|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
80-538 |
9.48e-72 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 240.04 E-value: 9.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 80 VGLQNIANTCYMNSALQALSNLPPMTHYFINCSDLVEYIAEQsarrcKPGGLAKSYRRLMQEIWQDVddPKEFIAPRGIL 159
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYN-----KDINLLCALRDLFKALQKNS--KSSSVSPKMFK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 160 YGIRTVHPMFRGYQQHDTQEFLRCFMDQLHEELteqvsmlpqtqnqpqyqslqqqqpsetddenddeaapaslshasese 239
Cdd:pfam00443 74 KSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL----------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 240 ydtcessmsersaevllkteyfvtpcrtngsnsglpeghsvqlqqaplqhqqknassaEQKPIEAARSIISDVFDGKLLS 319
Cdd:pfam00443 107 ----------------------------------------------------------NGNHSTENESLITDLFRGQLKS 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 320 SVQCLTCDRVSTREETFQDLSLPIPNRDFLNVLHQthslsvqslnaaetsartnegwlswmwnmlrswiygpsvtLYDCM 399
Cdd:pfam00443 129 RLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTAS----------------------------------------LQICF 168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 400 ASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLSYSSKISSDVYFPLEgFDMRPYIHKDCKS- 478
Cdd:pfam00443 169 LQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPk 247
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22026877 479 --EVAIYNLSSVICHHGTVGGGHYTCFARNTLNGKWYEFDDQFVTEVSSEL-VQSCQAYVLFY 538
Cdd:pfam00443 248 tnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
307-538 |
1.59e-60 |
|
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: 205.98 E-value: 1.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 307 SIISDVFDGKLLSSVQCLTCDRVSTREETFQDLSLPIPNRDflnvlhqthslsvqslnaaetsartnegwlswmwnmlrs 386
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGS--------------------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 387 wIYGPSVTLYDCMASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLSYSSKISSDVYFPLEGF 466
Cdd:cd02674 79 -GDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22026877 467 DMRPYIHKDCKSEVAIYNLSSVICHHGTVGGGHYTCFARNTLNGKWYEFDDQFVTEVSSELVQSCQAYVLFY 538
Cdd:cd02674 158 DLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
78-542 |
2.26e-40 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 160.82 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 78 GLVGLQNIANTCYMNSALQALSNLPPMTHYFIncSDlvEYiaEQSARRCKP----GGLAKSYRRLMQEIWqdvDDPKEFI 153
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL--SD--EY--EESINEENPlgmhGSVASAYADLIKQLY---DGNLHAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 154 APRGILYGIRTVHPMFRGYQQHDTQEFLRCFMDQLHEELTeQVSMLPQTQNQPQYQSLQQQQPSETDD-------END-- 224
Cdd:COG5560 335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLN-RIIKKPYTSKPDLSPGDDVVVKKKAKEcwwehlkRNDsi 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 225 -------------------------DEAAPASLSHASESEYD---------------TCESSMSE--RSAEVLLKTEYFV 262
Cdd:COG5560 414 itdlfqgmykstltcpgcgsvsitfDPFMDLTLPLPVSMVWKhtivvfpesgrrqplKIELDASStiRGLKKLVDAEYGK 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 263 TPCRTNGSNSGLPEGHSVQLQQAPLQHQQK----------------------------------------------NASS 296
Cdd:COG5560 494 LGCFEIKVMCIYYGGNYNMLEPADKVLLQDipqtdfvylyetndngievpvvhlriekgykskrlfgdpflqlnvlIKAS 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 297 AEQKPIEAARSIISDVFDGKL---LSSVQcLTCDRVSTREETFQDLSLPIPNRDFLNVLHQTH-SLSVQSLNAAETSART 372
Cdd:COG5560 574 IYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQmNFNDAVVISCEWEEKR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 373 NEGWLSW--MWNMLRSWIYGPSVTLYDCMASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLS 450
Cdd:COG5560 653 YLSLFSYdpLWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRS 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 451 YSSKISSDVYFPLEGFDMRPYIHKDCKSEVaIYNLSSVICHHGTVGGGHYTCFARNTLNGKWYEFDDQFVTEVSSELVQS 530
Cdd:COG5560 733 FRDKIDDLVEYPIDDLDLSGVEYMVDDPRL-IYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT 811
|
570
....*....|..
gi 22026877 531 CQAYVLFYHKHN 542
Cdd:COG5560 812 SSAYVLFYRRKS 823
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
667-755 |
6.01e-28 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 107.83 E-value: 6.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 667 NEFDSTAIYAIAMPWLRSWQQFSRGKTHKDPGPITNEGIAAPtENGSATVSCVRLGSDYAQLNARLWRFLHNIYGGGPEI 746
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCS-HGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPGP 79
|
....*....
gi 22026877 747 ILRQALSDE 755
Cdd:smart00695 80 IPRKVVCQG 88
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
560-643 |
1.99e-25 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 100.90 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 560 PLCDSDIQFYITREWLSRLATFSE------PGPINNQEMLCPHGGILHSKADVISQIAVPISQPLWDYLYRTFGGGPAvn 633
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
90
....*....|
gi 22026877 634 IIFECEICKR 643
Cdd:smart00695 79 PIPRKVVCQG 88
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
674-749 |
1.69e-16 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 75.10 E-value: 1.69e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22026877 674 IYAIAMPWLRSWQQFSRGKThKDPGPITNEGIAAPTENGSATVScVRLGSDYAQLNARLWRFLHNIYGGGPEIILR 749
Cdd:pfam06337 4 VYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLKPN-LQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
564-638 |
3.28e-09 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 54.30 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 564 SDIQFYITREWLSRLATF-----SEPGPINNQEMLC--PHGGILHSKADVISQIAVPisQPLWDYLYRTFGGGPAVNIIF 636
Cdd:pfam06337 1 GDKVYLISSKWLNKWKSYvkepnNEPGPIDNSDLLDdeSNGQLKPNLQEGVDYVIVP--EEVWEFLVEWYGGGPEIKRNV 78
|
..
gi 22026877 637 EC 638
Cdd:pfam06337 79 VN 80
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
80-538 |
9.48e-72 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 240.04 E-value: 9.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 80 VGLQNIANTCYMNSALQALSNLPPMTHYFINCSDLVEYIAEQsarrcKPGGLAKSYRRLMQEIWQDVddPKEFIAPRGIL 159
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYN-----KDINLLCALRDLFKALQKNS--KSSSVSPKMFK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 160 YGIRTVHPMFRGYQQHDTQEFLRCFMDQLHEELteqvsmlpqtqnqpqyqslqqqqpsetddenddeaapaslshasese 239
Cdd:pfam00443 74 KSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL----------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 240 ydtcessmsersaevllkteyfvtpcrtngsnsglpeghsvqlqqaplqhqqknassaEQKPIEAARSIISDVFDGKLLS 319
Cdd:pfam00443 107 ----------------------------------------------------------NGNHSTENESLITDLFRGQLKS 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 320 SVQCLTCDRVSTREETFQDLSLPIPNRDFLNVLHQthslsvqslnaaetsartnegwlswmwnmlrswiygpsvtLYDCM 399
Cdd:pfam00443 129 RLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTAS----------------------------------------LQICF 168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 400 ASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLSYSSKISSDVYFPLEgFDMRPYIHKDCKS- 478
Cdd:pfam00443 169 LQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPk 247
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22026877 479 --EVAIYNLSSVICHHGTVGGGHYTCFARNTLNGKWYEFDDQFVTEVSSEL-VQSCQAYVLFY 538
Cdd:pfam00443 248 tnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
307-538 |
1.59e-60 |
|
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: 205.98 E-value: 1.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 307 SIISDVFDGKLLSSVQCLTCDRVSTREETFQDLSLPIPNRDflnvlhqthslsvqslnaaetsartnegwlswmwnmlrs 386
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGS--------------------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 387 wIYGPSVTLYDCMASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLSYSSKISSDVYFPLEGF 466
Cdd:cd02674 79 -GDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22026877 467 DMRPYIHKDCKSEVAIYNLSSVICHHGTVGGGHYTCFARNTLNGKWYEFDDQFVTEVSSELVQSCQAYVLFY 538
Cdd:cd02674 158 DLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
81-538 |
8.07e-53 |
|
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: 185.38 E-value: 8.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 81 GLQNIANTCYMNSALQALSNlppmthyfincsdlveyiaeqsarrckpgglaksyrrlmqeiwqdvddpkefiaprgily 160
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 161 girtvhpmfrgyQQHDTQEFLRCFMDQLHEELteqvsmlpqtqnqpqyqslqqqqpsetddenddeaapaslshasesey 240
Cdd:cd02257 21 ------------EQQDAHEFLLFLLDKLHEEL------------------------------------------------ 40
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 241 dtcessmsersaevllkteyfvtpcrtngsnsglpeghsvqlqqaplqhqqkNASSAEQKPIEAARSIISDVFDGKLLSS 320
Cdd:cd02257 41 ----------------------------------------------------KKSSKRTSDSSSLKSLIHDLFGGKLEST 68
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 321 VQCLTCDRVSTREETFQDLSLPIPNRDflnvlhqthslsvqslnaaetsartnegwlswmwnmlrswiyGPSVTLYDCMA 400
Cdd:cd02257 69 IVCLECGHESVSTEPELFLSLPLPVKG------------------------------------------LPQVSLEDCLE 106
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 401 SFFSADELKGDNMYSCERCnKLRTGIKYSRVLTLPEVLCIHLKRF-RNDLSYSSKISSDVYFPLEgFDMRPYIHKDCKSE 479
Cdd:cd02257 107 KFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFsFNEDGTKEKLNTKVSFPLE-LDLSPYLSEGEKDS 184
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 480 VA-----IYNLSSVICHHGT-VGGGHYTCFARNTLNGKWYEFDDQFVTEVSSELVQ-----SCQAYVLFY 538
Cdd:cd02257 185 DSdngsyKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-538 |
1.39e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 180.55 E-value: 1.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 81 GLQNIANTCYMNSALQALSNLPPmthyfincsdLVEYIAEQSARRCKPGGLAKSYRRLMQEIWQDVDDPKEFIAPRGILY 160
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPP----------LANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 161 GIRTVHPMFRGYQQHDTQEFLRCFMDQLHeelteqvsmlpqtqnqpqyqslqqqqpsetddenddeaapaslshasesey 240
Cdd:cd02661 73 NLKQISKHFRIGRQEDAHEFLRYLLDAMQ--------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 241 dtcessmsersaevllkteyfvtpcrtngsNSGLPeghsvqlqqaplqhqqKNASSAEQKPIEAARSIISDVFDGKLLSS 320
Cdd:cd02661 102 ------------------------------KACLD----------------RFKKLKAVDPSSQETTLVQQIFGGYLRSQ 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 321 VQCLTCDRVSTREETFQDLSLPIPNrdflnvlhqthslsVQSLNaaetsartnegwlswmwnmlrswiygpsvtlyDCMA 400
Cdd:cd02661 136 VKCLNCKHVSNTYDPFLDLSLDIKG--------------ADSLE--------------------------------DALE 169
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 401 SFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDlsYSSKISSDVYFPLEgFDMRPYIhKDCKSEV 480
Cdd:cd02661 170 QFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF--RGGKINKQISFPET-LDLSPYM-SQPNDGP 245
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 22026877 481 AIYNLSSVICHHGT-VGGGHYTCFARnTLNGKWYEFDDQFVTEVSSELVQSCQAYVLFY 538
Cdd:cd02661 246 LKYKLYAVLVHSGFsPHSGHYYCYVK-SSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-539 |
5.06e-48 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 174.10 E-value: 5.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 81 GLQNIANTCYMNSALQALSNLPPMTHYFI----NCSDLVeyiaeQSARRCkpggLAKSyrrlMQEIWQDVD--DPKEFIA 154
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLsdrhSCTCLS-----CSPNSC----LSCA----MDEIFQEFYysGDRSPYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 155 PRGILYGIRTVHPMFRGYQQHDTQEFLRCFMDQLHEELTeqvsmlpqtqnqpqyqslqqqqpsetddenDDEAAPASLSH 234
Cdd:cd02660 69 PINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYG------------------------------GDKNEANDESH 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 235 aseseydtCessmsersaevllkteyfvtPCrtngsnsglpeghsvqlqqaplqhqqknassaeqkpieaarsIISDVFD 314
Cdd:cd02660 119 --------C--------------------NC------------------------------------------IIHQTFS 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 315 GKLLSSVQCLTCDRVSTREETFQDLSLPIPNRdflnvlhQTHSLSVQSLNAAETSartnegwlswmwnmlrswiygpsvT 394
Cdd:cd02660 129 GSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNK-------STPSWALGESGVSGTP------------------------T 177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 395 LYDCMASFFSADELkGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDL-SYSSKISSDVYFPLEgFDMRPYIH 473
Cdd:cd02660 178 LSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLnKTSRKIDTYVQFPLE-LNMTPYTS 255
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22026877 474 --------KDCKSEVAIYNLSSVICHHGTVGGGHYTCFARNTlNGKWYEFDDQFVTEVSSELVQSCQAYVLFYH 539
Cdd:cd02660 256 ssigdtqdSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-543 |
4.00e-41 |
|
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: 154.34 E-value: 4.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 78 GLVGLQNIANTCYMNSALQALSnlppMTHYFINcsDLVEYIAEQSARRCKPGGLAksYRRL---MQEIWQDVDDPKEFIA 154
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLY----MTPEFRN--AVYSIPPTEDDDDNKSVPLA--LQRLflfLQLSESPVKTTELTDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 155 PRGilYGIRTVHPMfrgyQQHDTQEFLRCFMDQLHEelteqvsMLPQTqnqpqyqslqqqqpsetddenddeaapaslsh 234
Cdd:cd02659 73 TRS--FGWDSLNTF----EQHDVQEFFRVLFDKLEE-------KLKGT-------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 235 aseseydtcessmsersaevllkteyfvtpcrtngsnsglpeghsvqlqqaplqhqqknassaEQKPIeaarsiISDVFD 314
Cdd:cd02659 108 ---------------------------------------------------------------GQEGL------IKNLFG 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 315 GKLLSSVQCLTCDRVSTREETFQDLSLPIPNRDflnvlhqthslsvqslnaaetsartnegwlswmwnmlrswiygpsvT 394
Cdd:cd02659 119 GKLVNYIICKECPHESEREEYFLDLQVAVKGKK----------------------------------------------N 152
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 395 LYDCMASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLSY--SSKISSDVYFPLEgFDMRPYI 472
Cdd:cd02659 153 LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETmmRIKINDRFEFPLE-LDMEPYT 231
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 473 HKDCK----------SEVAIYNLSSVICHHGTVGGGHYTCFARNTLNGKWYEFDDQFVTEVSSE---------------- 526
Cdd:cd02659 232 EKGLAkkegdsekkdSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNdaeeecfggeetqkty 311
|
490 500
....*....|....*....|...
gi 22026877 527 ------LVQSCQAYVLFYHKHNP 543
Cdd:cd02659 312 dsgpraFKRTTNAYMLFYERKSP 334
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
78-542 |
2.26e-40 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 160.82 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 78 GLVGLQNIANTCYMNSALQALSNLPPMTHYFIncSDlvEYiaEQSARRCKP----GGLAKSYRRLMQEIWqdvDDPKEFI 153
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL--SD--EY--EESINEENPlgmhGSVASAYADLIKQLY---DGNLHAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 154 APRGILYGIRTVHPMFRGYQQHDTQEFLRCFMDQLHEELTeQVSMLPQTQNQPQYQSLQQQQPSETDD-------END-- 224
Cdd:COG5560 335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLN-RIIKKPYTSKPDLSPGDDVVVKKKAKEcwwehlkRNDsi 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 225 -------------------------DEAAPASLSHASESEYD---------------TCESSMSE--RSAEVLLKTEYFV 262
Cdd:COG5560 414 itdlfqgmykstltcpgcgsvsitfDPFMDLTLPLPVSMVWKhtivvfpesgrrqplKIELDASStiRGLKKLVDAEYGK 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 263 TPCRTNGSNSGLPEGHSVQLQQAPLQHQQK----------------------------------------------NASS 296
Cdd:COG5560 494 LGCFEIKVMCIYYGGNYNMLEPADKVLLQDipqtdfvylyetndngievpvvhlriekgykskrlfgdpflqlnvlIKAS 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 297 AEQKPIEAARSIISDVFDGKL---LSSVQcLTCDRVSTREETFQDLSLPIPNRDFLNVLHQTH-SLSVQSLNAAETSART 372
Cdd:COG5560 574 IYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQmNFNDAVVISCEWEEKR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 373 NEGWLSW--MWNMLRSWIYGPSVTLYDCMASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLS 450
Cdd:COG5560 653 YLSLFSYdpLWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRS 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 451 YSSKISSDVYFPLEGFDMRPYIHKDCKSEVaIYNLSSVICHHGTVGGGHYTCFARNTLNGKWYEFDDQFVTEVSSELVQS 530
Cdd:COG5560 733 FRDKIDDLVEYPIDDLDLSGVEYMVDDPRL-IYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT 811
|
570
....*....|..
gi 22026877 531 CQAYVLFYHKHN 542
Cdd:COG5560 812 SSAYVLFYRRKS 823
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-538 |
1.66e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 128.20 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 81 GLQNIANTCYMNSALQALsnlppmthYFINC----SDLVEYIAEQSARrckpgglaksyrrlmqeiwQDVDDPKEFIAPr 156
Cdd:cd02663 1 GLENFGNTCYCNSVLQAL--------YFENLltclKDLFESISEQKKR-------------------TGVISPKKFITR- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 157 gilygIRTVHPMFRGYQQHDTQEFLRCFMDQLHEELteqvsmlpqtqnqpqyqslqqqqpsetDDENDDEAAPASLSHAS 236
Cdd:cd02663 53 -----LKRENELFDNYMHQDAHEFLNFLLNEIAEIL---------------------------DAERKAEKANRKLNNNN 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 237 ESEYDTcessmsersaevllkteyfvtpcrtngsnsglpeghsvqlqqaplqhqqknassaeqkpieaarSIISDVFDGK 316
Cdd:cd02663 101 NAEPQP----------------------------------------------------------------TWVHEIFQGI 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 317 LLSSVQCLTCDRVSTREETFQDLSLPIPNrdflnvlhqtHSlsvqslnaaetsartnegwlswmwnmlrswiygpSVTly 396
Cdd:cd02663 117 LTNETRCLTCETVSSRDETFLDLSIDVEQ----------NT----------------------------------SIT-- 150
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 397 DCMASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLSYS--SKISSDVYFPLEgfdMRPY-IH 473
Cdd:cd02663 151 SCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYRVVFPLE---LRLFnTT 227
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22026877 474 KDCKSEVAIYNLSSVICHHGtvGG---GHYTCFARNtlNGKWYEFDDQFVTEVSSELVQ--------SCQAYVLFY 538
Cdd:cd02663 228 DDAENPDRLYELVAVVVHIG--GGpnhGHYVSIVKS--HGGWLLFDDETVEKIDENAVEeffgdspnQATAYVLFY 299
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-538 |
1.60e-31 |
|
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: 124.81 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 81 GLQNIANTCYMNSALQALSNLPpmthyfincsdlveyiaeqsarrckpgglakSYRRLMQEiwqdvddpkefiAPRGILY 160
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTP-------------------------------ALRELLSE------------TPKELFS 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 161 GIRTVHPMFRGYQQHDTQEFLRCFMDQLheelteqvsmlpqtqnqpqyqslqqqqpsetddenddeaapaslshasesey 240
Cdd:cd02667 38 QVCRKAPQFKGYQQQDSHELLRYLLDGL---------------------------------------------------- 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 241 dtcessmsersaevllkteyfvtpcrtngsnsglpeghsvqlqqaplqhqqknassaeqkpieaaRSIISDVFDGKLLSS 320
Cdd:cd02667 66 -----------------------------------------------------------------RTFIDSIFGGELTST 80
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 321 VQCLTCDRVSTREETFQDLSLPIPNRDFlnvlhqthslsvqslnaaetsartnegwlswmwnmlrswiygPSVTLYDCMA 400
Cdd:cd02667 81 IMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------------SECSIESCLK 118
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 401 SFFSADELKGDNMYSCERCNKlrtGIKYSRVLTLPEVLCIHLKRFRNDLSYS-SKISSDVYFPlEGFDMRPYIHKDC--- 476
Cdd:cd02667 119 QFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANlRKVSRHVSFP-EILDLAPFCDPKCnss 194
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 477 -KSEVAIYNLSSVICHHGTVGGGHYTCFAR---------------------NTLNGKWYEFDDQFVTEVSSELVQSCQAY 534
Cdd:cd02667 195 eDKSSVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeaGPGSGQWYYISDSDVREVSLEEVLKSEAY 274
|
....
gi 22026877 535 VLFY 538
Cdd:cd02667 275 LLFY 278
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
667-755 |
6.01e-28 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 107.83 E-value: 6.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 667 NEFDSTAIYAIAMPWLRSWQQFSRGKTHKDPGPITNEGIAAPtENGSATVSCVRLGSDYAQLNARLWRFLHNIYGGGPEI 746
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCS-HGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPGP 79
|
....*....
gi 22026877 747 ILRQALSDE 755
Cdd:smart00695 80 IPRKVVCQG 88
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-522 |
1.49e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 111.74 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 282 LQQAPLQHQQKNAssaeqkpieaARSIISDVFDGKLLSSVQCLTCDRVSTREETFQDLSLPIpnrdflnvlhQTHSlsvq 361
Cdd:cd02668 101 LLEAKLSKSKNPD----------LKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----------KGHK---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 362 slnaaetsartnegwlswmwnmlrswiygpsvTLYDCMASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIH 441
Cdd:cd02668 157 --------------------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 442 LKRFRNDLSYSS--KISSDVYFPLEgFDMRPYIhKDCKSEVAIYNLSSVICHHGT-VGGGHYTCFARNTLNGKWYEFDDQ 518
Cdd:cd02668 205 LLRFVFDRKTGAkkKLNASISFPEI-LDMGEYL-AESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDE 282
|
....
gi 22026877 519 FVTE 522
Cdd:cd02668 283 DVEE 286
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
560-643 |
1.99e-25 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 100.90 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 560 PLCDSDIQFYITREWLSRLATFSE------PGPINNQEMLCPHGGILHSKADVISQIAVPISQPLWDYLYRTFGGGPAvn 633
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
90
....*....|
gi 22026877 634 IIFECEICKR 643
Cdd:smart00695 79 PIPRKVVCQG 88
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
71-538 |
2.59e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 108.06 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 71 TAKGSGTGLVGLQNIANTCYMNSALQALSNLPPMTHyfiNCSDLVEYIAEQSARrckpgglaKSYRRLMQEIWQDVDDPK 150
Cdd:cd02671 16 EKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKH---GLKHLVSLISSVEQL--------QSSFLLNPEKYNDELANQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 151 efiAPRGILYGIRTVHPMFRGYQQHDTQEFLRCFMDQLheelteqvsmlpqtqnqpqyqslqqqqpsetddenddeaapa 230
Cdd:cd02671 85 ---APRRLLNALREVNPMYEGYLQHDAQEVLQCILGNI------------------------------------------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 231 slshaseseydtcessmsersaevllkteyfvtpcrtngsnsglpeghsvqlqqaplqhqqknassaeqkpieaaRSIIS 310
Cdd:cd02671 120 ---------------------------------------------------------------------------QELVE 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 311 DVFDGKLLSSVQCLTCDRVSTREETFQDLSLPIPNRDFLNVlhqTHSLSVQSLNAAETSartnegwlswmwnmlrswiyg 390
Cdd:cd02671 125 KDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKS---EESSEISPDPKTEMK--------------------- 180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 391 psvTLYDCMASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLSYS------SKISSDVYFPL- 463
Cdd:cd02671 181 ---TLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPLk 257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 464 ---EGFDMRPYIHkdcksevaIYNLSSVICHHG-TVGGGHYTCFARntlngkWYEFDD---------QFVTEVSSELVQS 530
Cdd:cd02671 258 lslEEWSTKPKND--------VYRLFAVVMHSGaTISSGHYTAYVR------WLLFDDsevkvteekDFLEALSPNTSST 323
|
....*...
gi 22026877 531 CQAYVLFY 538
Cdd:cd02671 324 STPYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
290-538 |
4.04e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 99.36 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 290 QQKNASSAEQKPIEAARSIISDVFDGKLLSSVQCLTCDRVST-REETFQDLSLPIPNRdflnvlhqthslsvqslnaaet 368
Cdd:cd02662 33 EQQDAHELFQVLLETLEQLLKFPFDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQ---------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 369 sartnegwlSWMWNMlrswiygpsvTLYDCMASFFSADELKGdnmYSCERCnklRTGIKysrvlTLPEVLCIHLKRFRND 448
Cdd:cd02662 91 ---------SSGSGT----------TLEHCLDDFLSTEIIDD---YKCDRC---QTVIV-----RLPQILCIHLSRSVFD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 449 LSY-SSKISSDVYFPLEgfdMRPYIhkdcksevaiYNLSSVICHHGTVGGGHYTCFARNTLNGK---------------- 511
Cdd:cd02662 141 GRGtSTKNSCKVSFPER---LPKVL----------YRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpss 207
|
250 260 270
....*....|....*....|....*....|..
gi 22026877 512 ----WYEFDDQFVTEVS-SELVQSCQAYVLFY 538
Cdd:cd02662 208 tshpWWRISDTTVKEVSeSEVLEQKSAYMLFY 239
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
255-538 |
8.55e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 100.64 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 255 LLKTEYFV------TPCRTNGSNSglpEGHSVQLQQAPLQHQQKNASSAEQKPIEAAR---------------------- 306
Cdd:cd02664 18 LFMAKDFRrqvlslNLPRLGDSQS---VMKKLQLLQAHLMHTQRRAEAPPDYFLEASRppwftpgsqqdcseylrylldr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 307 --SIISDVFDGKLLSSVQCLTCDRVSTREETFQDLSLPIPnrdflnvlhqthslSVQSLnaaetsartnegwlswmwnml 384
Cdd:cd02664 95 lhTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP--------------SVQDL--------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 385 rswiygpsvtlydcMASFFSADELKGDNMYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLSYSS--KISSDVYFP 462
Cdd:cd02664 140 --------------LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVreKIMDNVSIN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 463 L-----------EGFDMRPYIHKDCKSEVAI------YNLSSVICHHGT-VGGGHYTCFARN------------------ 506
Cdd:cd02664 206 EvlslpvrveskSSESPLEKKEEESGDDGELvtrqvhYRLYAVVVHSGYsSESGHYFTYARDqtdadstgqecpepkdae 285
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 22026877 507 --TLNGKWYEFDDQFVTEVSSELVQSCQ-------AYVLFY 538
Cdd:cd02664 286 enDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFY 326
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-538 |
8.58e-20 |
|
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: 91.23 E-value: 8.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 81 GLQNIANTCYMNSALQALSNLPP--------MTHYFINCSDLVEYIAEQSARRCKpGGLAKSYRRLMqEIWQDVDDPKEF 152
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSfqwryddlENKFPSDVVDPANDLNCQLIKLAD-GLLSGRYSKPA-SLKSENDPYQVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 153 IAPRGILYGIRTVHPMFRGYQQHDTQEFLRCFMDQLheelteqvsmlpqtqnqpqyqslqqqqpsetddenddeaapasl 232
Cdd:cd02658 79 IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKL-------------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 233 shaseseydtcessmsERSAEVLLKTEyfvtpcrtngsnsglpeghsvqlqqaplqhqqknassaeqkpieaarsiISDV 312
Cdd:cd02658 115 ----------------DRESFKNLGLN-------------------------------------------------PNDL 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 313 FDGKLLSSVQCLTCDRVSTREETFQDLSLPIPNRDFLNVLHQTHSLsvqslnaaetsartnegwlswmwnmlrswiygPS 392
Cdd:cd02658 130 FKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGELVY--------------------------------EP 177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 393 VTLYDCMASFFSADELKgdnmYSCERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLSY-SSKISSDVYFPLEGFDMRpy 471
Cdd:cd02658 178 VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLDVPIDVPEELGPGK-- 251
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 472 ihkdcksevaiYNLSSVICHHGT-VGGGHYTCFARNTLN--GKWYEFDDQFVTEVSSELVQSCQAYVLFY 538
Cdd:cd02658 252 -----------YELIAFISHKGTsVHSGHYVAHIKKEIDgeGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
77-524 |
2.16e-18 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 91.09 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 77 TGLVGLQNIANTCYMNSALQALsnlppmthYFINcsdlveyiaeqsarrckpgglakSYRRLMQEIWQDVDDPKEFI--A 154
Cdd:COG5077 191 TGYVGLRNQGATCYMNSLLQSL--------FFIA-----------------------KFRKDVYGIPTDHPRGRDSValA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 155 PRGILYGIRTV-HPM-------------FRGYQQHDTQEFLRCFMDQLheelteqvsmlpqtqnqpqyqslqqqqpsetd 220
Cdd:COG5077 240 LQRLFYNLQTGeEPVdtteltrsfgwdsDDSFMQHDIQEFNRVLQDNL-------------------------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 221 denddeaapaslshaseseydtcESSMsersaevllkteyfvtpcrtngsnsglpeghsvqlqqaplqhqqknassaEQK 300
Cdd:COG5077 288 -----------------------EKSM--------------------------------------------------RGT 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 301 PIEAArsiISDVFDGKLLSSVQCLTCDRVSTREETFQDlslpipnrDFLNVLHqthslsvqslnaaetsartnegwlswm 380
Cdd:COG5077 295 VVENA---LNGIFVGKMKSYIKCVNVNYESARVEDFWD--------IQLNVKG--------------------------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 381 wnmlrswiygpSVTLYDCMASFFSADELKGDNMYSCER--CNKLRTGIKYSrvlTLPEVLCIHLKRFRNDLSYSS--KIS 456
Cdd:COG5077 337 -----------MKNLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIFE---SLPPVLHLQLKRFEYDFERDMmvKIN 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22026877 457 SDVYFPLEgFDMRPYIHKDCK---SEVAIYNLSSVICHHGTVGGGHYTCFARNTLNGKWYEFDDQFVTEVS 524
Cdd:COG5077 403 DRYEFPLE-IDLLPFLDRDADkseNSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRAT 472
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-538 |
9.99e-18 |
|
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: 86.99 E-value: 9.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 78 GLVGLQNIANTCYMNSALQALSNLPPMTHYFincsdLVEYIAEQSARRCKPggLAKSYRRLMQEIWqdvdDPKEF---IA 154
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFF-----LLYENYENIKDRKSE--LVKRLSELIRKIW----NPRNFkghVS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 155 PRGILYGIRTV-HPMFRGYQQHDTQEFLRCFMDQLHEELteqvsmlpqtqnqpqyqslqqqqpsetddenddeaapasls 233
Cdd:cd02669 187 PHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDL----------------------------------------- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 234 haseseydtcessmsersaevllkteyfvtpCRTNGSNSglpeghsvqlqqaplqhqqknassaeqkpieaarSIISDVF 313
Cdd:cd02669 226 -------------------------------GGSKKPNS----------------------------------SIIHDCF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 314 DGKL--------------LSSVQCLTCDRV-STREETFQDLSLPIPNRdflnvlhqthSLSVQSLNAaetsartnegwls 378
Cdd:cd02669 241 QGKVqietqkikphaeeeGSKDKFFKDSRVkKTSVSPFLLLTLDLPPP----------PLFKDGNEE------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 379 wmwNMLrswiygPSVTLYDCMASFFSadelkgdnmyscERCNKLRTGIKYSRVLTLPEVLCIHLKRFRNDLSYSSKISSD 458
Cdd:cd02669 298 ---NII------PQVPLKQLLKKYDG------------KTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 459 VYFPLEGFDMRPYIHKDCKSE--VAIYNLSSVICHHGTVGG-GHYTCFARNTLNGKWYEFDDQFVTEVSSELVQSCQAYV 535
Cdd:cd02669 357 VNFPIKNLDLSDYVHFDKPSLnlSTKYNLVANIVHEGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYI 436
|
...
gi 22026877 536 LFY 538
Cdd:cd02669 437 QIW 439
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
674-749 |
1.69e-16 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 75.10 E-value: 1.69e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22026877 674 IYAIAMPWLRSWQQFSRGKThKDPGPITNEGIAAPTENGSATVScVRLGSDYAQLNARLWRFLHNIYGGGPEIILR 749
Cdd:pfam06337 4 VYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLKPN-LQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-538 |
5.39e-16 |
|
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: 80.07 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 81 GLQNIANTCYMNSALQALSNLPPMThyfincSDLVEYIAEQSARRCKPGGLAKSYRRLMQEIwqdvDDPKEFIAPRGILY 160
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELR------DALKNYNPARRGANQSSDNLTNALRDLFDTM----DKKQEPVPPIEFLQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 161 GIRTVHPMF------RGYQQHDTQEflrCFmdqlheelteqvsmlpqtqnqpqyqslqqqqpsetddenddeaapaslsh 234
Cdd:cd02657 71 LLRMAFPQFaekqnqGGYAQQDAEE---CW-------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 235 aseseydtcessmsersaevllkteyfvtpcrtngsnsglpeghsVQLQQApLQHQQKNASSAeqkpieaaRSIISDVFD 314
Cdd:cd02657 98 ---------------------------------------------SQLLSV-LSQKLPGAGSK--------GSFIDQLFG 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 315 GKLLSSVQCLTCDR---VSTREETFqdLSLPIPNRDFLNVLHQ--THSLSvqslnaaETSARTNEgwlswmwnmlrswiy 389
Cdd:cd02657 124 IELETKMKCTESPDeeeVSTESEYK--LQCHISITTEVNYLQDglKKGLE-------EEIEKHSP--------------- 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 390 gpsvtlydcmasffsadELKGDNMYScercnklrtgiKYSRVLTLPEVLCIHLKRF--RNDLSYSSKISSDVYFPLEgFD 467
Cdd:cd02657 180 -----------------TLGRDAIYT-----------KTSRISRLPKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LD 230
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22026877 468 MRPYihkdCkSEVAIYNLSSVICHHG-TVGGGHYTCFARNTLNGKWYEFDDQFVTEVSSELVQSCQ-------AYVLFY 538
Cdd:cd02657 231 LYEL----C-TPSGYYELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
428-540 |
3.21e-12 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 68.29 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 428 YSRVLTLPEVLCIHLKRFRNDLSYSsKISSDVyfpLEGFDMRpyIHKDCKSEVA---IYNLSSVICHHGTVGGGHYTCFA 504
Cdd:COG5533 173 EVSFVKLPKILTIQLKRFANLGGNQ-KIDTEV---DEKFELP--VKHDQILNIVketYYDLVGFVLHQGSLEGGHYIAYV 246
|
90 100 110
....*....|....*....|....*....|....*....
gi 22026877 505 RNtlNGKWYEFDDQFVTEVSSE---LVQSCQAYVLFYHK 540
Cdd:COG5533 247 KK--GGKWEKANDSDVTPVSEEeaiNEKAKNAYLYFYER 283
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
564-638 |
3.28e-09 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 54.30 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 564 SDIQFYITREWLSRLATF-----SEPGPINNQEMLC--PHGGILHSKADVISQIAVPisQPLWDYLYRTFGGGPAVNIIF 636
Cdd:pfam06337 1 GDKVYLISSKWLNKWKSYvkepnNEPGPIDNSDLLDdeSNGQLKPNLQEGVDYVIVP--EEVWEFLVEWYGGGPEIKRNV 78
|
..
gi 22026877 637 EC 638
Cdd:pfam06337 79 VN 80
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
416-538 |
4.68e-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: 58.31 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 416 CERCnKLRTGIKYSRVLTLPEVLCIHLKRfrndlsYSSKISSDVYFPLEGFDMRPYIHKDCKsevaiYNLSSVICHHG-T 494
Cdd:cd02673 129 CSSC-KCESAISSERIMTFPECLSINLKR------YKLRIATSDYLKKNEEIMKKYCGTDAK-----YSLVAVICHLGeS 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 22026877 495 VGGGHYTCFARNTLNG-KWYEFDDQFVTEVSSELVQ---SCQAYVLFY 538
Cdd:cd02673 197 PYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
416-538 |
1.10e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 48.28 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 416 CERCNKLRTGIKYSRVLTLP----EVLCIHLKRFRN-------DLSYSSKISSDVYFPLEgfDMRPYIHKDCKSEVAIYN 484
Cdd:cd02672 137 CDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTNGefddinvVLPSGKVMQNKVSPKAI--DHDKLVKNRGQESIYKYE 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 22026877 485 LSSVICH-HGTVGGGHYTCFAR----NTLNGKWYEFDDQFVTEVsSELvqscqAYVLFY 538
Cdd:cd02672 215 LVGYVCEiNDSSRGQHNVVFVIkvneESTHGRWYLFNDFLVTPV-SEL-----AYILLY 267
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
483-538 |
2.29e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 44.40 E-value: 2.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22026877 483 YNLSSVICHHGTVGGGHYTCFARNTLNGKWYEFDDQFVTEV-SSELVQ-----SCQAYVLFY 538
Cdd:cd02666 281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVpASEVFLftlgnTATPYFLVY 342
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
434-538 |
4.75e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 42.93 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 434 LPEVLCIHLKRFRNDLSYSSKISSDVYFPlegfdmrpyihKDCKSEVaiYNLSSVICHHGTVGGGHYTCFARNTLNGKWY 513
Cdd:cd02665 128 LPPVLTFELSRFEFNQGRPEKIHDKLEFP-----------QIIQQVP--YELHAVLVHEGQANAGHYWAYIYKQSRQEWE 194
|
90 100 110
....*....|....*....|....*....|...
gi 22026877 514 EFDDQFVTEVSSELVQS--------CQAYVLFY 538
Cdd:cd02665 195 KYNDISVTESSWEEVERdsfgggrnPSAYCLMY 227
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| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
80-204 |
1.31e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 42.09 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026877 80 VGLQNIANTCYMNSALQALSNLPPMTHYFINCSDLVEYIAEQSARRCKPGGLAKSYRRLMQEIwqdvddpkEFIAPRGIL 159
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTERRIGGREVSRSELQRSN--------QFVYELRSL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 22026877 160 Y------GIRTVHPMFR----GYQQHDTQEFLRCFMDQLH--EELTEQVSMLPQTQN 204
Cdd:cd02666 74 FndlihsNTRSVTPSKElaylALRQQDVTECIDNVLFQLEvaLEPISNAFAGPDTED 130
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