|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
250-651 |
7.19e-71 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 232.72 E-value: 7.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 250 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSTSehlfpqatngkaqipsrpasstaagfsvrsdraqgfepqgfcw 329
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSE------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 330 ssgasisrsleliqnKEPSSKHISLCHELHTLFRVMWSGKW-ALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKV 408
Cdd:pfam00443 38 ---------------DSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 409 QQELESEGSTRRILIpfsqrkltkqvlkvVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPERYHCVEkgfvplnq 488
Cdd:pfam00443 103 HEDLNGNHSTENESL--------------ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK-------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 489 tECLLTEMLAKFTETEALEGRI-YACDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSgRNHREKIGVH 567
Cdd:pfam00443 161 -TASLQICFLQFSKLEELDDEEkYYCDKCGCKQ-----------DAIKQLKISRLPPVLIIHLKRFSYN-RSTWEKLNTE 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 568 VVFDQVLTMEPYCCGDmLSSLDKDTFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVE-EVCKTQA 646
Cdd:pfam00443 228 VEFPLELDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSA 305
|
....*
gi 1958802143 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 |
2.24e-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: 210.69 E-value: 2.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLnldpstsehlfpqatngkaqipsrpasstaagfsvrSDRAQGFepqgfcws 330
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL------------------------------------SDRHSCT-------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 331 sgasisrsleliqNKEPSSKHiSLCHELHTLFRVMW-SGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQ 409
Cdd:cd02660 38 -------------CLSCSPNS-CLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 410 QElesegSTRRILIPFSqrklTKQVLKVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPERYHCVEKGFVPLNQT 489
Cdd:cd02660 104 TH-----YGGDKNEAND----ESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSG 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 490 ECLLTEMLAKFTETEALEGRIYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVV 569
Cdd:cd02660 175 TPTLSDCLDRFTRPEKLGDFAYKCSGCGST-----------QEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQ 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 570 FDQVLTMEPYC----CGDMLSSLDKDTFAYDLSAVVMHHGKgFGSGHYTAYCYNtEGGFWVHCNDSKLDVCSVEEVCKTQ 645
Cdd:cd02660 244 FPLELNMTPYTsssiGDTQDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQ-GDGQWFKFDDAMITRVSEEEVLKSQ 321
|
....*..
gi 1958802143 646 AYILFYT 652
Cdd:cd02660 322 AYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
392-651 |
2.56e-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: 2.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 392 YDQQDAQEFLCELLHKVQQELESEGSTRRILipfsqrkltKQVLKVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLE 471
Cdd:cd02257 20 SEQQDAHEFLLFLLDKLHEELKKSSKRTSDS---------SSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 472 FPERyhcvekgfvplNQTECLLTEMLAKFTETEALEGriYACDQCNSKRrksnpkplvLSEARKQLMIYRLPQVLRLHLK 551
Cdd:cd02257 91 LPVK-----------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKKK---------KQEATKRLKIKKLPPVLIIHLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 552 RFRWSGRNHREKIGVHVVFDQVLTMEPYC-CGDMLSSLDKDTFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCND 630
Cdd:cd02257 149 RFSFNEDGTKEKLNTKVSFPLELDLSPYLsEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFND 228
|
250 260
....*....|....*....|....*.
gi 1958802143 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 |
1.99e-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: 172.46 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 250 TGLRNLGNTCYMNSILQVLSHlqkfrecflnldpstsehlfpqatngkaqipSRPAsstaAGFSVRSDRAQGFEPQGFCw 329
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTH-------------------------------TPPL----ANYLLSREHSKDCCNEGFC- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 330 ssgasISRSLEliqnkepssKHISlchelhtlfRVMWSGKWALVSPF--AMLHSVWsliPAFRGYDQQDAQEFLCELLHK 407
Cdd:cd02661 46 -----MMCALE---------AHVE---------RALASSGPGSAPRIfsSNLKQIS---KHFRIGRQEDAHEFLRYLLDA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 408 VQqelesegstRRILIPFSQRKLTKQVLK---VVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEfperyhcVEKGfv 484
Cdd:cd02661 100 MQ---------KACLDRFKKLKAVDPSSQettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD-------IKGA-- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 485 plnQTeclLTEMLAKFTETEALEGR-IYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFrwsGRNHREK 563
Cdd:cd02661 162 ---DS---LEDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRF---SNFRGGK 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 564 IGVHVVFDQVLTMEPYccgdmLSSLDKDTFAYDLSAVVMHHGKGFGSGHYTAYCyNTEGGFWVHCNDSKLDVCSVEEVCK 643
Cdd:cd02661 222 INKQISFPETLDLSPY-----MSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYV-KSSNGKWYNMDDSKVSPVSIETVLS 295
|
....*...
gi 1958802143 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 |
5.53e-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: 5.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 352 ISLCHELHTLFrvmwsgkwaLVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKvqqelesegstrriLIPFsqrklt 431
Cdd:cd02667 18 LSQTPALRELL---------SETPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDG--------------LRTF------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 432 kqvlkvVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPEryhcvekgfvpLNQTECLLTEMLAKFTETEALEGR-I 510
Cdd:cd02667 69 ------IDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSD-----------EIKSECSIESCLKQFTEVEILEGNnK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 511 YACDQCnskrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVFDQVLTMEPYCCGDMLSSLDK 590
Cdd:cd02667 132 FACENC--------------TKAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 591 DTFAYDLSAVVMHHGkGFGSGHYTAYCY------------------NTEG---GFWVHCNDSKLDVCSVEEVCKTQAYIL 649
Cdd:cd02667 198 SSVLYRLYGVVEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaaDEAGpgsGQWYYISDSDVREVSLEEVLKSEAYLL 276
|
..
gi 1958802143 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 |
5.81e-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: 160.15 E-value: 5.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 393 DQQDAQEFLCELLhkvqQELESegstrrilipfsqrkltkqvlkVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEF 472
Cdd:cd02674 21 DQQDAQEFLLFLL----DGLHS----------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 473 PERYHcvekgfvplNQTECLLTEMLAKFTETEALEGRIYA-CDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLK 551
Cdd:cd02674 75 PSGSG---------DAPKVTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 552 RFRWSGRNhREKIGVHVVFD-QVLTMEPYCcgdmLSSLDKDTFAYDLSAVVMHHGKGFGsGHYTAYCYNTEGGFWVHCND 630
Cdd:cd02674 135 RFSFSRGS-TRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNHYGSLNG-GHYTAYCKNNETNDWYKFDD 208
|
250 260
....*....|....*....|..
gi 1958802143 631 SKLDVCSVEEVCKTQAYILFYT 652
Cdd:cd02674 209 SRVTKVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-652 |
2.18e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 144.87 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLdPSTsehlfpQATNGKAQIPSRPasstaagfsvrsdraqgFEPQGfcws 330
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEC-NST------EDAELKNMPPDKP-----------------HEPQT---- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 331 sgasisrsleliqnkepsskhisLCHELHTLFRVMWSGKWALVSPFAmlhsvwsLIPAFR--GYDQQDAQEFLCELLHKV 408
Cdd:cd02668 53 -----------------------IIDQLQLIFAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFSKLFLSLL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 409 QQELESEgstrrilipfsqrkLTKQVLKVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEfperyhcvekgfvpLNQ 488
Cdd:cd02668 103 EAKLSKS--------------KNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQ--------------LKG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 489 TECLlTEMLAKFTETEALEG-RIYACDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLKRF---RWSGrnHREKI 564
Cdd:cd02668 155 HKTL-EECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFvfdRKTG--AKKKL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 565 GVHVVFDQVLTMEPYCCGDmlsslDKDTFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLD---------- 634
Cdd:cd02668 221 NASISFPEILDMGEYLAES-----DEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEempgkplklg 295
|
410 420
....*....|....*....|....*....
gi 1958802143 635 -----------VCSVEEVCKTQAYILFYT 652
Cdd:cd02668 296 nsedpakprksEIKKGTHSSRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-653 |
2.45e-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: 145.09 E-value: 2.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPstsehlfpqatngkaqipsrpasstaagfsvrsdrAQGFEPQgfcws 330
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPP-----------------------------------TEDDDDN----- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 331 sgASISRSLELIQNKEPSSKHISLCHELHTLFRVMWsgkWALVSPFamlhsvwslipafrgyDQQDAQEFLCELLHKVQQ 410
Cdd:cd02659 44 --KSVPLALQRLFLFLQLSESPVKTTELTDKTRSFG---WDSLNTF----------------EQHDVQEFFRVLFDKLEE 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 411 ELESEGstrrilipfsQRKLtkqvlkvVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFperyhcveKGFVPlnqte 490
Cdd:cd02659 103 KLKGTG----------QEGL-------IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAV--------KGKKN----- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 491 clLTEMLAKFTETEALEG-RIYACDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLKRFRWSG-RNHREKIGVHV 568
Cdd:cd02659 153 --LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFEFDFeTMMRIKINDRF 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 569 VFDQVLTMEPYC------CGDMLSSLDKDTFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVEEVC 642
Cdd:cd02659 220 EFPLELDMEPYTekglakKEGDSEKKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAE 298
|
410 420 430
....*....|....*....|....*....|...
gi 1958802143 643 K----------------------TQAYILFYTR 653
Cdd:cd02659 299 EecfggeetqktydsgprafkrtTNAYMLFYER 331
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
358-652 |
2.01e-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: 135.90 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 358 LHTLFRVMWSGK--WALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEGSTRRILIPFSQRKLTKQVL 435
Cdd:cd02663 27 LKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 436 KVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPEryhcvekgfvplnqtECLLTEMLAKFTETEALEGR-IYACD 514
Cdd:cd02663 107 TWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ---------------NTSITSCLRQFSATETLCGRnKFYCD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 515 QCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSGRNHR-EKIGVHVVFDqvLTMEPYCCGDMLSSLDKdtf 593
Cdd:cd02663 172 ECCSLQ-----------EAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFP--LELRLFNTTDDAENPDR--- 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958802143 594 AYDLSAVVMHHGKGFGSGHYTAYCYNTegGFWVHCND---SKLDVCSVEEV-----CKTQAYILFYT 652
Cdd:cd02663 236 LYELVAVVVHIGGGPNHGHYVSIVKSH--GGWLLFDDetvEKIDENAVEEFfgdspNQATAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-651 |
1.01e-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: 108.19 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPStsehlfpqatngkaqipSRPASSTAAGFSVrsdraqgfepqgfcws 330
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPA-----------------RRGANQSSDNLTN---------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 331 sgasisrsleliqnkepsskhislchELHTLFRVMwSGKWALVSPFAMLHSVWSLIPAF------RGYDQQDAQEFLCEL 404
Cdd:cd02657 48 --------------------------ALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQFaekqnqGGYAQQDAEECWSQL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 405 LHKVQQELESEGSTRRilipfsqrkltkqvlkVVNTIFHGQLLSQVTCV-SCNYKSNTIEPFWDLSLefperyHCVEKGF 483
Cdd:cd02657 101 LSVLSQKLPGAGSKGS----------------FIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQC------HISITTE 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 484 VplnqtECLLTEMLAKFTETEALEGRIYACDQCNSKRRKsnpkplvlsearkqlmIYRLPQVLRLHLKRFRWSGR-NHRE 562
Cdd:cd02657 159 V-----NYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSR----------------ISRLPKYLTVQFVRFFWKRDiQKKA 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 563 KIGVHVVFDQVLTMEPYCCGdmlSSLdkdtfaYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVEEVC 642
Cdd:cd02657 218 KILRKVKFPFELDLYELCTP---SGY------YELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDIL 288
|
410
....*....|....*.
gi 1958802143 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 |
1.74e-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: 104.97 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 246 APGVTGLRNLGNTCYMNSILQVLSHLQKFREcflNLdpstsEHLFpqatngkaqipsrpasstaagfsvrsdraqgfepq 325
Cdd:cd02671 21 LLPFVGLNNLGNTCYLNSVLQVLYFCPGFKH---GL-----KHLV----------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 326 gfcwSSGASISrsleliqnkepssKHISLCHELHTLFrvmwSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELL 405
Cdd:cd02671 58 ----SLISSVE-------------QLQSSFLLNPEKY----NDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCIL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 406 HKVQQELESegstrrilipfsqrkltkqvlkvvntIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPERYHCVEKGFVP 485
Cdd:cd02671 117 GNIQELVEK--------------------------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 486 LNQTECLLTEMLAKFTETEALEGRI-----YACDQCNSkrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWSGRNH 560
Cdd:cd02671 171 ISPDPKTEMKTLKWAISQFASVERIvgedkYFCENCHH-----------YTEAERSLLFDKLPEVITIHLKCFAANGSEF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 561 REKIGVHVVFDQVLTMEPYCCGDMLSSLDKDTfaYDLSAVVMHHGKGFGSGHYTAYCYnteggfWVHCNDSK-------- 632
Cdd:cd02671 240 DCYGGLSKVNTPLLTPLKLSLEEWSTKPKNDV--YRLFAVVMHSGATISSGHYTAYVR------WLLFDDSEvkvteekd 311
|
410 420
....*....|....*....|
gi 1958802143 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 |
2.89e-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: 101.41 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPstsehlfpQATNGkaqipsrpasstaagfsvrsdraqgfepqgfcws 330
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNL--------PRLGD---------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 331 sgasisrsleliQNKEPSSKHISLCHELHTLFRvmwsgkwALVSPFAMLHSVWSliPAFRGYDQQDAQEFLCELLHKVQQ 410
Cdd:cd02664 39 ------------SQSVMKKLQLLQAHLMHTQRR-------AEAPPDYFLEASRP--PWFTPGSQQDCSEYLRYLLDRLHT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 411 elesegstrrilipfsqrkltkqvlkVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPeryhcvekgfvplnqte 490
Cdd:cd02664 98 --------------------------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP----------------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 491 cLLTEMLAKFTETEALEG-RIYACDQCNSkrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWSGRNH-REKIGVHV 568
Cdd:cd02664 135 -SVQDLLNYFLSPEKLTGdNQYYCEKCAS-----------LQDAEKEMKVTGAPEYLILTLLRFSYDQKTHvREKIMDNV 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 569 VFDQVLTM----------EPYCCGDMLSSLDKD----TFAYDLSAVVMHHGKGFGSGHYtaYCY---------------- 618
Cdd:cd02664 203 SINEVLSLpvrvesksseSPLEKKEEESGDDGElvtrQVHYRLYAVVVHSGYSSESGHY--FTYardqtdadstgqecpe 280
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958802143 619 ------NTEGGFWVHCNDSKLDVCSVEEV-------CKTQAYILFY 651
Cdd:cd02664 281 pkdaeeNDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
26-87 |
4.58e-23 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 92.71 E-value: 4.58e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958802143 26 CLECATTESAWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDLYVFCYLCKDYVLNDN 87
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-651 |
2.39e-22 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 98.16 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLdpstsEHLFPQAtngkaqiPSRPASStaagfsvrsdraqgFEPQ----- 325
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDL-----ENKFPSD-------VVDPAND--------------LNCQlikla 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 326 -GFCwsSGASiSRSLELIQNKEPSSKHISlchelhtlfrvmwsgkwalvsPFaMLHSvwsLI----PAFRGYDQQDAQEF 400
Cdd:cd02658 55 dGLL--SGRY-SKPASLKSENDPYQVGIK---------------------PS-MFKA---LIgkghPEFSTMRQQDALEF 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 401 LCELLHKVQQELESEGSTRrilipfsqrkltkqvlkvVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPER----Y 476
Cdd:cd02658 107 LLHLIDKLDRESFKNLGLN------------------PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDeateK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 477 HCVEKGFVPLNQTEClltemLAKFTETEALEgriYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFR-- 554
Cdd:cd02658 169 EEGELVYEPVPLEDC-----LKAYFAPETIE---DFCSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQll 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 555 --WSGRnhreKIGVHVVFDQVLTMEPyccgdmlssldkdtfaYDLSAVVMHHGKGFGSGHYTAYCY--NTEGGFWVHCND 630
Cdd:cd02658 230 enWVPK----KLDVPIDVPEELGPGK----------------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFND 289
|
410 420
....*....|....*....|.
gi 1958802143 631 SKLDVCSVEEVCKTQAYILFY 651
Cdd:cd02658 290 EKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
383-651 |
7.57e-22 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 95.13 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 383 WSLIPAFRGY-----DQQDAQEFLCELLHKVQQELESegstrriliPFsqrkltkqvlkvvntifHGQLLSQVTCVSCNY 457
Cdd:cd02662 18 LASLPSLIEYleeflEQQDAHELFQVLLETLEQLLKF---------PF-----------------DGLLASRIVCLQCGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 458 KSN-TIEPFWDLSLEFPERyhcvekgfvpLNQTECLLTEMLAKFTETEALEGriYACDQCnskrrksnpkplvlsearkQ 536
Cdd:cd02662 72 SSKvRYESFTMLSLPVPNQ----------SSGSGTTLEHCLDDFLSTEIIDD--YKCDRC-------------------Q 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 537 LMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVFDQVLTmepyccgdmlssldkdTFAYDLSAVVMHHGkGFGSGHYTAY 616
Cdd:cd02662 121 TVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERLP----------------KVLYRLRAVVVHYG-SHSSGHYVCY 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958802143 617 --------------------CYNTEGGFWVHCNDSKLDVCSVEEVCKT-QAYILFY 651
Cdd:cd02662 184 rrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLEQkSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
248-655 |
1.48e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 99.96 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 248 GVTGLRNLGNTCYMNSILQVLSHLQKFRECFLnldpstsehlfpqatngkaqipsrpasstaagfsvrSDraqGFEPQgf 327
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL------------------------------------SD---EYEES-- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 328 cwssgasisrslelIQNKEPSSKHISLCHELHTLFRVMWSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLC----- 402
Cdd:COG5560 303 --------------INEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAflldg 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 403 --ELLHKVQQELESEGSTRRILIPFSQRKLTKQVLK--------VVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSL-- 470
Cdd:COG5560 369 lhEDLNRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLpl 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 471 --------------------------------------------------------------------------EFPERY 476
Cdd:COG5560 449 pvsmvwkhtivvfpesgrrqplkieldasstirglkklvdaeygklgcfeikvmciyyggnynmlepadkvllqDIPQTD 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 477 HCVEKG----------------------------FVPLN----------------------------------QTECLLT 494
Cdd:COG5560 529 FVYLYEtndngievpvvhlriekgykskrlfgdpFLQLNvlikasiydklvkefeellvlvemkktdvdlvseQVRLLRE 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 495 EM----------------------------------------------------------------------LAKFTETE 504
Cdd:COG5560 609 ESspsswlkleteidtkreeqveeegqmnfndavvisceweekrylslfsydplwtireigaaertitlqdcLNEFSKPE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 505 AL--EGRIYaCDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRwSGRNHREKIGVHVVF---DQVLTMepy 579
Cdd:COG5560 689 QLglSDSWY-CPGCKEFR-----------QASKQMELWRLPMILIIHLKRFS-SVRSFRDKIDDLVEYpidDLDLSG--- 752
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958802143 580 ccgdMLSSLDKDTFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVEEVCKTQAYILFYTRRT 655
Cdd:COG5560 753 ----VEYMVDDPRLIYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
251-653 |
2.16e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 89.09 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 251 GLRNLGNTCYMNSILQVLShlqkfrecfLNLdPSTSEHLFPQATNGKAQIpsrpasstaagfSVRSDRaqgFEPQGFCws 330
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA---------LYL-PKLDELLDDLSKELKVLK------------NVIRKP---EPDLNQE-- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 331 sgasisrsleliqnkepsskhislchELHTLFRVMWSGKwalvspfamLHSVWSLIPAfrgYDQQDAQEFLCELLHKVQQ 410
Cdd:COG5533 54 --------------------------EALKLFTALWSSK---------EHKVGWIPPM---GSQEDAHELLGKLLDELKL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 411 ELESEGsTRRILIPFSqrkltkqvlkvvntifhgqllsqvtcvscNYKSNTIEPFWDLSLEFPERyhcveKGFVPLNQTE 490
Cdd:COG5533 96 DLVNSF-TIRIFKTTK-----------------------------DKKKTSTGDWFDIIIELPDQ-----TWVNNLKTLQ 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 491 CLLTEMLAKFTetealegriyacDQCNSKRrKSNPKPLVLSEARKQLMIYRLPQVLRLHLKRFRWSGRNHR------EKI 564
Cdd:COG5533 141 EFIDNMEELVD------------DETGVKA-KENEELEVQAKQEYEVSFVKLPKILTIQLKRFANLGGNQKidtevdEKF 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 565 GVHVVFDQVLTMEPyccgdmlssldkdTFAYDLSAVVMHHGkGFGSGHYTAYCynTEGGFWVHCNDSKLDVCSVEEVCKT 644
Cdd:COG5533 208 ELPVKHDQILNIVK-------------ETYYDLVGFVLHQG-SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINE 271
|
410
....*....|..
gi 1958802143 645 ---QAYILFYTR 653
Cdd:COG5533 272 kakNAYLYFYER 283
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
248-641 |
4.54e-16 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 82.61 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 248 GVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNL-----DPSTSEHLFPQATNGKAQIPSRPASSTAAgfsVRSdraqgf 322
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIptdhpRGRDSVALALQRLFYNLQTGEEPVDTTEL---TRS------ 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 323 epqgFCWSSGASISrsleliqnkepsskhislchelhtlfrvmwsgkwalvspfamlhsvwslipafrgydQQDAQEFlc 402
Cdd:COG5077 263 ----FGWDSDDSFM---------------------------------------------------------QHDIQEF-- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 403 ellhkvqqelesegstRRILIPFSQRKLTKQVLK-VVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFperyhcveK 481
Cdd:COG5077 280 ----------------NRVLQDNLEKSMRGTVVEnALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--------K 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 482 GFVPLNqteclltEMLAKFTETEALEG-RIYACDQCNskrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWS-GRN 559
Cdd:COG5077 336 GMKNLQ-------ESFRRYIQVETLDGdNRYNAEKHG------------LQDAKKGVIFESLPPVLHLQLKRFEYDfERD 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 560 HREKIGVHVVFDQVLTMEPYCCGDMLSSLDKDtFAYDLSAVVMHHGKgFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVE 639
Cdd:COG5077 397 MMVKINDRYEFPLEIDLLPFLDRDADKSENSD-AVYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRATEK 474
|
..
gi 1958802143 640 EV 641
Cdd:COG5077 475 EV 476
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
26-72 |
1.11e-14 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 68.55 E-value: 1.11e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958802143 26 CLECATTESAWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDL 72
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQ 48
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
250-641 |
2.03e-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: 72.14 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 250 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSTSEhlfpqATNGKAQIPSRPasstaagfsvrsdraqgfepqgfcw 329
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAE-----LASDYPTERRIG------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 330 ssGASISRSLELIQNKepsskhisLCHELHTLFRVMWSGKWALVSPFAMLhsvwslipAFRGYDQQDAQEflceLLHKVQ 409
Cdd:cd02666 52 --GREVSRSELQRSNQ--------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVTE----CIDNVL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 410 QELESEGSTRRILIPFSQRKLTKQVLKVVNTIFHGQLLSQVT-CVSCNYKSNTIEPFWDLSLEFPeryhCVEKGFVPLNQ 488
Cdd:cd02666 110 FQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVD----VGKKGREIVVL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 489 TE-CLLTEMLAKFTETEALEG-RIYACDQCN----------SKRRKSNPKPL-VLSEARKQLMIYRLPQVLRLhlkrfRW 555
Cdd:cd02666 186 LEpKDLYDALDRYFDYDSLTKlPQRSQVQAQlaqplqreliSMDRYELPSSIdDIDELIREAIQSESSLVRQA-----QN 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 556 SGRNHREKIgvhvvfdqvltmepyccgdmlSSLDKD--TFAYDLSAVVMHHGKGfGSGHYTAYCYNTEGGFWVHCNDSKL 633
Cdd:cd02666 261 ELAELKHEI---------------------EKQFDDlkSYGYRLHAVFIHRGEA-SSGHYWVYIKDFEENVWRKYNDETV 318
|
....*...
gi 1958802143 634 DVCSVEEV 641
Cdd:cd02666 319 TVVPASEV 326
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
247-651 |
2.66e-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: 72.35 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 247 PGVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDpstsehlfpqatngkaqipsrpasstaagfsvrsdraqgfepqg 326
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYE-------------------------------------------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 327 fcwssgasisrSLELIQNKEPSskhisLCHELHTLFRVMWSGKW--ALVSPFAMLH--SVWSLIPaFRGYDQQDAQEFLC 402
Cdd:cd02669 153 -----------NYENIKDRKSE-----LVKRLSELIRKIWNPRNfkGHVSPHELLQavSKVSKKK-FSITEQSDPVEFLS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 403 ELLHKVQQELE-SEGSTRRILIPFSQRKLTKQVLKVVNTIFHGQLLSQVTCVSCNYKSNTIePFWDLSLEFPERyhcvek 481
Cdd:cd02669 216 WLLNTLHKDLGgSKKPNSSIIHDCFQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLPPP------ 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 482 gfvPLNQTE--------CLLTEMLAKFTETEALEgriyacdqcnskrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRF 553
Cdd:cd02669 289 ---PLFKDGneeniipqVPLKQLLKKYDGKTETE----------------------LKDSLKRYLISRLPKYLIFHIKRF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 554 RwsgRNH--REKIGVHVVFDQVLTMEPYCCGDMLSSLDKDTfAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDS 631
Cdd:cd02669 344 S---KNNffKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLST-KYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDL 419
|
410 420
....*....|....*....|
gi 1958802143 632 KLDVCSVEEVCKTQAYILFY 651
Cdd:cd02669 420 NVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
379-651 |
3.03e-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: 67.17 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 379 LHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEgSTRRILIPFSQRKLTK-QVLKV-VNTIFhgqllsqvTCVSCN 456
Cdd:cd02673 18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVN-RTNVPPSNIEIKRLNPlEAFKYtIESSY--------VCIGCS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 457 YKSNTIEPFWDLSLEFPERYHCVEKgfvplnqtecLLTEMLAKFTETEALegriyaCDQCNSKRRKSNPKplvlsearkq 536
Cdd:cd02673 89 FEENVSDVGNFLDVSMIDNKLDIDE----------LLISNFKTWSPIEKD------CSSCKCESAISSER---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 537 lmIYRLPQVLRLHLKRFRWsgrnhREKIGVHVVfDQVLTMEPYCcgdmlSSLDKdtfaYDLSAVVMHHGKGFGSGHYTAY 616
Cdd:cd02673 143 --IMTFPECLSINLKRYKL-----RIATSDYLK-KNEEIMKKYC-----GTDAK----YSLVAVICHLGESPYDGHYIAY 205
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958802143 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 |
2.20e-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: 43.32 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802143 542 LPQVLRLHLKRFRWsGRNHREKIGVHVVFDQVLTMEPYccgdmlssldkdtfayDLSAVVMHHGKGfGSGHYTAYCYNTE 621
Cdd:cd02665 128 LPPVLTFELSRFEF-NQGRPEKIHDKLEFPQIIQQVPY----------------ELHAVLVHEGQA-NAGHYWAYIYKQS 189
|
90 100 110
....*....|....*....|....*....|....*...
gi 1958802143 622 GGFWVHCNDSKLDVCSVEEVCK--------TQAYILFY 651
Cdd:cd02665 190 RQEWEKYNDISVTESSWEEVERdsfgggrnPSAYCLMY 227
|
|
| |
