|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-462 |
1.88e-124 |
|
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: 368.36 E-value: 1.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 1 MKKLQHLFAFLAHTQREAYAPRI-FFEASRPPWFTPRSQQDCSEYLRFLLDRLHeeekilriqsshkpseglgctetclq 79
Cdd:cd02664 43 MKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGSQQDCSEYLRYLLDRLH-------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 80 evtnkvavpsespstggsekTLIEKMFGGKLRTHICCLNCRSTSHKVEAFTDLSLAFCpspsvedssfqdpaslpsaqdd 159
Cdd:cd02664 97 --------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 160 glmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsppvefpcaknssvpgesakilvskdvpqnpggesttSVTDLLN 239
Cdd:cd02664 135 -------------------------------------------------------------------------SVQDLLN 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 240 YFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLELPVKRTSLSSLS 319
Cdd:cd02664 142 YFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKSSES 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 320 EGwsadadftdvnenlAKKLKPSGTEEAFCPKLVPYLLSSVVVHSGVSSESGHYYSYARNITGTESSYQMRPQseslslt 399
Cdd:cd02664 222 PL--------------EKKEEESGDDGELVTRQVHYRLYAVVVHSGYSSESGHYFTYARDQTDADSTGQECPE------- 280
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746614 400 psqssllggespntviEQDLENKEMSQEWFLFNDSRVTFTSFQSVQKITSRFPKDTAYVLFYK 462
Cdd:cd02664 281 ----------------PKDAEENDESKNWYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFYE 327
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
4-461 |
1.02e-20 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 92.89 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 4 LQHLF-AFLAHTQREAYAPRIFFEA--SRPPWFTPRSQQDCSEYLRFLLDRLHEEekilriqsshkpSEGLGCTEtclqe 80
Cdd:pfam00443 51 LRDLFkALQKNSKSSSVSPKMFKKSlgKLNPDFSGYKQQDAQEFLLFLLDGLHED------------LNGNHSTE----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 81 vtnkvavpsespstggsEKTLIEKMFGGKLRTHICCLNCRSTSHKVEAFTDLSLAFCPSPSVEDSSFQDPASLPsaqddg 160
Cdd:pfam00443 114 -----------------NESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFLQ------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 161 lmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsppvefpcaknssvpgesakilvskdvpqnpggesttsvtdllny 240
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 241 FLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKyhVRRKILDNVSLPLVLelpvkrtSLSSLSE 320
Cdd:pfam00443 171 FSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLEL-------DLSRYLA 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 321 gwsadadfTDVNENLAKKLK--------PSGTEEafcpklvpyllssvvvhsgvsseSGHYYSYARNitgtessyqmrpq 392
Cdd:pfam00443 242 --------EELKPKTNNLQDyrlvavvvHSGSLS-----------------------SGHYIAYIKA------------- 277
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746614 393 seslsltpsqssllggespntvieqdlenkEMSQEWFLFNDSRVTFTSFQSVQKitsrfpKDTAYVLFY 461
Cdd:pfam00443 278 ------------------------------YENNRWYKFDDEKVTEVDEETAVL------SSSAYILFY 310
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
229-465 |
4.44e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 62.59 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 229 ESTTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYhvRRKILDNVSLPLvlel 308
Cdd:COG5560 672 ERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPI---- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 309 pvkrtslsslsegwsadadftdvnenlaKKLKPSGTEEAFCPKLVPYLLsSVVVHSGVSSESGHYYSYARNITgtessyq 388
Cdd:COG5560 746 ----------------------------DDLDLSGVEYMVDDPRLIYDL-YAVDNHYGGLSGGHYTAYARNFA------- 789
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746614 389 mrpqseslsltpsqssllggespntvieqdlenkemSQEWFLFNDSRVTFTSfqSVQKITSrfpkdTAYVLFYKKQS 465
Cdd:COG5560 790 ------------------------------------NNGWYLFDDSRITEVD--PEDSVTS-----SAYVLFYRRKS 823
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-462 |
1.88e-124 |
|
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: 368.36 E-value: 1.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 1 MKKLQHLFAFLAHTQREAYAPRI-FFEASRPPWFTPRSQQDCSEYLRFLLDRLHeeekilriqsshkpseglgctetclq 79
Cdd:cd02664 43 MKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGSQQDCSEYLRYLLDRLH-------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 80 evtnkvavpsespstggsekTLIEKMFGGKLRTHICCLNCRSTSHKVEAFTDLSLAFCpspsvedssfqdpaslpsaqdd 159
Cdd:cd02664 97 --------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 160 glmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsppvefpcaknssvpgesakilvskdvpqnpggesttSVTDLLN 239
Cdd:cd02664 135 -------------------------------------------------------------------------SVQDLLN 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 240 YFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLELPVKRTSLSSLS 319
Cdd:cd02664 142 YFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKSSES 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 320 EGwsadadftdvnenlAKKLKPSGTEEAFCPKLVPYLLSSVVVHSGVSSESGHYYSYARNITGTESSYQMRPQseslslt 399
Cdd:cd02664 222 PL--------------EKKEEESGDDGELVTRQVHYRLYAVVVHSGYSSESGHYFTYARDQTDADSTGQECPE------- 280
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746614 400 psqssllggespntviEQDLENKEMSQEWFLFNDSRVTFTSFQSVQKITSRFPKDTAYVLFYK 462
Cdd:cd02664 281 ----------------PKDAEENDESKNWYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFYE 327
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
37-462 |
2.06e-29 |
|
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: 116.81 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 37 SQQDCSEYLRFLLDRLHEEEKILRIQSSHKPSEglgctetclqevtnkvavpsespstggseKTLIEKMFGGKLRTHICC 116
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL-----------------------------KSLIHDLFGGKLESTIVC 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 117 LNCRSTSHKVEAFTDLSLafcpspsvedssfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgs 196
Cdd:cd02257 72 LECGHESVSTEPELFLSL-------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 197 ppvefpcaknssvpgesakilvskDVPQNPGGESttSVTDLLNYFLAPEVLTGENQYYCESCaSLQNAEKTMQITEEPEY 276
Cdd:cd02257 90 ------------------------PLPVKGLPQV--SLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPV 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 277 LILTLLRFSYDQKYhVRRKILDNVSLPLVLelpvkrtslsslsegwsadadftdvneNLAKKLKPSGTEEAFCPKLVPYL 356
Cdd:cd02257 143 LIIHLKRFSFNEDG-TKEKLNTKVSFPLEL---------------------------DLSPYLSEGEKDSDSDNGSYKYE 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 357 LSSVVVHSGVSSESGHYYSYARNITgtessyqmrpqseslsltpsqssllggespntvieqdlenkemSQEWFLFNDSRV 436
Cdd:cd02257 195 LVAVVVHSGTSADSGHYVAYVKDPS-------------------------------------------DGKWYKFNDDKV 231
|
410 420
....*....|....*....|....*.
gi 1958746614 437 TFTSFQSVQKITSRfpKDTAYVLFYK 462
Cdd:cd02257 232 TEVSEEEVLEFGSL--SSSAYILFYE 255
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
4-461 |
1.02e-20 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 92.89 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 4 LQHLF-AFLAHTQREAYAPRIFFEA--SRPPWFTPRSQQDCSEYLRFLLDRLHEEekilriqsshkpSEGLGCTEtclqe 80
Cdd:pfam00443 51 LRDLFkALQKNSKSSSVSPKMFKKSlgKLNPDFSGYKQQDAQEFLLFLLDGLHED------------LNGNHSTE----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 81 vtnkvavpsespstggsEKTLIEKMFGGKLRTHICCLNCRSTSHKVEAFTDLSLAFCPSPSVEDSSFQDPASLPsaqddg 160
Cdd:pfam00443 114 -----------------NESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFLQ------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 161 lmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsppvefpcaknssvpgesakilvskdvpqnpggesttsvtdllny 240
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 241 FLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKyhVRRKILDNVSLPLVLelpvkrtSLSSLSE 320
Cdd:pfam00443 171 FSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLEL-------DLSRYLA 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 321 gwsadadfTDVNENLAKKLK--------PSGTEEafcpklvpyllssvvvhsgvsseSGHYYSYARNitgtessyqmrpq 392
Cdd:pfam00443 242 --------EELKPKTNNLQDyrlvavvvHSGSLS-----------------------SGHYIAYIKA------------- 277
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746614 393 seslsltpsqssllggespntvieqdlenkEMSQEWFLFNDSRVTFTSFQSVQKitsrfpKDTAYVLFY 461
Cdd:pfam00443 278 ------------------------------YENNRWYKFDDEKVTEVDEETAVL------SSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-461 |
2.87e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 85.79 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 5 QHLFAFLAHTqREAYAPRIFFEASRPPW--FTPRSQQDCSEYLRFLLDRLHEeekilriqsshkpseglgcteTCLQEVT 82
Cdd:cd02661 52 AHVERALASS-GPGSAPRIFSSNLKQISkhFRIGRQEDAHEFLRYLLDAMQK---------------------ACLDRFK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 83 NKVAVPSESPSTggsekTLIEKMFGGKLRTHICCLNCRSTSHKVEAFTDLSLAFCPSPSVEDSsfqdpaslpsaqddglm 162
Cdd:cd02661 110 KLKAVDPSSQET-----TLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDA----------------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 163 qtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsppvefpcaknssvpgesakilvskdvpqnpggesttsvtdlLNYFL 242
Cdd:cd02661 168 ---------------------------------------------------------------------------LEQFT 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 243 APEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQkyhvRRKILDNVSLPLVLELpvkRTSLSSLSEGw 322
Cdd:cd02661 173 KPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR----GGKINKQISFPETLDL---SPYMSQPNDG- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 323 sadadftdvnenlakklkpsgteeafcpkLVPYLLSSVVVHSGVSSESGHYYSYARNITGTessyqmrpqseslsltpsq 402
Cdd:cd02661 245 -----------------------------PLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGK------------------- 276
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746614 403 ssllggespntvieqdlenkemsqeWFLFNDSRVTFTSFQSVQkitsrfpKDTAYVLFY 461
Cdd:cd02661 277 -------------------------WYNMDDSKVSPVSIETVL-------SQKAYILFY 303
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
4-466 |
3.80e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 85.77 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 4 LQHLFAFLAHTQREAYAPRIFFEASRPPWFT--PRSQQDCSEYLRFLLDRLheEEKilriqsshkpseglgctetclqev 81
Cdd:cd02659 50 LQRLFLFLQLSESPVKTTELTDKTRSFGWDSlnTFEQHDVQEFFRVLFDKL--EEK------------------------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 82 tnkvavpseSPSTGgsEKTLIEKMFGGKLRTHICCLNCRSTSHKVEAFTDLSLAFCPSPSVEDSsFQDpaslpsaqddgl 161
Cdd:cd02659 104 ---------LKGTG--QEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEES-LDA------------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 162 mqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsppvefpcaknssvpgesakilvskdvpqnpggesttsvtdllnyF 241
Cdd:cd02659 160 -------------------------------------------------------------------------------Y 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 242 LAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLEL-PVKRTSLSSLSE 320
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMePYTEKGLAKKEG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 321 GWSADADFTDVNEnLAKKLKPSGTEEAfcpklvpyllssvvvhsgvssesGHYYSYARNITgtessyqmrpqseslsltp 400
Cdd:cd02659 241 DSEKKDSESYIYE-LHGVLVHSGDAHG-----------------------GHYYSYIKDRD------------------- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 401 sqssllggespntvieqdlenkemSQEWFLFNDSRVTFTSFQSV--------------QKITSRFPKDT-AYVLFYKKQS 465
Cdd:cd02659 278 ------------------------DGKWYKFNDDVVTPFDPNDAeeecfggeetqktyDSGPRAFKRTTnAYMLFYERKS 333
|
.
gi 1958746614 466 R 466
Cdd:cd02659 334 P 334
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
38-309 |
3.56e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 82.36 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 38 QQDCSEYLRFLLDRLHEeekilriqsshkpseglgctetCLQEVTNKVAVPSESPSTGGSE--KTLIEKMFGGKLRTHIC 115
Cdd:cd02663 65 HQDAHEFLNFLLNEIAE----------------------ILDAERKAEKANRKLNNNNNAEpqPTWVHEIFQGILTNETR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 116 CLNCRSTSHKVEAFTDLSLafcpspsvedssfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlg 195
Cdd:cd02663 123 CLTCETVSSRDETFLDLSI------------------------------------------------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 196 sppvefpcaknssvpgesakilvskDVPQNpggestTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPE 275
Cdd:cd02663 142 -------------------------DVEQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPK 190
|
250 260 270
....*....|....*....|....*....|....
gi 1958746614 276 YLILTLLRFSYDQKYHVRRKILDNVSLPLVLELP 309
Cdd:cd02663 191 ILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-308 |
6.80e-15 |
|
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: 75.92 E-value: 6.80e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746614 231 TTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLEL 308
Cdd:cd02668 155 HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDM 232
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
38-462 |
6.60e-14 |
|
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: 71.16 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 38 QQDCSEYLRFLLDRLHeeekilriqsshkpseglgctetclqevtnkvavpsespstggsekTLIEKMFGGKLRTHICCL 117
Cdd:cd02674 22 QQDAQEFLLFLLDGLH----------------------------------------------SIIVDLFQGQLKSRLTCL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 118 NCRSTSHKVEAFTDLSLAfcpspsvedssfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsp 197
Cdd:cd02674 56 TCGKTSTTFEPFTYLSLP-------------------------------------------------------------- 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 198 pvefpcaknssvpgesakilvskdVPQNPGGESTTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYL 277
Cdd:cd02674 74 ------------------------IPSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVL 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 278 ILTLLRFSYDQKYhvRRKILDNVSLPLvlelpvkrtSLSSLSEgWSADADFTDVNE-NLAKKLKPSGTEEAfcpklvpyl 356
Cdd:cd02674 130 IIHLKRFSFSRGS--TRKLTTPVTFPL---------NDLDLTP-YVDTRSFTGPFKyDLYAVVNHYGSLNG--------- 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 357 lssvvvhsgvssesGHYYSYARNitgtessyqmrpqseslsltpsqssllggespntvieqdlenkEMSQEWFLFNDSRV 436
Cdd:cd02674 189 --------------GHYTAYCKN-------------------------------------------NETNDWYKFDDSRV 211
|
410 420
....*....|....*....|....*.
gi 1958746614 437 TFTSFQSVQkitsrfpKDTAYVLFYK 462
Cdd:cd02674 212 TKVSESSVV-------SSSAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
37-462 |
3.17e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 67.78 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 37 SQQDCSEYLRFLLDRLHEEEKILRIQSSHKPSeglgCTetCLqevtnkvavpsespstggsektlIEKMFGGKLRTHICC 116
Cdd:cd02660 87 SQQDAHEFFQFLLDQLHTHYGGDKNEANDESH----CN--CI-----------------------IHQTFSGSLQSSVTC 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 117 LNCRSTSHKVEAFTDLSLAFcpspsvedssfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgs 196
Cdd:cd02660 138 QRCGGVSTTVDPFLDLSLDI------------------------------------------------------------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 197 ppvefpcaKNSSVPGESAKILvskdvpqnpGGESTTSVTDLLNYFLAPEVLtGENQYYCESCASLQNAEKTMQITEEPEY 276
Cdd:cd02660 158 --------PNKSTPSWALGES---------GVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 277 LILTLLRFSYDQkYHVRRKILDNVSLPLVLELpvkrTSLSSLSEGWSADADFtdvnenlakkLKPSGTEEAFcpKLVPYl 356
Cdd:cd02660 220 LCFQLKRFEHSL-NKTSRKIDTYVQFPLELNM----TPYTSSSIGDTQDSNS----------LDPDYTYDLF--AVVVH- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 357 lssvvvhsGVSSESGHYYSYARNITGtessyqmrpqseslsltpsqssllggespntvieqdlenkemsqEWFLFNDSRV 436
Cdd:cd02660 282 --------KGTLDTGHYTAYCRQGDG--------------------------------------------QWFKFDDAMI 309
|
410 420
....*....|....*....|....*.
gi 1958746614 437 TFTSFQSVQKitSRfpkdtAYVLFYK 462
Cdd:cd02660 310 TRVSEEEVLK--SQ-----AYLLFYH 328
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
21-461 |
8.81e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 65.87 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 21 PRIFFE--ASRPPWFTPRSQQDCSEYLRFLLDRLheeekilriqsshkpseglgctetclqevtnkvavpsespstggse 98
Cdd:cd02667 32 PKELFSqvCRKAPQFKGYQQQDSHELLRYLLDGL---------------------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 99 KTLIEKMFGGKLRTHICCLNCRSTSHKVEAFTDLSLafcpsPSVEDSsfqdpaslpsaqddglmqtsvtdaeeepvvcnp 178
Cdd:cd02667 66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL-----PRSDEI--------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 179 aaaafvcdsvvnerrlgsppvefpcaknssvpgesakilvskdvpqnpggESTTSVTDLLNYFLAPEVLTGENQYYCESC 258
Cdd:cd02667 108 --------------------------------------------------KSECSIESCLKQFTEVEILEGNNKFACENC 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 259 aslQNAEKTMQITEEPEYLILTLLRFSYDQKyHVRRKILDNVSLPLVLELpvkrtslsslsegwsadADFTDVNENLAKk 338
Cdd:cd02667 138 ---TKAKKQYLISKLPPVLVIHLKRFQQPRS-ANLRKVSRHVSFPEILDL-----------------APFCDPKCNSSE- 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 339 lkpsgTEEAFCPKLVPYLlssvvvHSGVSSESGHYYSYARnitgtessyqMRPQSESLSLTPSQSsllggespntviEQD 418
Cdd:cd02667 196 -----DKSSVLYRLYGVV------EHSGTMRSGHYVAYVK----------VRPPQQRLSDLTKSK------------PAA 242
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958746614 419 LENKEMSQEWFLFNDSRVtftsfQSVQkiTSRFPKDTAYVLFY 461
Cdd:cd02667 243 DEAGPGSGQWYYISDSDV-----REVS--LEEVLKSEAYLLFY 278
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
229-465 |
4.44e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 62.59 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 229 ESTTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYhvRRKILDNVSLPLvlel 308
Cdd:COG5560 672 ERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPI---- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 309 pvkrtslsslsegwsadadftdvnenlaKKLKPSGTEEAFCPKLVPYLLsSVVVHSGVSSESGHYYSYARNITgtessyq 388
Cdd:COG5560 746 ----------------------------DDLDLSGVEYMVDDPRLIYDL-YAVDNHYGGLSGGHYTAYARNFA------- 789
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746614 389 mrpqseslsltpsqssllggespntvieqdlenkemSQEWFLFNDSRVTFTSfqSVQKITSrfpkdTAYVLFYKKQS 465
Cdd:COG5560 790 ------------------------------------NNGWYLFDDSRITEVD--PEDSVTS-----SAYVLFYRRKS 823
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
212-308 |
1.96e-05 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 47.56 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 212 ESAKILVSKDVPQNPGGESTtsVTDLLNYFLAPEVLTGENQYYCEScASLQNAEKTMQITEEPEYLILTLLRFSYDQKYH 291
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMKN--LQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERD 396
|
90
....*....|....*..
gi 1958746614 292 VRRKILDNVSLPLVLEL 308
Cdd:COG5077 397 MMVKINDRYEFPLEIDL 413
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
208-304 |
1.03e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 41.42 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746614 208 SVP---GESAKILVSKDVPQNPGGESTTsVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRF 284
Cdd:cd02671 154 SVPvqeSELSKSEESSEISPDPKTEMKT-LKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCF 232
|
90 100
....*....|....*....|
gi 1958746614 285 SYDQKYHVRRKILDNVSLPL 304
Cdd:cd02671 233 AANGSEFDCYGGLSKVNTPL 252
|
|
| |
