 651
Cdd:cd02664 281 pkdaeeNDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-651 |
1.55e-23 |
|
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: 101.63 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLdpstsEHLFPQATNgkaqlsgRPASSSAAELS-VRsvraqgcepQGLCw 329
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDL-----ENKFPSDVV-------DPANDLNCQLIkLA---------DGLL- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 330 sSGASiSRSLELIQNKEPSSKHISlchelhtlfrvmwsgkwalvsPFaMLHSvwsLI----PAFRGYDQQDAQEFLCELL 405
Cdd:cd02658 59 -SGRY-SKPASLKSENDPYQVGIK---------------------PS-MFKA---LIgkghPEFSTMRQQDALEFLLHLI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 406 HKVQQELESEGSTRrilipfsqrkltkqvlkvVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPER----YHCIEK 481
Cdd:cd02658 112 DKLDRESFKNLGLN------------------PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDeateKEEGEL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 482 GFVPLNQTEClltemLAKFTETEALEgriYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFR----WSG 557
Cdd:cd02658 174 VYEPVPLEDC-----LKAYFAPETIE---DFCSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQllenWVP 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 558 RnhreKIGVHVIFDQVLTMEPyccrdmlssldketfaYDLSAVVMHHGKGFGSGHYTAYCY--NTEGGFWVHCNDSKLDV 635
Cdd:cd02658 235 K----KLDVPIDVPEELGPGK----------------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFNDEKVVA 294
|
410
....*....|....*.
gi 38259220 636 CSVEEVCKTQAYILFY 651
Cdd:cd02658 295 SQDPPEMKKLGYIYFY 310
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
26-87 |
1.14e-22 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 91.55 E-value: 1.14e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38259220 26 CLQCATTESAWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDLYVFCYLCKDYVLNDN 87
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
248-655 |
2.18e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 99.19 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 248 GVTGLRNLGNTCYMNSILQVLSHLQKFRECFLnldpstsehlfpqatngkaqlsgrpasssaaelsvrsvraqgcepqgl 327
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL------------------------------------------------ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 328 cwssgasiSRSLELIQNKE-PSSKHISLCHELHTLFRVMWSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLC---- 402
Cdd:COG5560 296 --------SDEYEESINEEnPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAflld 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 403 ---ELLHKVQQELESEGSTRRILIPFSQRKLTKQVLK--------VVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSL- 470
Cdd:COG5560 368 glhEDLNRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLp 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 471 ---------------------------------------------------------------------------EFPER 475
Cdd:COG5560 448 lpvsmvwkhtivvfpesgrrqplkieldasstirglkklvdaeygklgcfeikvmciyyggnynmlepadkvllqDIPQT 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 476 YHCIEKG----------------------------FVPLN----------------------------------QTECLL 493
Cdd:COG5560 528 DFVYLYEtndngievpvvhlriekgykskrlfgdpFLQLNvlikasiydklvkefeellvlvemkktdvdlvseQVRLLR 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 494 TEM----------------------------------------------------------------------LAKFTET 503
Cdd:COG5560 608 EESspsswlkleteidtkreeqveeegqmnfndavvisceweekrylslfsydplwtireigaaertitlqdcLNEFSKP 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 504 EAL--EGRIYaCDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRwSGRNHREKIGVHV---IFDQVLTMep 578
Cdd:COG5560 688 EQLglSDSWY-CPGCKEFR-----------QASKQMELWRLPMILIIHLKRFS-SVRSFRDKIDDLVeypIDDLDLSG-- 752
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38259220 579 yccrdMLSSLDKETFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVEEVCKTQAYILFYTRRT 655
Cdd:COG5560 753 -----VEYMVDDPRLIYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
383-651 |
2.90e-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: 93.20 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 383 WSLIPAFRGY-----DQQDAQEFLCELLHKVQQELESegstrriliPFsqrkltkqvlkvvntifHGQLLSQVTCISCNY 457
Cdd:cd02662 18 LASLPSLIEYleeflEQQDAHELFQVLLETLEQLLKF---------PF-----------------DGLLASRIVCLQCGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 458 KSN-TIEPFWDLSLEFPERyhciekgfvpLNQTECLLTEMLAKFTETEALEGriYACDQCnskrrksnpkplvlsearkQ 536
Cdd:cd02662 72 SSKvRYESFTMLSLPVPNQ----------SSGSGTTLEHCLDDFLSTEIIDD--YKCDRC-------------------Q 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 537 LMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVIFDQVLTmepyccrdmlssldkeTFAYDLSAVVMHHGkGFGSGHYTAY 616
Cdd:cd02662 121 TVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERLP----------------KVLYRLRAVVVHYG-SHSSGHYVCY 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 38259220 617 --------------------CYNTEGGFWVHCNDSKLDVCSVEEVCKT-QAYILFY 651
Cdd:cd02662 184 rrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLEQkSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
251-653 |
8.84e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 90.25 E-value: 8.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 251 GLRNLGNTCYMNSILQVLShlqkfrecfLNLdPSTSEHLFPQATNGKAqlsgrpasssaaelsvrsvraqgcepqglcws 330
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA---------LYL-PKLDELLDDLSKELKV-------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 331 sgasisrsleLIQNKEPSSKHISLChELHTLFRVMWSGKwalvspfamLHSVWSLIPAfrgYDQQDAQEFLCELLHKVQQ 410
Cdd:COG5533 39 ----------LKNVIRKPEPDLNQE-EALKLFTALWSSK---------EHKVGWIPPM---GSQEDAHELLGKLLDELKL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 411 ELESEGsTRRILIPFSqrkltkqvlkvvntifhgqllsqvtciscNYKSNTIEPFWDLSLEFPERyhcieKGFVPLNQTE 490
Cdd:COG5533 96 DLVNSF-TIRIFKTTK-----------------------------DKKKTSTGDWFDIIIELPDQ-----TWVNNLKTLQ 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 491 CLLTEMLAKFTetealegriyacDQCNSKRrKSNPKPLVLSEARKQLMIYRLPQVLRLHLKRFRWSGRNHR------EKI 564
Cdd:COG5533 141 EFIDNMEELVD------------DETGVKA-KENEELEVQAKQEYEVSFVKLPKILTIQLKRFANLGGNQKidtevdEKF 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 565 GVHVIFDQvltmepyccrdmlSSLDKETFAYDLSAVVMHHGkGFGSGHYTAYCynTEGGFWVHCNDSKLDVCSVEEVCKT 644
Cdd:COG5533 208 ELPVKHDQ-------------ILNIVKETYYDLVGFVLHQG-SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINE 271
|
410
....*....|..
gi 38259220 645 ---QAYILFYTR 653
Cdd:COG5533 272 kakNAYLYFYER 283
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
248-641 |
5.88e-16 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 82.23 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 248 GVTGLRNLGNTCYMNSILQVLSHLQKFRecflnldpstsehlfpqatngkaqlsgrpasssaaelsvrsvraqgcepqgl 327
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFR---------------------------------------------------- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 328 cwssgasisRSLELIQNKEPSSKHiSLCHELHTLFRVMWSGKwalvSPFAMLHSVWSLI-PAFRGYDQQDAQEFlcellh 406
Cdd:COG5077 220 ---------KDVYGIPTDHPRGRD-SVALALQRLFYNLQTGE----EPVDTTELTRSFGwDSDDSFMQHDIQEF------ 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 407 kvqqelesegstRRILIPFSQRKLTKQVLK-VVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFperyhcieKGFVP 485
Cdd:COG5077 280 ------------NRVLQDNLEKSMRGTVVEnALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--------KGMKN 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 486 LNqteclltEMLAKFTETEALEG-RIYACDQCNskrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWS-GRNHREK 563
Cdd:COG5077 340 LQ-------ESFRRYIQVETLDGdNRYNAEKHG------------LQDAKKGVIFESLPPVLHLQLKRFEYDfERDMMVK 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38259220 564 IGVHVIFDQVLTMEPYCCRDMLSSLDKEtFAYDLSAVVMHHGKgFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVEEV 641
Cdd:COG5077 401 INDRYEFPLEIDLLPFLDRDADKSENSD-AVYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
26-72 |
3.36e-14 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 67.01 E-value: 3.36e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 38259220 26 CLQCATTESAWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDL 72
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQ 48
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
247-651 |
6.63e-14 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 74.28 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 247 PGVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSTSEhlfpqaTNGKAQLSGRPAsssaaeLSVRSVraqgcepqg 326
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENI------KDRKSELVKRLS------ELIRKI--------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 327 lcWSsgasisrsleliqnkepsskhislchelHTLFRvmwsgkwALVSPFAMLH--SVWSLIPaFRGYDQQDAQEFLCEL 404
Cdd:cd02669 176 --WN----------------------------PRNFK-------GHVSPHELLQavSKVSKKK-FSITEQSDPVEFLSWL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 405 LHKVQQELE-SEGSTRRILIPFSQRKLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIePFWDLSLEFPER---YHCIE 480
Cdd:cd02669 218 LNTLHKDLGgSKKPNSSIIHDCFQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLPPPplfKDGNE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 481 KGFVPlnQTecLLTEMLAKFTETEALEgriyacdqcnskrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRwsgRNH 560
Cdd:cd02669 297 ENIIP--QV--PLKQLLKKYDGKTETE----------------------LKDSLKRYLISRLPKYLIFHIKRFS---KNN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 561 --REKIGVHVIFDQVLTMEPYCCRDMLSSLDKETfAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSV 638
Cdd:cd02669 348 ffKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLST-KYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLP 426
|
410
....*....|...
gi 38259220 639 EEVCKTQAYILFY 651
Cdd:cd02669 427 QLIFLSESYIQIW 439
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
250-641 |
3.88e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 71.37 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 250 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSTSEhlfpqatngkaqlsgrpasSSAAELSVRSVraqgcepqglcw 329
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAE-------------------LASDYPTERRI------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 330 sSGASISRSLELIQNKepsskhisLCHELHTLFRVMWSGKWALVSPFAMLhsvwslipAFRGYDQQDAQEflceLLHKVQ 409
Cdd:cd02666 51 -GGREVSRSELQRSNQ--------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVTE----CIDNVL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 410 QELESEGSTRRILIPFSQRKLTKQVLKVVNTIFHGQLLSQVT-CISCNYKSNTIEPFWDLSLEFPeryhCIEKGFVPLNQ 488
Cdd:cd02666 110 FQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVD----VGKKGREIVVL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 489 TE-CLLTEMLAKFTETEALEG-RIYACDQCN----------SKRRKSNPKPL-VLSEARKQLMIYRLPQVLRLhlkrfRW 555
Cdd:cd02666 186 LEpKDLYDALDRYFDYDSLTKlPQRSQVQAQlaqplqreliSMDRYELPSSIdDIDELIREAIQSESSLVRQA-----QN 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 556 SGRNHREKIgvHVIFDqvltmepyccrdmlsslDKETFAYDLSAVVMHHGKGfGSGHYTAYCYNTEGGFWVHCNDSKLDV 635
Cdd:cd02666 261 ELAELKHEI--EKQFD-----------------DLKSYGYRLHAVFIHRGEA-SSGHYWVYIKDFEENVWRKYNDETVTV 320
|
....*.
gi 38259220 636 CSVEEV 641
Cdd:cd02666 321 VPASEV 326
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
379-651 |
8.23e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 68.71 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 379 LHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEgSTRRILIPFSQRKLTK-QVLKV-VNTIFhgqllsqvTCISCN 456
Cdd:cd02673 18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVN-RTNVPPSNIEIKRLNPlEAFKYtIESSY--------VCIGCS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 457 YKSNTIEPFWDLSLEFPERYHCIEKgfvplnqtecLLTEMLAKFTETEAlegriyACDQCNSKRRKSNPKplvlsearkq 536
Cdd:cd02673 89 FEENVSDVGNFLDVSMIDNKLDIDE----------LLISNFKTWSPIEK------DCSSCKCESAISSER---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 537 lmIYRLPQVLRLHLKRFRWsgrnhREKIGVHVIfDQVLTMEPYCcrdmlSSLDKetfaYDLSAVVMHHGKGFGSGHYTAY 616
Cdd:cd02673 143 --IMTFPECLSINLKRYKL-----RIATSDYLK-KNEEIMKKYC-----GTDAK----YSLVAVICHLGESPYDGHYIAY 205
|
250 260 270
....*....|....*....|....*....|....*....
gi 38259220 617 CYN-TEGGFWVHCNDSKLDVCSVEEVCK---TQAYILFY 651
Cdd:cd02673 206 TKElYNGSSWLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
542-651 |
2.76e-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: 42.93 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38259220 542 LPQVLRLHLKRFRWsGRNHREKIGVHVIFDQVLTMEPYccrdmlssldketfayDLSAVVMHHGKGfGSGHYTAYCYNTE 621
Cdd:cd02665 128 LPPVLTFELSRFEF-NQGRPEKIHDKLEFPQIIQQVPY----------------ELHAVLVHEGQA-NAGHYWAYIYKQS 189
|
90 100 110
....*....|....*....|....*....|....*...
gi 38259220 622 GGFWVHCNDSKLDVCSVEEVCK--------TQAYILFY 651
Cdd:cd02665 190 RQEWEKYNDISVTESSWEEVERdsfgggrnPSAYCLMY 227
|
|
| |
