|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
109-409 |
0e+00 |
|
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: 564.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 109 GAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQAHITQALSNPGDVIKPMFVINEMRRIARH 188
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 189 FRFGNQEDAHEFLQYTVDAMQKACLNGSNKL---DRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKA 265
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 266 AQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQ 345
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2072358257 346 PNGEPIIYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 409
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
110-408 |
1.19e-78 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 261.99 E-value: 1.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 110 AGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFC--MMCTMQAHITQALSN-PGDVIKPMFVINEMRRIA 186
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNsKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 187 RHFRFGNQEDAHEFLQYTVDAMQKAClngsnKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAA 266
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 267 QSV------NKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYPEYLD 338
Cdd:pfam00443 156 SAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2072358257 339 IRPYMSQPNGEP----IIYVLYAVLVHTGfNCHAGHYFCYIKA-SNGLWYQMNDSIVSTSD-IRSVLSQQAYVLFY 408
Cdd:pfam00443 236 LSRYLAEELKPKtnnlQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-409 |
1.36e-72 |
|
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: 245.36 E-value: 1.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEG--FCMMCTMqAHITQALSNPGDVIK--PMFVINEMRRIA 186
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSpnSCLSCAM-DEIFQEFYYSGDRSPygPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 187 RHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIK-- 264
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 265 ------AAQSVNKA-------LEQFVKPEQLdGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGG---KIA 328
Cdd:cd02660 161 stpswaLGESGVSGtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 329 KDVKYPEYLDIRPYMSQPNGEP---------IIYVLYAVLVHTGfNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVL 399
Cdd:cd02660 240 TYVQFPLELNMTPYTSSSIGDTqdsnsldpdYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318
|
330
....*....|
gi 2072358257 400 SQQAYVLFYI 409
Cdd:cd02660 319 KSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
111-409 |
7.08e-69 |
|
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: 231.99 E-value: 7.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLtytpplanymlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvinemrriarhfr 190
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 191 FGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI----KAA 266
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 267 QSVNKALEQFVKPEQLDGENSYKCSKCKKmVPASKRFTIHRSSNVLTLSLKRFA---NFTGGKIAKDVKYPEYLDIRPYM 343
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2072358257 344 SQP------NGEPIIYVLYAVLVHTGFNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVL-----SQQAYVLFYI 409
Cdd:cd02257 178 SEGekdsdsDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-409 |
1.78e-53 |
|
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: 186.72 E-value: 1.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLtytpplanymlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvinemrriarhfr 190
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 191 FGNQEDAHEFLQYTVDAMqkaclngsnkldrHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI------K 264
Cdd:cd02674 19 SADQQDAQEFLLFLLDGL-------------HS----IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdA 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 265 AAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFaNFTGG---KIAKDVKYP-EYLDIR 340
Cdd:cd02674 82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2072358257 341 PY-MSQPNGEPIIYVLYAVLVHTG-FNChaGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 409
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYGsLNG--GHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-411 |
5.50e-51 |
|
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: 183.61 E-value: 5.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPPLAN--YMLSHEHSKTCHAEGFCMMcTMQAHITQALSNPGDVIKPMfvinemrriARH 188
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNavYSIPPTEDDDDNKSVPLAL-QRLFLFLQLSESPVKTTELT---------DKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 189 FRFG-------NQEDAHEFLQYTVDAMQkaclNGSNKLDRHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITL 261
Cdd:cd02659 74 RSFGwdslntfEQHDVQEFFRVLFDKLE----EKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 262 EIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGGKIAKD---VKYPEYL 337
Cdd:cd02659 146 AVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDFETMMRIKIndrFEFPLEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 338 DIRPYMSQPNG-----------EPIIYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQ--- 402
Cdd:cd02659 226 DMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfgg 304
|
330 340
....*....|....*....|....*...
gi 2072358257 403 -------------------AYVLFYIRS 411
Cdd:cd02659 305 eetqktydsgprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-408 |
1.33e-50 |
|
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: 180.28 E-value: 1.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPPLANYMLShehsktchaegfcmmctmqahitqalsNPgdviKPMFviNEMRRIARHFR 190
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE---------------------------TP----KELF--SQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 191 FGNQEDAHEFLQYTVDAMQkaclngsnkldrhtqatTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITL----EIKAA 266
Cdd:cd02667 48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 267 QSVNKALEQFVKPEQLDGENSYKCSKCKKmvpASKRFTIHRSSNVLTLSLKRF-----ANFTggKIAKDVKYPEYLDIRP 341
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 342 YMSQPN-----GEPIIYVLYAVLVHTGfNCHAGHYFCYIKASN----------------------GLWYQMNDSIVSTSD 394
Cdd:cd02667 186 FCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 2072358257 395 IRSVLSQQAYVLFY 408
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-408 |
2.07e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 163.25 E-value: 2.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYtpplaNYMLshehskTCHAEGFCMMctmqahITQALSnpGDVIKPMFVINEMRRIARHFR 190
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLL------TCLKDLFESI------SEQKKR--TGVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 191 FGNQEDAHEFLQY-------TVDAMQKACL---NGSNKLDRHTQaTTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDIT 260
Cdd:cd02663 62 NYMHQDAHEFLNFllneiaeILDAERKAEKanrKLNNNNNAEPQ-PTWVHEIFQGILTNETRCLTCETVSSRDETFLDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 261 LEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFAnFTGG-----KIAKDVKYPE 335
Cdd:cd02663 141 IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFK-YDEQlnryiKLFYRVVFPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 336 YLdiRPYMSQPNGEP--IIYVLYAVLVHTGFNCHAGHYFCYIKaSNGLWYQMNDSIVSTSDIRSVL--------SQQAYV 405
Cdd:cd02663 220 EL--RLFNTTDDAENpdRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEeffgdspnQATAYV 296
|
...
gi 2072358257 406 LFY 408
Cdd:cd02663 297 LFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-408 |
2.23e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 152.57 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPPLANYMLShehsktchaegfcmmCTMQAHITQALSNPGDVIKPMFVINEMRRIARHFR 190
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 191 FGN-------------------QEDAHEFLQYTVDAMQkACLNGSNKLDrhtqATTLVCQIFGGYLRSRVKCLNCKGVSD 251
Cdd:cd02668 66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-AKLSKSKNPD----LKNIVQDLFRGEYSYVTQCSKCGRESS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 252 TFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFAnF---TGG--K 326
Cdd:cd02668 141 LPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV-FdrkTGAkkK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 327 IAKDVKYPEYLDIRPYMSQPNGEPIIYVLYAVLVHTGFNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVL------ 399
Cdd:cd02668 220 LNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMPGKPLKlgnsed 299
|
330 340
....*....|....*....|....
gi 2072358257 400 ---------------SQQAYVLFY 408
Cdd:cd02668 300 pakprkseikkgthsSRTAYMLVY 323
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-408 |
1.80e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 138.39 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKT--CHAEGFCM-MCTMQAHITQALSNPgdviKPMFVINEMRriAR 187
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLgdSQSVMKKLqLLQAHLMHTQRRAEA----PPDYFLEASR--PP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 188 HFRFGNQEDAHEFLQYTVDamqkaclngsnKLDrhtqatTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLeikAAQ 267
Cdd:cd02664 75 WFTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SFP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 268 SVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGG---KIAKDVKYPEYLD--IRP 341
Cdd:cd02664 135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSlpVRV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 342 YMS----------QPNGE-------PIIYVLYAVLVHTGFNCHAGHYFCYI---------------------KASNGLWY 383
Cdd:cd02664 215 ESKssesplekkeEESGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWY 294
|
330 340 350
....*....|....*....|....*....|..
gi 2072358257 384 QMNDSIVS---TSDIRSVLS----QQAYVLFY 408
Cdd:cd02664 295 LFNDSRVTfssFESVQNVTSrfpkDTPYILFY 326
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-408 |
2.53e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 113.96 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEG--FCMMCTMqAHITQAL-----SNPGDV----------I 173
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQL-IKLADGLlsgrySKPASLksendpyqvgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 174 KP-MF--VI---NEMrriarhFRFGNQEDAHEFLQYTVDAMQKACLNgsnkldRHTQATTlvcQIFGGYLRSRVKCLNCK 247
Cdd:cd02658 80 KPsMFkaLIgkgHPE------FSTMRQQDALEFLLHLIDKLDRESFK------NLGLNPN---DLFKFMIEDRLECLSCK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 248 GVSDTFD---------PYLDIT-----LEIKAAQSVNKALEQFVKPEQLDgensYKCSKCKKMVPASKRFTIHRSSNVLT 313
Cdd:cd02658 145 KVKYTSElseilslpvPKDEATekeegELVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 314 LSLKRFA---NFTGGKIAKDVKYPEYLDIRPYMsqpngepiiyvLYAVLVHTGFNCHAGHYFCYIK---ASNGLWYQMND 387
Cdd:cd02658 221 INMKRFQlleNWVPKKLDVPIDVPEELGPGKYE-----------LIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFND 289
|
330 340
....*....|....*....|.
gi 2072358257 388 SIVSTSDIRSVLSQQAYVLFY 408
Cdd:cd02658 290 EKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
110-408 |
4.19e-26 |
|
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: 110.75 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 110 AGLQNLGNTCFANAALQCLTYTPPLAN---YMLSHEHSKTCHAEGFCMMCTM--QAHITQAlsnpgdvikPMFVINEMRR 184
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSFLLNPEKynDELANQA---------PRRLLNALRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 185 IARHFRFGNQEDAHEFLQYTVDAMQKaclngsnkldrhtqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDIT---- 260
Cdd:cd02671 96 VNPMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISvpvq 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 261 ------------------LEIKAAQsvnKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-- 320
Cdd:cd02671 159 eselskseesseispdpkTEMKTLK---WAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAan 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 321 ----NFTGG--KIAKDVKYPEYLDIRPYMSQPNGEpiIYVLYAVLVHTGFNCHAGHYFCYIKasnglWYQMNDS---IVS 391
Cdd:cd02671 236 gsefDCYGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSevkVTE 308
|
330 340
....*....|....*....|...
gi 2072358257 392 TSDIRSVLSQQA------YVLFY 408
Cdd:cd02671 309 EKDFLEALSPNTsststpYLLFY 331
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
111-410 |
7.69e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 112.66 E-value: 7.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPPLAN--YMLSHEHSKTCHAEGFCMM-CTMQahiTQALSNPGDVIKpmFVINEMRRIAR 187
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSVALALQrLFYN---LQTGEEPVDTTE--LTRSFGWDSDD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 188 HFrfgNQEDAHEFLQYTVDAMQKAClngsnkldRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQ 267
Cdd:COG5077 270 SF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 268 SVNKALEQFVKPEQLDGENSYKCSKcKKMVPASKRFTIHRSSNVLTLSLKRF-ANFTGG---KIAKDVKYPEYLDIRPYM 343
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 344 S----QPNGEPIIYVLYAVLVHTGfNCHAGHYFCYIKAS-NGLWYQMNDSIVSTSDIRSVLSQ----------------- 401
Cdd:COG5077 418 DrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsg 496
|
330
....*....|....
gi 2072358257 402 -----QAYVLFYIR 410
Cdd:COG5077 497 ikrfmSAYMLVYLR 510
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
111-410 |
1.26e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 102.57 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLT-YTPPLANYM---------LSHEHSKTCHAEGFCMMctmqahiTQALSNpgdvikpmFVIN 180
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRKPEPDLNQEEA-------LKLFTA--------LWSS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 181 EMRRIARHFRFGNQEDAHEFLQYTVDAMqkaclngsnKLDRHTQATTLVCQIFGGYLRSrvkclnckgvsdTFDPYLDIT 260
Cdd:COG5533 66 KEHKVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKT------------STGDWFDII 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 261 LEIKAAQSVN--KALEQFVKP--EQLD-------GENSYKCSKCKKMVPASKRftihRSSNVLTLSLKRFANFTGG-KIA 328
Cdd:COG5533 125 IELPDQTWVNnlKTLQEFIDNmeELVDdetgvkaKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKID 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 329 KDVKYPEYLDIRPYMSQPNGEPIIYVLYAVLVHTGfNCHAGHYFCYIKaSNGLWYQMNDSIVST---SDIRSVLSQQAYV 405
Cdd:COG5533 201 TEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPvseEEAINEKAKNAYL 278
|
....*
gi 2072358257 406 LFYIR 410
Cdd:COG5533 279 YFYER 283
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-408 |
2.19e-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 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: 102.41 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPP----LANYMLSHEHSktchaegfcmmctMQAHIT---------QALSNPGDVIKPMF 177
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPElrdaLKNYNPARRGA-------------NQSSDNltnalrdlfDTMDKKQEPVPPIE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 178 VINEMRriaRHF-RFGNQEDAHEFLQytvdamQKA--CLNG-----SNKLDRHTQATTLVCQIFGGYLRSRVKCL-NCKG 248
Cdd:cd02657 68 FLQLLR---MAFpQFAEKQNQGGYAQ------QDAeeCWSQllsvlSQKLPGAGSKGSFIDQLFGIELETKMKCTeSPDE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 249 VSDTFDP------YLDITLEIKAAQS-VNKALEQFVK--PEQLDGENSYkcskckkmvpaSKRFTIHRSSNVLTLSLKRF 319
Cdd:cd02657 139 EEVSTESeyklqcHISITTEVNYLQDgLKKGLEEEIEkhSPTLGRDAIY-----------TKTSRISRLPKYLTVQFVRF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 320 -----ANfTGGKIAKDVKYPEYLDIRPYMSqPNGepiIYVLYAVLVHTGFNCHAGHYFCYIKASN-GLWYQMND---SIV 390
Cdd:cd02657 208 fwkrdIQ-KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDdkvSEV 282
|
330 340
....*....|....*....|...
gi 2072358257 391 STSDIRSvLS-----QQAYVLFY 408
Cdd:cd02657 283 TEEDILK-LSgggdwHIAYILLY 304
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-408 |
3.03e-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: 97.05 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPPLANYmlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvINemrriarhfR 190
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-----------------------------------------LE---------E 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 191 FGNQEDAHEFLQYTVDAMQKACLNgsnkldrhtqattlvcqIFGGYLRSRVKCLNCKGVS-DTFDPYLDITLEIKAAQSV 269
Cdd:cd02662 31 FLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQSSG 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 270 NKA-----LEQFVKPEQLDGensYKCSKCK-KMVPASKRFTIH--RSS-NVLTLSLKRFANftggkiakdVKYPEYLDIR 340
Cdd:cd02662 94 SGTtlehcLDDFLSTEIIDD---YKCDRCQtVIVRLPQILCIHlsRSVfDGRGTSTKNSCK---------VSFPERLPKV 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 341 pymsqpngepiIYVLYAVLVHTGFnCHAGHYFCY--------------------IKASNGL-WYQMNDSIVSTSDIRSVL 399
Cdd:cd02662 162 -----------LYRLRAVVVHYGS-HSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHpWWRISDTTVKEVSESEVL 229
|
330
....*....|
gi 2072358257 400 SQ-QAYVLFY 408
Cdd:cd02662 230 EQkSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
268-412 |
8.19e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 99.19 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 268 SVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYP-EYLDIRPYMS 344
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2072358257 345 QPNGEPIIYVLYAVLVHTGFnCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYIRSH 412
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGG-LSGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
111-263 |
1.20e-14 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 79.16 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGfcmMCTMQAHITQALSnpgDVIKPMFVINEMRRIARHFR 190
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEN---PLGMHGSVASAYA---DLIKQLYDGNLHAFTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 191 F----------GN-QEDAHEFLQYTVDAMQKAcLN------------------------GSNKLDRHTQAT-TLVCQIFG 234
Cdd:COG5560 341 KtigsfneefsGYdQQDSQEFIAFLLDGLHED-LNriikkpytskpdlspgddvvvkkkAKECWWEHLKRNdSIITDLFQ 419
|
170 180
....*....|....*....|....*....
gi 2072358257 235 GYLRSRVKCLNCKGVSDTFDPYLDITLEI 263
Cdd:COG5560 420 GMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
110-390 |
1.16e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 73.46 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 110 AGLQNLGNTCFANAALQCLTYTPPLANYMLSH-------EHS-----------------KTCHAEGFCmmctmqahitQA 165
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHlateclkEHCllcelgflfdmlekakgKNCQASNFL----------RA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 166 LSNPGDViKPMFVINEMRRIARHFRFGNQEDA-HEFLqytvdaMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCL 244
Cdd:pfam13423 71 LSSIPEA-SALGLLDEDRETNSAISLSSLIQSfNRFL------LDQLSSEENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 245 NCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQ-----LDGENSYK--CSKCKKMVPASKRFTIHRSSNVLTLSlk 317
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYPRKPSSNNKKPPNQTFSSilkssLERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLN-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 318 rfANFTGGKIAKDVKYPEYL--DIRPYMS---QPNGEPIIYVLYAVLVHTGFNCHAGHYFCYIKASN--------GLWYQ 384
Cdd:pfam13423 222 --AALTNEEWRQLWKTPGWLppEIGLTLSddlQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYL 299
|
....*.
gi 2072358257 385 MNDSIV 390
Cdd:pfam13423 300 FNDFLV 305
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-387 |
4.19e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 70.04 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 111 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMqAHITQALSNPGD---VIKPMFVINE-MRRIA 186
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRL-SELIRKIWNPRNfkgHVSPHELLQAvSKVSK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 187 RHFRFGNQEDAHEFLQYTVDAMqKACLNGSNKldrhtQATTLVCQIFGGYLR--------------SRVKCLNCKGVSDT 252
Cdd:cd02669 200 KKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 253 FD-PYLDITLEIKAA---QSVNKA--LEQfVKPEQLdgENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRF--ANFTG 324
Cdd:cd02669 274 SVsPFLLLTLDLPPPplfKDGNEEniIPQ-VPLKQL--LKKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFskNNFFK 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2072358257 325 GKIAKDVKYP-EYLDIRPYMSQP---NGEPIIYVLYAVLVHTGFNCHAGHYFCYI-KASNGLWYQMND 387
Cdd:cd02669 351 EKNPTIVNFPiKNLDLSDYVHFDkpsLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQD 418
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-408 |
1.13e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 54.46 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 112 LQNLGNTCFANAALQcltytpplanymlshehsktchaegfcmmctmqahitqALSNPGDVIKpmfvinemrriarHFRF 191
Cdd:cd02673 2 LVNTGNSCYFNSTMQ--------------------------------------ALSSIGKINT-------------EFDN 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 192 GNQEDAHEFLQYTVDAMQKAC-LNGSNKLDRHTQATTL-VCQIFGGYLRSRVKCLNCKGVSDTFDpyLDITLEIKAAQSV 269
Cdd:cd02673 31 DDQQDAHEFLLTLLEAIDDIMqVNRTNVPPSNIEIKRLnPLEAFKYTIESSYVCIGCSFEENVSD--VGNFLDVSMIDNK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 270 NKALEQFVKPEQLDGENSYKCSKCK-KMVPASKRFTihRSSNVLTLSLKRFANFTGgkIAKDVKypeylDIRPYMSQPNG 348
Cdd:cd02673 109 LDIDELLISNFKTWSPIEKDCSSCKcESAISSERIM--TFPECLSINLKRYKLRIA--TSDYLK-----KNEEIMKKYCG 179
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2072358257 349 EPIIYVLYAVLVHTGFNCHAGHYFCYIKAS--NGLWYQMNDSI---VSTSDIRSVLSQQAYVLFY 408
Cdd:cd02673 180 TDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEirpVSKNDVSTNARSSGYLIFY 244
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
831-1059 |
5.70e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 50.67 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 831 GPPGVPRTPPHEAARRAESPAAEAGEKRSPAPPAPSEDGAEPALRVHLRRDWGEAAEEPPAPPAPDRTAAAPADGGARRG 910
Cdd:PRK12678 62 GAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 911 PPGDEGDAGIPARDKADGLGGLRRAERGHCRDRSHCRDRSRRDRDRDRDRDARDPGRSGDRGRSGSGDRGERLRDSRGGS 990
Cdd:PRK12678 142 ARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRR 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 991 AAHGPHRHGRRRSYGREHCAGSPRPPGHSHGHGGPEPRG-PGRYGHHRPRSRSRSGPEQDWGRHRRAESE 1059
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGrRGRRFRDRDRRGRRGGDGGNEREPELREDD 291
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
110-391 |
7.62e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 49.80 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 110 AGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGfcmMCTMQAHITQALSNpGDVIKPMFVINEMRRIARHF 189
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASD---YPTERRIGGREVSR-SELQRSNQFVYELRSLFNDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 190 RFGN----------------QEDAHEFLQYTVDAMQKACLNGSN-----KLDRHTQATTLVCQIF-GGYLRSRVKCLNCK 247
Cdd:cd02666 78 IHSNtrsvtpskelaylalrQQDVTECIDNVLFQLEVALEPISNafagpDTEDDKEQSDLIKRLFsGKTKQQLVPESMGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 248 GVSD---------TFDPYLDITLEIKA---AQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASK------RFTIHRSS 309
Cdd:cd02666 158 QPSVrtkterflsLLVDVGKKGREIVVllePKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRelismdRYELPSSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 310 NVlTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGE-PIIYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMND 387
Cdd:cd02666 238 DD-IDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLkSYGYRLHAVFIHRG-EASSGHYWVYIKdFEENVWRKYND 315
|
....
gi 2072358257 388 SIVS 391
Cdd:cd02666 316 ETVT 319
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
777-1121 |
1.12e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.17 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 777 APPLADPGGVTSTKEGGPAADPAAPGEDGDRDGDRDEDGDRDKDETlPRIHAPCGPPGVPRTPPHEAARRAESPAAEAGE 856
Cdd:PHA03307 102 REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPP-PAASPPAAGASPAAVASDAASSRQAALPLSSPE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 857 KRSPAPPAPSEDGAEPALRVHLRRDwgEAAEEPPAPPAPDRTAAAPADGGARRGPPGDEGDAGIPARDKADGlgglrraE 936
Cdd:PHA03307 181 ETARAPSSPPAEPPPSTPPAAASPR--PPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWG-------P 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 937 RGHCRDRSHCRDRSRRDRDRDRDRDARDPGRSGDRGRSGSGDRGERLRDSRGGSAAH-GPHRHGRRRSYGREHCAGSPRP 1015
Cdd:PHA03307 252 ENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPApSSPRASSSSSSSRESSSSSTSS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 1016 PGH-SHGHGGPEPRGPGRYGH-HRPRSRSRSGPEQDWGRHRRAESELARAREDFHPGRLRWDRG--YRHRFAPYAAREHW 1091
Cdd:PHA03307 332 SSEsSRGAAVSPGPSPSRSPSpSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAgrARRRDATGRFPAGR 411
|
330 340 350
....*....|....*....|....*....|....*...
gi 2072358257 1092 ASARPRDCYWAQARGLDRPRDTTP--------PPGPDG 1121
Cdd:PHA03307 412 PRPSPLDAGAASGAFYARYPLLTPsgepwpgsPPPPPG 449
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
311-409 |
2.86e-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: 43.70 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 311 VLTLSLKRFA--NFTGGKIAKDVKYPEYLDIRPYMsqpngepiiyvLYAVLVHTGfNCHAGHYFCYI-KASNGLWYQMND 387
Cdd:cd02665 131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYND 198
|
90 100 110
....*....|....*....|....*....|
gi 2072358257 388 SIVSTSDIRSVLSQ--------QAYVLFYI 409
Cdd:cd02665 199 ISVTESSWEEVERDsfgggrnpSAYCLMYI 228
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
781-1002 |
1.05e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 781 ADPGGVTSTKEGGPAADPAAPGEDGDRDGDRDEDGDRDKDETLPRIHAPCGPPGVPRTPPHEAARRAESPAAEAGEKRSP 860
Cdd:PRK12678 63 AAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 861 APPAPSEDGAEPALRvhlrRDWGEAAEEPPAPPAPDRTAAAPADGGARRGPPGDEGDAGIPARDKADGLGGLR------- 933
Cdd:PRK12678 143 RKAGEGGEQPATEAR----ADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQgdrreer 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 934 -RAERGHCRDRSHCRDRSRRDRDRDRDRDARDPGRSGDRGRSGSGDRGERLRDSRGGSAAHGPHRHGRRR 1002
Cdd:PRK12678 219 gRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGNEREPELR 288
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
110-297 |
1.20e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 42.11 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 110 AGLQNLGNTCFANAALQCLTYTPPLANYMLsheHSKTCHAEGFCMMC-------TMQAHITQALSN--PGDVIKPMFVIN 180
Cdd:cd02672 16 AGLENHITNSYCNSLLQLLYFIPPFRNFTA---IILVACPKESCLLCelgylfsTLIQNFTRFLLEtiSQDQLGTPFSCG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072358257 181 EMRR-------IARHFRFGNQEDAHEFLQytvdamqkaCLNGSNKLDRHTQATTLVCQifggYLRSRVKCLNCKGVSDTF 253
Cdd:cd02672 93 TSRNsvsllytLSLPLGSTKTSKESTFLQ---------LLKRSLDLEKVTKAWCDTCC----KYQPLEQTTSIRHLPDIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2072358257 254 DPYLDITLEiKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMV 297
Cdd:cd02672 160 LLVLVINLS-VTNGEFDDINVVLPSGKVMQNKVSPKAIDHDKLV 202
|
|
| |
