|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
438-779 |
3.34e-170 |
|
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: 493.81 E-value: 3.34e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 438 RGLINLGNTCFMNCIVQALTHTPILRDFFLSDRH--RCEMPSPELCLVCEMSSLFREL-YSGNPSPHVPYKLLHLVWIHA 514
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHscTCLSCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 515 RHLAGYRQQDAHEFLIAALDVLHRHCKGDDvgKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLP 594
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDK--NEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 595 GSCTSFWPmspgressvNGEGHIPGITTLTDCLRRFTRPEHLGSSAkIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFE 674
Cdd:cd02660 159 NKSTPSWA---------LGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 675 HSA-KQRRKITTYISFPLELDMTPFMASSKesrmngQLQLPTNSGNNENKYSLFAVVNHQGTLESGHYTSFIRHHKDQWF 753
Cdd:cd02660 229 HSLnKTSRKIDTYVQFPLELNMTPYTSSSI------GDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQWF 302
|
330 340
....*....|....*....|....*.
gi 1149889052 754 KCDDAVITKASIKDVLDSEGYLLFYH 779
Cdd:cd02660 303 KFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
438-778 |
2.74e-84 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 270.85 E-value: 2.74e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 438 RGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELC--LVCEMSSLFRELYSGNPSPHV-PYKLLHLVWIHA 514
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSSSVsPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 515 RHLAGYRQQDAHEFLIAALDVLHRHCKGddvgkaaNNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLP 594
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNG-------NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 595 GSctsfwpmspgressvngeGHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFE 674
Cdd:pfam00443 154 GD------------------SAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 675 HSAKQRRKITTYISFPLELDMTPFMASSKESRMngqlqlptnsgNNENKYSLFAVVNHQGTLESGHYTSFIRHHKD-QWF 753
Cdd:pfam00443 216 YNRSTWEKLNTEVEFPLELDLSRYLAEELKPKT-----------NNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENnRWY 284
|
330 340
....*....|....*....|....*.
gi 1149889052 754 KCDDAVITKAS-IKDVLDSEGYLLFY 778
Cdd:pfam00443 285 KFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
438-778 |
8.34e-75 |
|
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: 245.26 E-value: 8.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 438 RGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHL 517
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 518 AGYRQQDAHEFLIAALDVLHRHC-KGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDlpgs 596
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKAClDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 597 ctsfwpmspgressvngeghIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFehS 676
Cdd:cd02661 158 --------------------IKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF--S 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 677 AKQRRKITTYISFPLELDMTPFMasskesrmngqlqlpTNSGNNENKYSLFAVVNHQGT-LESGHYTSFIRHHKDQWFKC 755
Cdd:cd02661 216 NFRGGKINKQISFPETLDLSPYM---------------SQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNGKWYNM 280
|
330 340
....*....|....*....|...
gi 1149889052 756 DDAVITKASIKDVLDSEGYLLFY 778
Cdd:cd02661 281 DDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
439-778 |
5.42e-71 |
|
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: 233.53 E-value: 5.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALTHtpilrdfflsdrhrcempspelclvcemsslfrelysgnpsphvpykllhlvwiharhla 518
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 519 gyRQQDAHEFLIAALDVLHRHCKGddVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPgsct 598
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKK--SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP---- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 599 sfwpmspgressVNGEGHIpgitTLTDCLRRFTRPEHLGSSAKIKCgSCQSYQESTKQLTMNKLPVVACFHFKRFEH-SA 677
Cdd:cd02257 93 ------------VKGLPQV----SLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFnED 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 678 KQRRKITTYISFPLELDMTPFMASSKEsrmngqlqlPTNSGNNENKYSLFAVVNHQGTL-ESGHYTSFIRHH-KDQWFKC 755
Cdd:cd02257 156 GTKEKLNTKVSFPLELDLSPYLSEGEK---------DSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPsDGKWYKF 226
|
330 340
....*....|....*....|....*...
gi 1149889052 756 DDAVITKASIKDVLD-----SEGYLLFY 778
Cdd:cd02257 227 NDDKVTEVSEEEVLEfgslsSSAYILFY 254
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-778 |
1.14e-67 |
|
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: 223.70 E-value: 1.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALTHtpilrdfflsdrhrcempspelclvcemsslfrelysgnpsphvpykllhlvwiharhla 518
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 519 gyRQQDAHEFLIAALDVLHRhckgddvgkaannpnhcncIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCT 598
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS-------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSG 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 599 SFWPMspgressvngeghipgitTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHSAK 678
Cdd:cd02674 80 DAPKV------------------TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRG 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 679 QRRKITTYISFPLE-LDMTPFmasskesrmngqlqLPTNSGNNENKYSLFAVVNHQGTLESGHYTSFIRH-HKDQWFKCD 756
Cdd:cd02674 142 STRKLTTPVTFPLNdLDLTPY--------------VDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNnETNDWYKFD 207
|
330 340
....*....|....*....|..
gi 1149889052 757 DAVITKASIKDVLDSEGYLLFY 778
Cdd:cd02674 208 DSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-778 |
4.84e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 185.67 E-value: 4.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALTHTPILRDFFLsdrhrcemPSPELCL--VCEMSSLFRelysgnpsphvpykllhlvwiharh 516
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLS--------ETPKELFsqVCRKAPQFK------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 517 laGYRQQDAHEFLIAALDVLhrhckgddvgkaannpnhcNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISldLPgs 596
Cdd:cd02667 48 --GYQQQDSHELLRYLLDGL-------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLS--LP-- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 597 ctsfwpmspgRESSVNGEghipgiTTLTDCLRRFTRPEHLGSSAKIKCGSCqsyQESTKQLTMNKLPVVACFHFKRFEHS 676
Cdd:cd02667 103 ----------RSDEIKSE------CSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 677 AKQR-RKITTYISFPLELDMTPFMASSKESrmngqlqlptNSGNNENKYSLFAVVNHQGTLESGHYTSFIRHH------- 748
Cdd:cd02667 164 RSANlRKVSRHVSFPEILDLAPFCDPKCNS----------SEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrls 233
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1149889052 749 ---------------KDQWFKCDDAVITKASIKDVLDSEGYLLFY 778
Cdd:cd02667 234 dltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
436-771 |
1.71e-46 |
|
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: 168.97 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 436 GLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRcEMPSPELCLVCEMSSLFRELYSGnpspHVPYKLLHLVWIHAR 515
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-EDDDDNKSVPLALQRLFLFLQLS----ESPVKTTELTDKTRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 516 H----LAGYRQQDAHEFLIAALDVLhrhckgDDVGKAANNPNhcncIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISL 591
Cdd:cd02659 76 FgwdsLNTFEQHDVQEFFRVLFDKL------EEKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 592 DlpgsctsfwpmspgressvngeghIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFK 671
Cdd:cd02659 146 A------------------------VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 672 RFEHS--AKQRRKITTYISFPLELDMTPFMASSkesrMNGQLQLPTNSGNNENKYSLFAVVNHQGTLESGHYTSFIR-HH 748
Cdd:cd02659 202 RFEFDfeTMMRIKINDRFEFPLELDMEPYTEKG----LAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKdRD 277
|
330 340
....*....|....*....|...
gi 1149889052 749 KDQWFKCDDAVITKASIKDVLDS 771
Cdd:cd02659 278 DGKWYKFNDDVVTPFDPNDAEEE 300
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-778 |
1.48e-36 |
|
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: 139.75 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALTHtpilrdfflsdrhrcempspeLCLVCEMSSLFRELYSGNPSPHV--PYKLLHLVWIHARH 516
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF---------------------ENLLTCLKDLFESISEQKKRTGVisPKKFITRLKRENEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 517 LAGYRQQDAHEFL-------IAALDVLHRHCKGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDI 589
Cdd:cd02663 60 FDNYMHQDAHEFLnfllneiAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 590 SLDLPGSctsfwpmspgressvngeghipgiTTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFH 669
Cdd:cd02663 140 SIDVEQN------------------------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 670 FKRFEHSAKQRR--KITTYISFPLEldmtpfmasskesrmngqLQLPTNSGNNEN---KYSLFAVVNHQG-TLESGHYTS 743
Cdd:cd02663 196 LKRFKYDEQLNRyiKLFYRVVFPLE------------------LRLFNTTDDAENpdrLYELVAVVVHIGgGPNHGHYVS 257
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1149889052 744 FIRHHkDQWFKCDDAVITKASIKDVLD--------SEGYLLFY 778
Cdd:cd02663 258 IVKSH-GGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
435-778 |
3.80e-35 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 143.49 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 435 IGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEM-PSPELC----LVCEMSSLFRELYSGNPSPHVPYKLLHL 509
Cdd:COG5560 263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESInEENPLGmhgsVASAYADLIKQLYDGNLHAFTPSGFKKT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 510 VWIHARHLAGYRQQDAHEFLIAALDVLHRH---------------CKGDDVgKAANNPNHC-------NC-IIDQIFTGG 566
Cdd:COG5560 343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDlnriikkpytskpdlSPGDDV-VVKKKAKECwwehlkrNDsIITDLFQGM 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 567 LQSDVTCQACHGVSTTIDPCWDISLDLPGSCT-----SFWPMS------------------------------------- 604
Cdd:COG5560 422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVwkhtiVVFPESgrrqplkieldasstirglkklvdaeygklgcfeikv 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 605 -------------------------------------------------PG----------------------------- 606
Cdd:COG5560 502 mciyyggnynmlepadkvllqdipqtdfvylyetndngievpvvhlrieKGykskrlfgdpflqlnvlikasiydklvke 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 607 --------------------------------------------RESSVNGEG--------------------------- 615
Cdd:COG5560 582 feellvlvemkktdvdlvseqvrllreesspsswlkleteidtkREEQVEEEGqmnfndavvisceweekrylslfsydp 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 616 ---------HIPGItTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHSAKQRRKITTY 686
Cdd:COG5560 662 lwtireigaAERTI-TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDL 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 687 ISFPL-ELDMTPFMASSKESRMNgqlqlptnsgnnenkYSLFAVVNHQGTLESGHYTSFIRHHKDQ-WFKCDDAVITKAS 764
Cdd:COG5560 741 VEYPIdDLDLSGVEYMVDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYARNFANNgWYLFDDSRITEVD 805
|
570
....*....|....
gi 1149889052 765 IKDVLDSEGYLLFY 778
Cdd:COG5560 806 PEDSVTSSAYVLFY 819
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-766 |
1.81e-33 |
|
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: 131.39 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALTHTPILRDFFLS---------DRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLlhl 509
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstedaelKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 510 vwIHARHLAGYRQQDAHEFLIAALDVLHRHCKgddvgkAANNPNHCNcIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDI 589
Cdd:cd02668 78 --VKALGLDTGQQQDAQEFSKLFLSLLEAKLS------KSKNPDLKN-IVQDLFRGEYSYVTQCSKCGRESSLPSKFYEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 590 SLDLPGSctsfwpmspgressvngeghipgiTTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFH 669
Cdd:cd02668 149 ELQLKGH------------------------KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 670 FKRFEHSAK--QRRKITTYISFPLELDMTPFMASSKEsrmngqlqlptnsGNNEnkYSLFAVVNHQGT-LESGHYTSFIR 746
Cdd:cd02668 205 LLRFVFDRKtgAKKKLNASISFPEILDMGEYLAESDE-------------GSYV--YELSGVLIHQGVsAYSGHYIAHIK 269
|
330 340
....*....|....*....|.
gi 1149889052 747 H-HKDQWFKCDDAVITKASIK 766
Cdd:cd02668 270 DeQTGEWYKFNDEDVEEMPGK 290
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-778 |
1.23e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 117.04 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMP--SPELCLVCEMSSLFRELYSG-------NPSPHVPYKLlHL 509
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQLIKLADGLLSGryskpasLKSENDPYQV-GI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 510 VWIHARHLAGY--------RQQDAHEFLIAALDVLHRHCKGddvgKAANNPNhcnciidQIFTGGLQSDVTCQACHGVST 581
Cdd:cd02658 80 KPSMFKALIGKghpefstmRQQDALEFLLHLIDKLDRESFK----NLGLNPN-------DLFKFMIEDRLECLSCKKVKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 582 TIDPCWDISLDLPgsctsfwpMSPGRESSVNGEGHIPgiTTLTDCLRRFTRPEHLgssaKIKCGSCQSYQESTKQLTMNK 661
Cdd:cd02658 149 TSELSEILSLPVP--------KDEATEKEEGELVYEP--VPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 662 LPVVACFHFKRFEHSA-KQRRKITTYISFPLELDmtpfmasskesrmngqlqlptnSGnnenKYSLFAVVNHQGT-LESG 739
Cdd:cd02658 215 FPDYLVINMKRFQLLEnWVPKKLDVPIDVPEELG----------------------PG----KYELIAFISHKGTsVHSG 268
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1149889052 740 HYTSFIR---HHKDQWFKCDDAVITKASIKDVLDSEGYLLFY 778
Cdd:cd02658 269 HYVAHIKkeiDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
433-778 |
1.69e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 119.35 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 433 FTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLS---DRHRCEMPSPelcLVCEMSSLFRELYS-----GNPSPHvpy 504
Cdd:cd02669 115 YLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyenYENIKDRKSE---LVKRLSELIRKIWNprnfkGHVSPH--- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 505 KLLHLVWIHARHLAGYRQQ-DAHEFLIAALDVLHRHCKgddvGKAANNPNhcncIIDQIFTGGLQ-----------SDVT 572
Cdd:cd02669 189 ELLQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLG----GSKKPNSS----IIHDCFQGKVQietqkikphaeEEGS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 573 CQACHG----VSTTIDPCWDISLDLPgsctsfwPMSPGResSVNGEGHIPGItTLTDCLRRFTrpehlGSsakikcgSCQ 648
Cdd:cd02669 261 KDKFFKdsrvKKTSVSPFLLLTLDLP-------PPPLFK--DGNEENIIPQV-PLKQLLKKYD-----GK-------TET 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 649 SYQESTKQLTMNKLPVVACFHFKRFEHSAKQRRKITTYISFPLE-LDMTPFMASskesrmngqlqlPTNSGNNENKYSLF 727
Cdd:cd02669 319 ELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKnLDLSDYVHF------------DKPSLNLSTKYNLV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1149889052 728 AVVNHQGT-LESGHYTSFIRHHK-DQWFKCDDAVITKASIKDVLDSEGYLLFY 778
Cdd:cd02669 387 ANIVHEGTpQEDGTWRVQLRHKStNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-778 |
2.43e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 115.89 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALTHTPILRD---FFLSDRHRCEmpSPELCLVCEMSSLFRELySGNPSPHVPYKLLHLVWIHAR 515
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGAN--QSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 516 HLA------GYRQQDAHEFLIAALDVLHRHCKGDDVGKAAnnpnhcnciIDQIFTGGLQSDVTCQACHGVSttidpcwdi 589
Cdd:cd02657 78 QFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKGSF---------IDQLFGIELETKMKCTESPDEE--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 590 sldlpgsctsfwPMSPGRESSVNgeGHIpGITTLTDCLrrFTRPEHlGSSAKIKCGSCQSYQES--TKQLTMNKLPVVAC 667
Cdd:cd02657 140 ------------EVSTESEYKLQ--CHI-SITTEVNYL--QDGLKK-GLEEEIEKHSPTLGRDAiyTKTSRISRLPKYLT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 668 FHFKRF--EHSAKQRRKITTYISFPLELDMTPFMasskesrmngqlqlpTNSGNnenkYSLFAVVNHQG-TLESGHYTSF 744
Cdd:cd02657 202 VQFVRFfwKRDIQKKAKILRKVKFPFELDLYELC---------------TPSGY----YELVAVITHQGrSADSGHYVAW 262
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1149889052 745 IRH-HKDQWFKCDDAVITKASIKDVLDSEG-------YLLFY 778
Cdd:cd02657 263 VRRkNDGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-778 |
2.77e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 113.45 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALTHTPilrDFFLSDRHRCEMPSP--ELCLVCEmssLFRELYSGNPSPHVPYKLLHLVWIHARH 516
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCP---GFKHGLKHLVSLISSveQLQSSFL---LNPEKYNDELANQAPRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 517 LAGYRQQDAHEFLIAALDVLHRhckgddvgkaannpnhcncIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGS 596
Cdd:cd02671 100 YEGYLQHDAQEVLQCILGNIQE-------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 597 CTSFWPMSPGRESSVNGEghipgITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHS 676
Cdd:cd02671 161 ELSKSEESSEISPDPKTE-----MKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAAN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 677 AKQR------RKITTYISFPLELDMtpFMASSKESRmngqlqlptnsgnneNKYSLFAVVNHQG-TLESGHYTSFIRhhk 749
Cdd:cd02671 236 GSEFdcygglSKVNTPLLTPLKLSL--EEWSTKPKN---------------DVYRLFAVVMHSGaTISSGHYTAYVR--- 295
|
330 340 350
....*....|....*....|....*....|....*...
gi 1149889052 750 dqWFKCDDAVITKASIKDVLD---------SEGYLLFY 778
Cdd:cd02671 296 --WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
436-770 |
3.24e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 115.74 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 436 GLRGLINLGNTCFMNCIVQALTHTPILRD--FFLSDRHrcemPSPELCLVCEMSSLFRELYSGNpsphVPYKLLHLV--- 510
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDH----PRGRDSVALALQRLFYNLQTGE----EPVDTTELTrsf 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 511 -WIHARHlagYRQQDAHEFLIAALDVLHRHCKGDDVGKAANNpnhcnciidqIFTGGLQSDVTCQACHGVSTTIDPCWDI 589
Cdd:COG5077 264 gWDSDDS---FMQHDIQEFNRVLQDNLEKSMRGTVVENALNG----------IFVGKMKSYIKCVNVNYESARVEDFWDI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 590 SLDLPGSctsfwpmspgressvngeghipgiTTLTDCLRRFTRPEHLGSSakiKCGSCQSY--QESTKQLTMNKLPVVAC 667
Cdd:COG5077 331 QLNVKGM------------------------KNLQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESLPPVLH 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 668 FHFKRFEHSAK--QRRKITTYISFPLELDMTPFMasSKESRmngqlqlptNSGNNENKYSLFAVVNHQGTLESGHYTSFI 745
Cdd:COG5077 384 LQLKRFEYDFErdMMVKINDRYEFPLEIDLLPFL--DRDAD---------KSENSDAVYVLYGVLVHSGDLHEGHYYALL 452
|
330 340
....*....|....*....|....*.
gi 1149889052 746 RHHKD-QWFKCDDAVITKASIKDVLD 770
Cdd:COG5077 453 KPEKDgRWYKFDDTRVTRATEKEVLE 478
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-778 |
3.01e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 107.58 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLV--WIHARh 516
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASRppWFTPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 517 lagyRQQDAHEFLIAALDVLHrhckgddvgkaannpnhcnCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPgs 596
Cdd:cd02664 80 ----SQQDCSEYLRYLLDRLH-------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 597 ctsfwpmspgressvngeghipgitTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHS 676
Cdd:cd02664 135 -------------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 677 AKQ--RRKITTYISFPLELDMtPFMASSKESRMNGQLQLPTNSGNNEN-----KYSLFAVVNHQGT-LESGHYTSFIRHH 748
Cdd:cd02664 190 QKThvREKIMDNVSINEVLSL-PVRVESKSSESPLEKKEEESGDDGELvtrqvHYRLYAVVVHSGYsSESGHYFTYARDQ 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1149889052 749 KDQ---------------------WFKCDDAVITKASIKDVLDSEG-------YLLFY 778
Cdd:cd02664 269 TDAdstgqecpepkdaeendesknWYLFNDSRVTFSSFESVQNVTSrfpkdtpYILFY 326
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-778 |
6.60e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 101.29 E-value: 6.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALthtpilrdfflsdrhrcempspelclvcemSSLfrelysgnpsphvPYKLLHLVWIHArhla 518
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL------------------------------ASL-------------PSLIEYLEEFLE---- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 519 gyrQQDAHEFLIAALDVLHRHCKgddvgkaanNPnhcnciidqiFTGGLQSDVTCQACHGVST-TIDPCWDISLDLPGSc 597
Cdd:cd02662 34 ---QQDAHELFQVLLETLEQLLK---------FP----------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQ- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 598 tsfwpmspgressvngegHIPGITTLTDCLRRFTRPEHLGSsakIKCGSCQsyqestkqLTMNKLPVVACFHFKRFEHSA 677
Cdd:cd02662 91 ------------------SSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVFDG 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 678 K-QRRKITTYISFPLELdmtpfmasskesrmngqlqlptnsgnNENKYSLFAVVNHQGTLESGHYTSFIRHH-------- 748
Cdd:cd02662 142 RgTSTKNSCKVSFPERL--------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdkep 195
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1149889052 749 -------------KDQWFKCDDAVITKASIKDVL-DSEGYLLFY 778
Cdd:cd02662 196 gsfvrmregpsstSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
439-780 |
1.79e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 101.42 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALT-HTP-----ILRDFF----LSDRHRCEMPSPELClvcEMSSLFRELysgnpsphVPYKLLH 508
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPkldelLDDLSKelkvLKNVIRKPEPDLNQE---EALKLFTAL--------WSSKEHK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 509 LVWIHARhlagYRQQDAHEFLIAALDVLhrhckgddvgkaaNNPNHcNCIIDQIF-TGGlqsdvtcqacHGVSTTIDPCW 587
Cdd:COG5533 70 VGWIPPM----GSQEDAHELLGKLLDEL-------------KLDLV-NSFTIRIFkTTK----------DKKKTSTGDWF 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 588 DISLDLPgsctsfwpmspgRESSVNGEghipgiTTLTDCLRRFtrpEHLGSSAK-IKCGSCQSYQESTKQLTMN---KLP 663
Cdd:COG5533 122 DIIIELP------------DQTWVNNL------KTLQEFIDNM---EELVDDETgVKAKENEELEVQAKQEYEVsfvKLP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 664 VVACFHFKRFEHSAkQRRKITTYISFPLELdmtPFMASskesrmngqlqlPTNSGNNENKYSLFAVVNHQGTLESGHYTS 743
Cdd:COG5533 181 KILTIQLKRFANLG-GNQKIDTEVDEKFEL---PVKHD------------QILNIVKETYYDLVGFVLHQGSLEGGHYIA 244
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1149889052 744 FIRhHKDQWFKCDDAVITKASIKDVLDS---EGYLLFYHK 780
Cdd:COG5533 245 YVK-KGGKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
439-757 |
6.03e-16 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 79.24 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQALTHTPILRDFFLSdrHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHAR--- 515
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 516 -HLAGYRQQDAHEFLIAAL-DVLHR---HCKGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTidpcwdis 590
Cdd:pfam13423 80 lGLLDEDRETNSAISLSSLiQSFNRfllDQLSSEENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVR-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 591 ldlPGSCTSFWPMSPGRESSVNgegHIPGITTLTDCLRRFTRPEhlgSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHF 670
Cdd:pfam13423 152 ---ESSTHVLDLIYPRKPSSNN---KKPPNQTFSSILKSSLERE---TTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 671 KRfeHSAKQRRKITTYISFPLELDMTpfmasskesrmngqLQLPTNSGNNENKYSLFAVVNH-QGTLESGHYTSFIR--- 746
Cdd:pfam13423 223 AL--TNEEWRQLWKTPGWLPPEIGLT--------------LSDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVKvad 286
|
330
....*....|....*.
gi 1149889052 747 -----HHKDQWFKCDD 757
Cdd:pfam13423 287 seledPTESQWYLFND 302
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
310-370 |
9.29e-14 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 66.52 E-value: 9.29e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149889052 310 CHVCGTHLNrLHSCLSCVFFGCFT--EKHIHEHAETKQHNLAVDLYYGGIYCFMCKDYVYDKD 370
Cdd:pfam02148 1 CSLCGNTSN-LWLCLTCGHVGCGRyqNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-778 |
1.66e-11 |
|
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: 66.36 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 439 GLINLGNTCFMNCIVQAL-THTPiLRDFFL----------SDRH-------RCEMPSPELC---LVCEMSSLFRELYSGN 497
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFfTIKP-LRDLVLnfdeskaelaSDYPterriggREVSRSELQRsnqFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 498 PSPHVPYKLLHLvwiharhlAGYRQQDAHEFLIAALDVLHRHCKGD---DVGKAANNPNHCNCIIDQIFTGGL-QSDVTC 573
Cdd:cd02666 82 TRSVTPSKELAY--------LALRQQDVTECIDNVLFQLEVALEPIsnaFAGPDTEDDKEQSDLIKRLFSGKTkQQLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 574 QACHGVSTTIDPCWDISLDLPgsCTSFWPMSPGRESSVngeghipgitTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQ-E 652
Cdd:cd02666 154 SMGNQPSVRTKTERFLSLLVD--VGKKGREIVVLLEPK----------DLYDALDRYFDYDSLTKLPQRSQVQAQLAQpL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 653 STKQLTMNKlpvvacfhfkRFEHSAKQRRKI---TTYISFPLELDMTPFMASSKESRMNGQLQlptnsGNNENKYSLFAV 729
Cdd:cd02666 222 QRELISMDR----------YELPSSIDDIDElirEAIQSESSLVRQAQNELAELKHEIEKQFD-----DLKSYGYRLHAV 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149889052 730 VNHQGTLESGHYTSFIRHHKDQ--WFKCDDAVITKASIKDVLDSEG-----YLLFY 778
Cdd:cd02666 287 FIHRGEASSGHYWVYIKDFEENvwRKYNDETVTVVPASEVFLFTLGntatpYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
522-778 |
2.97e-10 |
|
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: 61.39 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 522 QQDAHEFL---IAALDVLHRHcKGDDVGKAANNPNHCNCIidQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDlpgsct 598
Cdd:cd02673 33 QQDAHEFLltlLEAIDDIMQV-NRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGNFLDVS------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 599 sfwpMSPGRESSvngeghipgITTLTDCLRRFTRPEHlgssakiKCGSCQSYQESTKQLTMNkLPVVACFHFKRFehsaK 678
Cdd:cd02673 104 ----MIDNKLDI---------DELLISNFKTWSPIEK-------DCSSCKCESAISSERIMT-FPECLSINLKRY----K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 679 QRRKITTYisfpleldmtpfMASSKESRMNGQLQLPtnsgnnenKYSLFAVVNHQG-TLESGHYTSFIR--HHKDQWFKC 755
Cdd:cd02673 159 LRIATSDY------------LKKNEEIMKKYCGTDA--------KYSLVAVICHLGeSPYDGHYIAYTKelYNGSSWLYC 218
|
250 260
....*....|....*....|....*.
gi 1149889052 756 DDAVITKASIKDVLD---SEGYLLFY 778
Cdd:cd02673 219 SDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
660-778 |
3.38e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 49.06 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 660 NKLPVVACFHFKRFEHSAKQRRKITTYISFPLELDMTPFMASSKESRMNGQLQLPT-------NSGNNENKYSLFAVVNH 732
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCQLECRVcyddkdfSPTCGKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149889052 733 QGT-LESGHYTSFIRHHKD------------QWFKCDD-----AVITKASIKDVLDSE-GYLLFY 778
Cdd:cd02670 176 RGTsLETGHYVAFVRYGSYsltetdneaynaQWVFFDDmadrdGVSNGFNIPAARLLEdPYMLFY 240
|
|
| Trypan_PARP |
pfam05887 |
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ... |
109-180 |
4.11e-06 |
|
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.
Pssm-ID: 368653 Cd Length: 134 Bit Score: 47.09 E-value: 4.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149889052 109 AKVEGkAEAAGKVDATERVETAGKVDAAGKVETAEGPGRR--AELKLEPEPEPAREAEQEQEPKGEPKPELEDE 180
Cdd:pfam05887 26 AAAEG-PEDKGLTKGGKGKGKGTKVSDDDTNGTDPEPEPEpePEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 98
|
|
| Trypan_PARP |
pfam05887 |
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ... |
140-180 |
5.92e-06 |
|
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.
Pssm-ID: 368653 Cd Length: 134 Bit Score: 46.32 E-value: 5.92e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1149889052 140 ETAEGPGRRAELKLEPEPEPAREAEQEQEPKGEPKPELEDE 180
Cdd:pfam05887 62 EPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 102
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
610-778 |
1.51e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 47.17 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 610 SVNGEGHipgittLTDCLRRFT---RPEHLGSSAKIKCGSCQSYQEstkqltmnkLPVVACFHFKRFEHSAKQRRKITTY 686
Cdd:cd02665 88 QVNGYGN------LHECLEAAMfegEVELLPSDHSVKSGQERWFTE---------LPPVLTFELSRFEFNQGRPEKIHDK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889052 687 ISFPLELdmtpfmasskesrmngqlqlptnsgnNENKYSLFAVVNHQGTLESGHYTSFI-RHHKDQWFKCDDAVITKASI 765
Cdd:cd02665 153 LEFPQII--------------------------QQVPYELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSW 206
|
170 180
....*....|....*....|.
gi 1149889052 766 KDVL-DSEG-------YLLFY 778
Cdd:cd02665 207 EEVErDSFGggrnpsaYCLMY 227
|
|
| |
