|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
69-499 |
9.49e-86 |
|
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: 264.61 E-value: 9.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTtqysrdqqgphthqclsltllnllkalscqevtedevldasclldvlr 148
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFL------------------------------------------------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 149 myrwqissfEEQDAHELFHVITSSLEderdrqprvthlfdvhsleqsemaprqvtchtrgsphpttnhWKSQHPFHGRLT 228
Cdd:cd02662 33 ---------EQQDAHELFQVLLETLE------------------------------------------QLLKFPFDGLLA 61
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 229 SNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieargtltgekvehqrstfv 308
Cdd:cd02662 62 SRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC---------------------- 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 309 kQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdfykyrllghkpsqhgpkatenpgsapevqdaqaapkp 388
Cdd:cd02662 120 -QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL---------------------------------------- 158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 389 glsqpgapktqiflngacspsllpalpspvafplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPSAKN---- 464
Cdd:cd02662 159 ------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKDkepg 196
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2458602108 465 --------PLSTSNQWLWISDDTVRKASLQEVL-SSSAYLLFYE 499
Cdd:cd02662 197 sfvrmregPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
69-499 |
2.16e-48 |
|
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: 167.66 E-value: 2.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSAcpafvkwleefttqysrdqqgphthqclsltllnllkalscqevtedevldasclldvlr 148
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 149 myrwqissfEEQDAHELFHVITSSLEDERDRQPRVThlfDVHSLEQSEMaprqvtchtrgsphpttnhwksQHPFHGRLT 228
Cdd:cd02257 21 ---------EQQDAHEFLLFLLDKLHEELKKSSKRT---SDSSSLKSLI----------------------HDLFGGKLE 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 229 SNMVCKHCEHQSpVRFDTFDSLSLSIPAATWgHPLTLDHCLHHFISSESVRDVVCDNCTKieargtltgekveHQRSTFV 308
Cdd:cd02257 67 STIVCLECGHES-VSTEPELFLSLPLPVKGL-PQVSLEDCLEKFFKEEILEGDNCYKCEK-------------KKKQEAT 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 309 KQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDFYKYRLLGHKPSQHGPkatenpgsapevqdaqaapkp 388
Cdd:cd02257 132 KRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGS--------------------- 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 389 glsqpgapktqiflngacspsllpalpspvafplpvvpdyssstYLFRLMAVVVHHGD-MHSGHFVTYRRSPPsaknpls 467
Cdd:cd02257 191 --------------------------------------------YKYELVAVVVHSGTsADSGHYVAYVKDPS------- 219
|
410 420 430
....*....|....*....|....*....|....*..
gi 2458602108 468 tSNQWLWISDDTVRKASLQEVL-----SSSAYLLFYE 499
Cdd:cd02257 220 -DGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
69-498 |
6.89e-41 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 149.52 E-value: 6.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSACPAFVKWLeeftTQYSRDQQGPHTHQCLSLTLLNLLKALSCQEVTEDEVLDASCLLDVLR 148
Cdd:pfam00443 2 GLVNLGNTCYMNSVLQSLFSIPPFRDYL----LRISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 149 MYRWQISSFEEQDAHELFHVITSSLEDERDRQPRVTHLFDVHSLeqsemaprqvtchtrgsphpttnhwksqhpFHGRLT 228
Cdd:pfam00443 78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDL------------------------------FRGQLK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 229 SNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieargtltgekvEHQR 304
Cdd:pfam00443 128 SRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 305 STfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDFYkyrllghkpsqhgpkatenpgsapevqdaqa 384
Cdd:pfam00443 194 AI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 385 apkpglsqpgapktqiflngaCSPSLLPalpspvafPLPVVPDYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsakn 464
Cdd:pfam00443 240 ---------------------LAEELKP--------KTNNLQDY-------RLVAVVVHSGSLSSGHYIAYIKAY----- 278
|
410 420 430
....*....|....*....|....*....|....*
gi 2458602108 465 plsTSNQWLWISDDTVRKASLQ-EVLSSSAYLLFY 498
Cdd:pfam00443 279 ---ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
69-499 |
3.63e-32 |
|
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: 124.42 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSACPAFVKWLEEfttqysrdqqgphthqclsltllnllkalscqevtedevlDASCLLDVLR 148
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE----------------------------------------TPKELFSQVC 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 149 MYRWQISSFEEQDAHELFHVITSSLEDERDRQprvthlfdvhsleqsemaprqvtchtrgsphpttnhwksqhpFHGRLT 228
Cdd:cd02667 41 RKAPQFKGYQQQDSHELLRYLLDGLRTFIDSI------------------------------------------FGGELT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 229 SNMVCKHCEHQSPVRFdTFDSLSLSIPAATWGhPLTLDHCLHHFISSESVRD---VVCDNCTKieARgtltgekvehqrs 305
Cdd:cd02667 79 STIMCESCGTVSLVYE-PFLDLSLPRSDEIKS-ECSIESCLKQFTEVEILEGnnkFACENCTK--AK------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 306 tfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDFYKYRllghKPSQHGPKATENPgsapevqdaqaa 385
Cdd:cd02667 142 ---KQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEIL--DLAPFC----DPKCNSSEDKSSV------------ 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 386 pkpglsqpgapktqiflngacspsllpalpspvafplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYRR-------- 457
Cdd:cd02667 201 ------------------------------------------------LYRLYGVVEHSGTMRSGHYVAYVKvrppqqrl 232
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2458602108 458 -----SPPSAKNPLSTSNQWLWISDDTVRKASLQEVLSSSAYLLFYE 499
Cdd:cd02667 233 sdltkSKPAADEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
69-498 |
9.25e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 113.62 E-value: 9.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSACPAFVK-WLEEFTTQYSRDQQGPHTHQCLSLTLLnllkalscQEVTEDEVLDASCLLDVL 147
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNyFLSDRHSCTCLSCSPNSCLSCAMDEIF--------QEFYYSGDRSPYGPINLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 148 rMYRWQIS----SFEEQDAHELFHVITSSLEderdrqprvTHLFDVHSLEQSEMaprQVTCHTrgspHPTtnhwksqhpF 223
Cdd:cd02660 74 -YLSWKHSrnlaGYSQQDAHEFFQFLLDQLH---------THYGGDKNEANDES---HCNCII----HQT---------F 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 224 HGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIP----------AATWGHPLTLDHCLHHFISSESVRDVV--CDNCTkiea 291
Cdd:cd02660 128 SGSLQSSVTCQRCGGVS-TTVDPFLDLSLDIPnkstpswalgESGVSGTPTLSDCLDRFTRPEKLGDFAykCSGCG---- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 292 rgtltgekvEHQRSTfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDFYkyrllghkpsqhgpkate 371
Cdd:cd02660 203 ---------STQEAT--KQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELNMTPY------------------ 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 372 npgsapevqdaqaapkpglsqpgapktqiflngaCSPSLLPALPSPVafplpvvpdySSSTYLFRLMAVVVHHGDMHSGH 451
Cdd:cd02660 254 ----------------------------------TSSSIGDTQDSNS----------LDPDYTYDLFAVVVHKGTLDTGH 289
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2458602108 452 FVTYRRsppsaknplSTSNQWLWISDDTVRKASLQEVLSSSAYLLFY 498
Cdd:cd02660 290 YTAYCR---------QGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
69-499 |
9.70e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 99.67 E-value: 9.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSAcpafvkwleefttqysrdqqgphthqclsltllnllkalscqevtedevldasclldvlr 148
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 149 myrwqissfEEQDAHELFhvitsslederdrqprvTHLFD-VHSLeqsemaprqVTchtrgsphpttnhwksqHPFHGRL 227
Cdd:cd02674 21 ---------DQQDAQEFL-----------------LFLLDgLHSI---------IV-----------------DLFQGQL 48
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 228 TSNMVCKHCEHQSpVRFDTFDSLSLSIPAA-TWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEArgtltgekveHQRST 306
Cdd:cd02674 49 KSRLTCLTCGKTS-TTFEPFTYLSLPIPSGsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKK----------KRKAT 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 307 fvKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRHEHVQF--NEFLMMDFYKYRllghkpSQHGPKatenpgsapevqdaqa 384
Cdd:cd02674 118 --KKLTISRLPKVLIIHLKRFS-FSRGSTRKLTTPVTFplNDLDLTPYVDTR------SFTGPF---------------- 172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 385 apkpglsqpgapktqiflngacspsllpalpspvafplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYRRSPpsakn 464
Cdd:cd02674 173 -------------------------------------------------KYDLYAVVNHYGSLNGGHYTAYCKNN----- 198
|
410 420 430
....*....|....*....|....*....|....*
gi 2458602108 465 plsTSNQWLWISDDTVRKASLQEVLSSSAYLLFYE 499
Cdd:cd02674 199 ---ETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
68-498 |
7.05e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 96.19 E-value: 7.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 68 PGLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGPHTHQCLSLTLLNLLKALSCQEVTEDEVLDASCLLDVL 147
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 148 RMYRwqissfeEQDAHELFHVITSSLederdrqprvthlfdvhsleqsemaprQVTCHTRGSPHPTTNHWK-----SQHP 222
Cdd:cd02661 82 RIGR-------QEDAHEFLRYLLDAM---------------------------QKACLDRFKKLKAVDPSSqettlVQQI 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 223 FHGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNCTKieargtltgeK 299
Cdd:cd02661 128 FGGYLRSQVKCLNCKHVSN-TYDPFLDLSLDIKGAD-----SLEDALEQFTKPEQLDGenkYKCERCKK----------K 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 300 VEHQrstfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKrheHVQFNEFLMMdfykyrllghkpsqhgpkatenpgsapev 379
Cdd:cd02661 192 VKAS-----KQLTIHRAPNVLTIHLKRFSNFRGGKINK---QISFPETLDL----------------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 380 qdaqaapKPGLSQPGAPktqiflngacspsllpalpspvafplpvvpdysSSTYlfRLMAVVVHHG-DMHSGHFVTYRRS 458
Cdd:cd02661 235 -------SPYMSQPNDG---------------------------------PLKY--KLYAVLVHSGfSPHSGHYYCYVKS 272
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2458602108 459 PPsaknplstsNQWLWISDDTVRKASLQEVLSSSAYLLFY 498
Cdd:cd02661 273 SN---------GKWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
65-501 |
6.18e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 81.92 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 65 GLVpGLVNLGNTCFMNSLLQGLSACPAFVKWLEE-FTTQYSRDQQG-PHTHQclsltllnllkALSCQEVTEDEVLDASC 142
Cdd:cd02659 1 GYV-GLKNQGATCYMNSLLQQLYMTPEFRNAVYSiPPTEDDDDNKSvPLALQ-----------RLFLFLQLSESPVKTTE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 143 LLDVLRMYRWQ-ISSFEEQDAHELFHVitsslederdrqprvthLFDvhSLEQSemaprqvtchTRGSPHPTTnhwkSQH 221
Cdd:cd02659 69 LTDKTRSFGWDsLNTFEQHDVQEFFRV-----------------LFD--KLEEK----------LKGTGQEGL----IKN 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 222 PFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRDvvcDNCTKIEArgtlTGEKVE 301
Cdd:cd02659 116 LFGGKLVNYIICKECPHES-EREEYFLDLQVAVKGKK-----NLEESLDAYVQGETLEG---DNKYFCEK----CGKKVD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 302 HqrstfVKQLKLGKLPQCLCIHLQRLswsshgtplkrhehvQFNEFLMM-----DFYKYrllghkpsqhgpkatenpgsa 376
Cdd:cd02659 183 A-----EKGVCFKKLPPVLTLQLKRF---------------EFDFETMMrikinDRFEF--------------------- 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 377 PEVQDaqaapkpglsqpgapktqiflngacspsLLPALPSPVAFPLPVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYR 456
Cdd:cd02659 222 PLELD----------------------------MEPYTEKGLAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYI 273
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2458602108 457 RSppsaknplSTSNQWLWISDDTVRKASLQEVL----------------------SSSAYLLFYERV 501
Cdd:cd02659 274 KD--------RDDGKWYKFNDDVVTPFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFYERK 332
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
69-365 |
8.40e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 69.27 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGPHTH-QCLSLTLLNLLKALSCQEVTEDEVLDASCLLDVL 147
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPANDlNCQLIKLADGLLSGRYSKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 148 -RMYRWQI-------SSFEEQDAHELFhvitsslederdrqprvTHLFDVhsLEQSemaprqvtCHTRGSPHPTTNhwks 219
Cdd:cd02658 81 pSMFKALIgkghpefSTMRQQDALEFL-----------------LHLIDK--LDRE--------SFKNLGLNPNDL---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 220 qhpFHGRLTSNMVCKHCEHqspVRFDTFDS--LSLSIPAATWGH---------PLTLDHCLHHFISSESVRDVVCDNCTK 288
Cdd:cd02658 130 ---FKFMIEDRLECLSCKK---VKYTSELSeiLSLPVPKDEATEkeegelvyePVPLEDCLKAYFAPETIEDFCSTCKEK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 289 IEArgtltgekvehqrstfVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDFYKYRLLG---HK-PSQ 364
Cdd:cd02658 204 TTA----------------TKTTGFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL--GPGKYELIAfisHKgTSV 265
|
.
gi 2458602108 365 H 365
Cdd:cd02658 266 H 266
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
435-499 |
1.28e-09 |
|
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: 58.69 E-value: 1.28e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2458602108 435 FRLMAVVVHHGDM-HSGHFVTYRRSppsaknpLSTSNQWLWISDDTVRKASLQEVL---SSSAYLLFYE 499
Cdd:cd02673 184 YSLVAVICHLGESpYDGHYIAYTKE-------LYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFYD 245
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
69-499 |
9.71e-09 |
|
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: 56.55 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSAcpafvkwleEFTTQYSRDqqgphTHQCLsltllnllkalSCQEVTEDeVLDASCLLDVLR 148
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF---------ENLLTCLKD-----LFESI-----------SEQKKRTG-VISPKKFITRLK 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 149 MYRWQISSFEEQDAHELFHV----ITSSLEDERdrqprvthlfdvhsleQSEMAPRQVTCHTRGSPHPTtnhWKSQHpFH 224
Cdd:cd02663 55 RENELFDNYMHQDAHEFLNFllneIAEILDAER----------------KAEKANRKLNNNNNAEPQPT---WVHEI-FQ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 225 GRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNC-TKIEARgtltgekv 300
Cdd:cd02663 115 GILTNETRCLTCETVSS-RDETFLDLSIDVEQNT-----SITSCLRQFSATETLCGrnkFYCDECcSLQEAE-------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 301 ehqrstfvKQLKLGKLPQCLCIHLQRlswsshgtpLKRHEHVQFNEFLmmdFYKyrllghkpsqhgpkatenpgsapevq 380
Cdd:cd02663 181 --------KRMKIKKLPKILALHLKR---------FKYDEQLNRYIKL---FYR-------------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 381 daqaapkpglsqpgapktqiflngacspsllpalpspVAFPL-----PVVPDYSSSTYLFRLMAVVVHHGD-MHSGHFVT 454
Cdd:cd02663 215 -------------------------------------VVFPLelrlfNTTDDAENPDRLYELVAVVVHIGGgPNHGHYVS 257
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2458602108 455 YRRsppsaknplsTSNQWLWISDDTVRK---ASLQEVL-----SSSAYLLFYE 499
Cdd:cd02663 258 IVK----------SHGGWLLFDDETVEKideNAVEEFFgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
69-499 |
4.64e-08 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239122 [Multi-domain] Cd Length: 305 Bit Score: 54.64 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGPHThqclsLTLLNLLKALSCQEVTedEVLDASCLLDVLR 148
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDN-----LTNALRDLFDTMDKKQ--EPVPPIEFLQLLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 149 MYRWQISSFEE------QDAHELFHVITSSLEderdrqprvthlfdvHSLEQSEMAPRQVTCHtrgsphpttnhwksqhp 222
Cdd:cd02657 74 MAFPQFAEKQNqggyaqQDAEECWSQLLSVLS---------------QKLPGAGSKGSFIDQL----------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 223 FHGRLTSNMVCKHCEHQSPVRFDTFDSLSLSIPAATwghpltldHCLHHFissesvrdvvcdncTKIEARGTLTGEK--- 299
Cdd:cd02657 122 FGIELETKMKCTESPDEEEVSTESEYKLQCHISITT--------EVNYLQ--------------DGLKKGLEEEIEKhsp 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 300 VEHQRSTFVKQLKLGKLPQCLCIHLQRLSW-SSHGTPLKRHEHVQFNefLMMDFYKYrllghkpsqhgpkatenpgsape 378
Cdd:cd02657 180 TLGRDAIYTKTSRISRLPKYLTVQFVRFFWkRDIQKKAKILRKVKFP--FELDLYEL----------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 379 vqdaqaapkpglsqpgapktqiflngaCSPSllpalpspvafplpvvpdyssstYLFRLMAVVVHHG-DMHSGHFVTYRR 457
Cdd:cd02657 235 ---------------------------CTPS-----------------------GYYELVAVITHQGrSADSGHYVAWVR 264
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2458602108 458 SPpsaknplsTSNQWLWISDDTVRKASLQEVL-------SSSAYLLFYE 499
Cdd:cd02657 265 RK--------NDGKWIKFDDDKVSEVTEEDILklsgggdWHIAYILLYK 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
263-500 |
2.32e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 53.73 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 263 LTLDHCLHHFISSESV---RDVVCDNCTkieargtltgekvEHQRSTfvKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRH 339
Cdd:COG5560 675 ITLQDCLNEFSKPEQLglsDSWYCPGCK-------------EFRQAS--KQMELWRLPMILIIHLKRFS-SVRSFRDKID 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 340 EHVQFneflmmdfykyrllghkpsqhgpkatenpgsapevqdaqaapkpglsqpgaPKTQIFLNGACSPSLLPALpspva 419
Cdd:COG5560 739 DLVEY---------------------------------------------------PIDDLDLSGVEYMVDDPRL----- 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 420 fplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYrrsppsAKNPlsTSNQWLWISDDTVRKASLQEVLSSSAYLLFYE 499
Cdd:COG5560 763 --------------IYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
.
gi 2458602108 500 R 500
Cdd:COG5560 821 R 821
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
69-359 |
9.85e-07 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 50.88 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGphthqclSLTLLNLLKALSCQEV---------TEDEVLD 139
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKN-------MPPDKPHEPQTIIDQLqlifaqlqfGNRSVVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 140 ASCLLDVLRmyrwqISSFEEQDAHELFHVITSSLEDERDRQPRVthlfdvhslEQSEMAPRQvtchtrgsphpttnhwks 219
Cdd:cd02668 74 PSGFVKALG-----LDTGQQQDAQEFSKLFLSLLEAKLSKSKNP---------DLKNIVQDL------------------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 220 qhpFHGRLTSNMVCKHCEHQSPVRfDTFDSLSLSIPaatwGHpLTLDHCLHHFISSESVRD---VVCDNCtkieargtlt 296
Cdd:cd02668 122 ---FRGEYSYVTQCSKCGRESSLP-SKFYELELQLK----GH-KTLEECIDEFLKEEQLTGdnqYFCESC---------- 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2458602108 297 GEKVEHQRSTfvkqlKLGKLPQCLCIHLQRLSWSSHGTPLKR-HEHVQFNEFLMMD---------FYKYRLLG 359
Cdd:cd02668 183 NSKTDATRRI-----RLTTLPPTLNFQLLRFVFDRKTGAKKKlNASISFPEILDMGeylaesdegSYVYELSG 250
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
69-264 |
6.87e-06 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 48.73 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSACPAFVKWleeFTTQYSRDQQGPHTHQCLSLTLLNLLKALSCQEVTEDEVLDASclldvlR 148
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTP------S 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 149 MYRWQISSF-------EEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQSEMAPRQVTCHTRGSPHPTTNH 216
Cdd:COG5560 338 GFKKTIGSFneefsgyDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDL 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2458602108 217 wksqhpFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 264
Cdd:COG5560 418 ------FQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
69-499 |
1.45e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 47.10 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 69 GLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGPHTHQCLSLTLLNLLKALScqEVTEDEVLDASclldvlr 148
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRA--EAPPDYFLEAS------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 149 myrwQISSF---EEQDAHELFHVITSSLederdrqprvthlfdvhsleqsemaprqvtchtrgspHPTTNHWksqhpFHG 225
Cdd:cd02664 72 ----RPPWFtpgSQQDCSEYLRYLLDRL-------------------------------------HTLIEKM-----FGG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 226 RLTSNMVCKHCeHQSPVRFDTFDSLSLSIPaatwghplTLDHCLHHFISSESV---RDVVCDNCTKIeargtltgEKVEh 302
Cdd:cd02664 106 KLSTTIRCLNC-NSTSARTERFRDLDLSFP--------SVQDLLNYFLSPEKLtgdNQYYCEKCASL--------QDAE- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 303 qrstfvKQLKLGKLPQCLCIHLQRLSWSShgtplKRHEHVQfneflMMDFYKYRLLGHKPSQHGPKATENPGSAPEVQDA 382
Cdd:cd02664 168 ------KEMKVTGAPEYLILTLLRFSYDQ-----KTHVREK-----IMDNVSINEVLSLPVRVESKSSESPLEKKEEESG 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 383 QAapkpglsqpgapktqiflnGACSPSLLPalpspvafplpvvpdyssstylFRLMAVVVHHG-DMHSGHFVTYRRSP-- 459
Cdd:cd02664 232 DD-------------------GELVTRQVH----------------------YRLYAVVVHSGySSESGHYFTYARDQtd 270
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2458602108 460 ----------PSAKNPLSTSNQWLWISDDTVRKASLQEVL-------SSSAYLLFYE 499
Cdd:cd02664 271 adstgqecpePKDAEENDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFYE 327
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
61-498 |
2.89e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 46.04 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 61 KRRKGLVP--GLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQgphtHQclsltllnlLKALSCQEVTEDEVL 138
Cdd:cd02671 16 EKRENLLPfvGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQ----LQ---------SSFLLNPEKYNDELA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 139 D--ASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDerdrqprvthLFdvhsleqSEMaprqvtchtrgsphpttnh 216
Cdd:cd02671 83 NqaPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE----------LV-------EKD------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 217 wksqhpFHGRLTSNMVCKHCEHQSPVRFDTFDslsLSIPAATWGHPL----------------TLDHCLHHFISSESVR- 279
Cdd:cd02671 127 ------FQGQLVLRTRCLECETFTERREDFQD---ISVPVQESELSKseesseispdpktemkTLKWAISQFASVERIVg 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 280 --DVVCDNCTKIeargtltgekVEHQRStfvkqLKLGKLPQCLCIHLQRLSWSShgtplkrhehvqfnefLMMDFYKyrl 357
Cdd:cd02671 198 edKYFCENCHHY----------TEAERS-----LLFDKLPEVITIHLKCFAANG----------------SEFDCYG--- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 358 lghkpsqhgpkatenpgsapevqdaqaapkpGLSQPGAPktqiflngacspsllpaLPSPVAFPLPVVPDySSSTYLFRL 437
Cdd:cd02671 244 -------------------------------GLSKVNTP-----------------LLTPLKLSLEEWST-KPKNDVYRL 274
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2458602108 438 MAVVVHHG-DMHSGHFVTYRRsppsaknplstsnqWLWISDDTVR---KASLQEVLS------SSAYLLFY 498
Cdd:cd02671 275 FAVVMHSGaTISSGHYTAYVR--------------WLLFDDSEVKvteEKDFLEALSpntsstSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
420-500 |
1.44e-04 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 43.64 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 420 FPLPVVPDYSSS---TYLFRLMAVVVHHGDMHSGHFVTYRRsppsaknplsTSNQWLWISDDTVRKASLQEVL---SSSA 493
Cdd:COG5533 207 FELPVKHDQILNivkETYYDLVGFVLHQGSLEGGHYIAYVK----------KGGKWEKANDSDVTPVSEEEAInekAKNA 276
|
....*..
gi 2458602108 494 YLLFYER 500
Cdd:COG5533 277 YLYFYER 283
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
430-489 |
3.31e-04 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 43.71 E-value: 3.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458602108 430 SSTYLFRLMAVVVHHGDMHSGHFVTYRRSppsaknplSTSNQWLWISDDTVRKASLQEVL 489
Cdd:COG5077 426 NSDAVYVLYGVLVHSGDLHEGHYYALLKP--------EKDGRWYKFDDTRVTRATEKEVL 477
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
69-86 |
5.32e-04 |
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Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 42.10 E-value: 5.32e-04
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| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
437-499 |
1.64e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 40.20 E-value: 1.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2458602108 437 LMAVVVHHG-DMHSGHFVTYRRSPPSAKNPLS---TSNQWLWISDDTVRKASLQEV------LSSSAYLLFYE 499
Cdd:cd02670 169 LCSAVCHRGtSLETGHYVAFVRYGSYSLTETDneaYNAQWVFFDDMADRDGVSNGFnipaarLLEDPYMLFYQ 241
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