|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1092-1449 |
2.71e-150 |
|
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: 467.50 E-value: 2.71e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1092 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1168
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1169 KELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1248
Cdd:cd02659 79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1249 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVAGMARQ 1328
Cdd:cd02659 159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1329 DsssevgengrnmdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 1408
Cdd:cd02659 239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958776447 1409 LEYECFGGEYRPKVYDqtnPYPDVRRRYWNAYMLFYQRVSD 1449
Cdd:cd02659 297 AEEECFGGEETQKTYD---SGPRAFKRTTNAYMLFYERKSP 334
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1094-1444 |
1.21e-66 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 228.48 E-value: 1.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1094 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDN----PDDSVFYQVQSLFGHL-MESKLQYYVPENFWKIFKMWN 1168
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrynKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1169 KELYVREQQDAYEFFTSLIDQMDEYLKKMG---REQIFKNTFQGIYSDQKICKDCPHRYEREEAFMAL------NLGVTS 1239
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgDSAELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1240 CQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESgrSIKYDEQIRFPWMLNMEP 1319
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1320 YTVAGMArqdsssevgengrnmdqggggsprKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVI 1399
Cdd:pfam00443 239 YLAEELK------------------------PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAY---ENNRWYKFDDEKV 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958776447 1400 EEFDLNDETLEyecfggeyrpkvydqtnpypdvrrryWNAYMLFY 1444
Cdd:pfam00443 292 TEVDEETAVLS--------------------------SSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1095-1445 |
1.58e-59 |
|
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: 205.79 E-value: 1.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYMQpglpesllsvdddtdnpddsvfyqvqslfghlmesklqyyvpenfwkifkmwnkelyvr 1174
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1175 eQQDAYEFFTSLIDQMDEYLKKMGR--------EQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGV----TSCQS 1242
Cdd:cd02257 22 -QQDAHEFLLFLLDKLHEELKKSSKrtsdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1243 LEISLDQFVRGEVLEGSNAYYCEKCKeKRITVKRTCIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLNMEPYTV 1322
Cdd:cd02257 101 LEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPYLS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1323 AGMARQDSSSEVGengrnmdqggggsprkkvalteNYELVGVIVHSGQ-AHAGHYYSFIKDRrgcGKGKWYKFNDTVIEE 1401
Cdd:cd02257 179 EGEKDSDSDNGSY----------------------KYELVAVVVHSGTsADSGHYVAYVKDP---SDGKWYKFNDDKVTE 233
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958776447 1402 FDLNDETleyecfggeyrpkvydqtnpypDVRRRYWNAYMLFYQ 1445
Cdd:cd02257 234 VSEEEVL----------------------EFGSLSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1444 |
1.01e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 177.23 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDS-----------VFYQVQSLFGHLMESKLQYYVPENFWKI 1163
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmppdkphepqtIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1164 FkmwnkELYVREQQDAYEF---FTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSC 1240
Cdd:cd02668 81 L-----GLDTGQQQDAQEFsklFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1241 QSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPY 1320
Cdd:cd02668 156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1321 tvagMARQDSSSEVgengrnmdqggggsprkkvaltenYELVGVIVHSGQ-AHAGHYYSFIKDRRgcgKGKWYKFNDTVI 1399
Cdd:cd02668 236 ----LAESDEGSYV------------------------YELSGVLIHQGVsAYSGHYIAHIKDEQ---TGEWYKFNDEDV 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1400 EE-----FDLNDETLEYECFGGEYRPKVYDQTnpypdvrrrywNAYMLFY 1444
Cdd:cd02668 285 EEmpgkpLKLGNSEDPAKPRKSEIKKGTHSSR-----------TAYMLVY 323
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1444 |
4.20e-44 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 163.22 E-value: 4.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDS--VFYQVQSLFGHLMESKLQYYVPENFWKIFKMWNKELY 1172
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1173 VREQQDAYEFFTSLIDQM-----DEYLKKMGREQIFKNT------FQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQ 1241
Cdd:cd02661 83 IGRQEDAHEFLRYLLDAMqkaclDRFKKLKAVDPSSQETtlvqqiFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1242 SLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFdwesGRSIKYDEQIRFPWMLNMEPYt 1321
Cdd:cd02661 163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN----FRGGKINKQISFPETLDLSPY- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1322 vagmarqdsssevgengrnMDQGGGGSPRkkvaltenYELVGVIVHSG-QAHAGHYYSFIKDRRgcgkGKWYKFNDTVIE 1400
Cdd:cd02661 238 -------------------MSQPNDGPLK--------YKLYAVLVHSGfSPHSGHYYCYVKSSN----GKWYNMDDSKVS 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958776447 1401 EFDLNDetleyecfggeyrpkVYDQtnpypdvrrrywNAYMLFY 1444
Cdd:cd02661 287 PVSIET---------------VLSQ------------KAYILFY 303
|
|
| Ubl_UBP24 |
cd17065 |
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ... |
360-438 |
4.18e-43 |
|
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain.
Pssm-ID: 340585 Cd Length: 79 Bit Score: 151.69 E-value: 4.18e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776447 360 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQVLTVK 438
Cdd:cd17065 1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1444 |
7.05e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 154.84 E-value: 7.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV--------------FYQVQSLFGHLMESKLQyyvpeNF 1160
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsclscamdeifqeFYYSGDRSPYGPINLLY-----LS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1161 WKIfkmwNKELYVREQQDAYEFFTSLIDQM--------DEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMA 1232
Cdd:cd02660 77 WKH----SRNLAGYSQQDAHEFFQFLLDQLhthyggdkNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1233 LNL---------------GVTSCQSLEISLDQFVRGEVLeGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDw 1297
Cdd:cd02660 153 LSLdipnkstpswalgesGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1298 ESGRSIKYDEQIRFPWMLNMEPYTVAGMARQDSSSEVgengrnmdqggggSPRKKvaltenYELVGVIVHSGQAHAGHYY 1377
Cdd:cd02660 231 LNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSL-------------DPDYT------YDLFAVVVHKGTLDTGHYT 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776447 1378 SFIKDrrgcGKGKWYKFNDTVIEEFDLNDetleyecfggeyrpkVYDQtnpypdvrrrywNAYMLFY 1444
Cdd:cd02660 292 AYCRQ----GDGQWFKFDDAMITRVSEEE---------------VLKS------------QAYLLFY 327
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1086-1546 |
5.20e-40 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 162.73 E-value: 5.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1086 DSRSISGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPEnFWKIFk 1165
Cdd:COG5077 186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTE-LTRSF- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1166 MWNKELYVReQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEI 1245
Cdd:COG5077 264 GWDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1246 SLDQFVRGEVLEGSNAYYCEK--CKEKRitvKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVA 1323
Cdd:COG5077 343 SFRRYIQVETLDGDNRYNAEKhgLQDAK---KGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDR 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1324 GMARQDSSSEVgengrnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFD 1403
Cdd:COG5077 420 DADKSENSDAV------------------------YVLYGVLVHSGDLHEGHYYALLKPEK---DGRWYKFDDTRVTRAT 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1404 LNdETLEyECFGGE--YRPKVYDQTNPypdvrRRYWNAYMLFYqrvsdqnspvlpkksrvsvVRQEAEDLSLSAPSSPEI 1481
Cdd:COG5077 473 EK-EVLE-ENFGGDhpYKDKIRDHSGI-----KRFMSAYMLVY-------------------LRKSMLDDLLNPVAAVDI 526
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776447 1482 SPQSSPRphrpnndrlsiLTKLVKKGEKKGLfvEKMPARIYQMVRDENLKFMKNRDVYssDYFSF 1546
Cdd:COG5077 527 PPHVEEV-----------LSEEIDKTEVRCK--EIDEIHLYRGVRLYTIDSFIHYHGF--DYPDF 576
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1445 |
1.57e-37 |
|
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: 143.99 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYmqpglpesllsvdddtdnpDDSVFYQVQSLFGHLMESKLQYYV--PENFWKIFKMWNKELY 1172
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY-------------------FENLLTCLKDLFESISEQKKRTGVisPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1173 VREQQDAYEFFTSLIDQMDEYL---KKMGREQIFKNT--------------FQGIYSDQKICKDCPHRYEREEAFMALNL 1235
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIAEILdaeRKAEKANRKLNNnnnaepqptwvheiFQGILTNETRCLTCETVSSRDETFLDLSI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1236 GVTSCQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWML 1315
Cdd:cd02663 142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1316 NMEpytvagmarqdSSSEVGENGRNMdqggggsprkkvaltenYELVGVIVHSGQ-AHAGHYYSFIKDrrgcgKGKWYKF 1394
Cdd:cd02663 222 RLF-----------NTTDDAENPDRL-----------------YELVAVVVHIGGgPNHGHYVSIVKS-----HGGWLLF 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958776447 1395 NDTVIEEFDlnDETLEYecFggeyrpkVYDQTNPYpdvrrrywNAYMLFYQ 1445
Cdd:cd02663 269 DDETVEKID--ENAVEE--F-------FGDSPNQA--------TAYVLFYQ 300
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1445 |
4.16e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 137.42 E-value: 4.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVfqqlymqpglpesllsvdddtdnpddsvfyqVQSLFGHlmesklqyyvpenfwkifkmwnkelyvr 1174
Cdd:cd02674 1 GLRNLGNTCYMNSI-------------------------------LQCLSAD---------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1175 eQQDAYEFFTSLIDQMDeylkkmgreQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNL------GVTSCQSLEISLD 1248
Cdd:cd02674 22 -QQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLpipsgsGDAPKVTLEDCLR 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1249 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDweSGRSIKYDEQIRFPW-MLNMEPYtvagmar 1327
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPLnDLDLTPY------- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1328 qdsssevgengrnMDQGGGGSPRKkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDE 1407
Cdd:cd02674 163 -------------VDTRSFTGPFK-------YDLYAVVNHYGSLNGGHYTAYCKNNE---TNDWYKFDDSRVTKVSESSV 219
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958776447 1408 tleyecfggeyrpkvydQTNpypdvrrrywNAYMLFYQ 1445
Cdd:cd02674 220 -----------------VSS----------SAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1406 |
5.72e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 137.62 E-value: 5.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENfwKIFK-MWNKELYV 1173
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD--YFLEaSRPPWFTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1174 REQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLeisLDQFVRG 1253
Cdd:cd02664 79 GSQQDCSEYLRYLLDRLHTLIEKM---------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL---LNYFLSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1254 EVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIK------YDEQIRFPwmlnmepytvagMAR 1327
Cdd:cd02664 147 EKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKimdnvsINEVLSLP------------VRV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1328 QDSSSEVGENGRNMDQGGGGSprkKVALTENYELVGVIVHSG-QAHAGHYYSF---IKDRRGCGK--------------G 1389
Cdd:cd02664 215 ESKSSESPLEKKEEESGDDGE---LVTRQVHYRLYAVVVHSGySSESGHYFTYardQTDADSTGQecpepkdaeendesK 291
|
330
....*....|....*..
gi 1958776447 1390 KWYKFNDTVIEEFDLND 1406
Cdd:cd02664 292 NWYLFNDSRVTFSSFES 308
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1445 |
5.39e-29 |
|
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: 118.64 E-value: 5.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDtdnpddsvfyqvqsLFGHLMESKLQYyvpenfwKIFKmwnkelyvr 1174
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAPQF-------KGYQ--------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1175 eQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEIS----LDQF 1250
Cdd:cd02667 51 -QQDSHELLRYLLDGLRTFIDSI---------FGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSECSiescLKQF 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1251 VRGEVLEGSNAYYCEKCKEKRitvKRTCIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLNMEPYtvagMARQDS 1330
Cdd:cd02667 121 TEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPF----CDPKCN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1331 SSEVGENGRnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDR------------------RGCGKGKWY 1392
Cdd:cd02667 193 SSEDKSSVL-------------------YRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltkskpaadeAGPGSGQWY 253
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958776447 1393 KFNDTVIEEFDLnDETLEYEcfggeyrpkvydqtnpypdvrrrywnAYMLFYQ 1445
Cdd:cd02667 254 YISDSDVREVSL-EEVLKSE--------------------------AYLLFYE 279
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1445 |
3.43e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 111.26 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYmqpGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLmeSKL-------QYYVPENFW------ 1161
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLF---SIPSFQWRYDDLENKFPSDVVDPANDLNCQL--IKLadgllsgRYSKPASLKsendpy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1162 ------KIFKM----WNKELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIysDQKI-CKDCPHRY--EREE 1228
Cdd:cd02658 76 qvgikpSMFKAligkGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPNDLFKFMI--EDRLeCLSCKKVKytSELS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1229 AFMALNL------------GVTSCQSLEISLDQFVRGEVLEgsnaYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGF- 1295
Cdd:cd02658 154 EILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLl 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1296 -DWesgRSIKYDEQIRFPWMLnmepytvagmarqdsssevgengrnmdqGGGgsprkkvalteNYELVGVIVHSG-QAHA 1373
Cdd:cd02658 230 eNW---VPKKLDVPIDVPEEL----------------------------GPG-----------KYELIAFISHKGtSVHS 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776447 1374 GHYYSFIKdRRGCGKGKWYKFNDTvieefdlndetleyecfggeyrpKVYDQTNPyPDVRRrywNAYMLFYQ 1445
Cdd:cd02658 268 GHYVAHIK-KEIDGEGKWVLFNDE-----------------------KVVASQDP-PEMKK---LGYIYFYQ 311
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1396 |
7.15e-19 |
|
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: 89.70 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQV---QSLFGHlMESKLQYYVPENFWKIF------- 1164
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTnalRDLFDT-MDKKQEPVPPIEFLQLLrmafpqf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1165 -KMWNKELYvrEQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKI-CKDCPHRYE---REEAFMALNLGVTS 1239
Cdd:cd02657 80 aEKQNQGGY--AQQDAEECWSQLLSVLSQKLPGAGSKGSFIDQLFGIELETKMkCTESPDEEEvstESEYKLQCHISITT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1240 -CQSLEISLDQFVRGEVLEGSnayycEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNME 1318
Cdd:cd02657 158 eVNYLQDGLKKGLEEEIEKHS-----PTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLY 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776447 1319 PYtvagmarqdsssevgengrnmdqggggsprkkVALTENYELVGVIVHSGQ-AHAGHYYSFIKDRrgcGKGKWYKFND 1396
Cdd:cd02657 233 EL--------------------------------CTPSGYYELVAVITHQGRsADSGHYVAWVRRK---NDGKWIKFDD 276
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1445 |
4.70e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 82.80 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVdddtdnpddsvfyqvqslfghlmesklqyyvpenfwkifkmwnkelyvR 1174
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF------------------------------------------------L 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1175 EQQDAYEFFTSLIDQMdeylkkmgrEQIFKNTFQGIYSDQKICKDCPHRYE-REEAFMALNLGV-----TSCQSLEISLD 1248
Cdd:cd02662 33 EQQDAHELFQVLLETL---------EQLLKFPFDGLLASRIVCLQCGESSKvRYESFTMLSLPVpnqssGSGTTLEHCLD 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1249 QFVRGEVLEGsnaYYCEKCKEKritvkrtcIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLnmepytvagmarq 1328
Cdd:cd02662 104 DFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERL------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1329 dsssevgengrnmdqggggsPRKKvaltenYELVGVIVHSGQAHAGHYYSF-----------------IKDRRGCGKGKW 1391
Cdd:cd02662 159 --------------------PKVL------YRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrMREGPSSTSHPW 212
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958776447 1392 YKFNDTVIEEFDLNDETLEYEcfggeyrpkvydqtnpypdvrrrywnAYMLFYQ 1445
Cdd:cd02662 213 WRISDTTVKEVSESEVLEQKS--------------------------AYMLFYE 240
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1070-1403 |
1.14e-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 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: 83.40 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1070 QPDPALT-KEFDYLPPvdsrsisgFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDdsvfyQVQSLFGHLM 1148
Cdd:cd02671 8 QPSSATScEKRENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVE-----QLQSSFLLNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1149 E---SKLQYYVPENFWKIFKMWNKELYVREQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKICKDCPHRYE 1225
Cdd:cd02671 75 EkynDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEKD---------FQGQLVLRTRCLECETFTE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1226 REEAFMALNLGV------TSCQSLEISLD-------------QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVL 1286
Cdd:cd02671 146 RREDFQDISVPVqeselsKSEESSEISPDpktemktlkwaisQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1287 VIHLMRFG-----FDWESGRSiKYDEQIRFPWMLNMEpytvagmarqdsssevgengrnmdqGGGGSPRKKValtenYEL 1361
Cdd:cd02671 226 TIHLKCFAangseFDCYGGLS-KVNTPLLTPLKLSLE-------------------------EWSTKPKNDV-----YRL 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958776447 1362 VGVIVHSG-QAHAGHYYSFIkdrrgcgkgKWYKFNDT---VIEEFD 1403
Cdd:cd02671 275 FAVVMHSGaTISSGHYTAYV---------RWLLFDDSevkVTEEKD 311
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1094-1399 |
1.36e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 73.84 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1094 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENFWKIFKMW--NKEL 1171
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIpeASAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1172 ----YVREQQDAyEFFTSLI--------DQM-DEYLKKMGREQ----IFKNTFQGIYSDQKICKDCPHRYEREEAFMALN 1234
Cdd:pfam13423 81 glldEDRETNSA-ISLSSLIqsfnrfllDQLsSEENSTPPNPSpaesPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1235 L--------------GVTSCQSLEISLDQfvrgevlEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESG 1300
Cdd:pfam13423 160 LiyprkpssnnkkppNQTFSSILKSSLER-------ETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1301 RSIKydeqirfPWmLNMEPYTVagmarqdsssevgengrnMDQGGGGSPRKKValtenYELVGVIVH-SGQAHAGHYYSF 1379
Cdd:pfam13423 233 WKTP-------GW-LPPEIGLT------------------LSDDLQGDNEIVK-----YELRGVVVHiGDSGTSGHLVSF 281
|
330 340
....*....|....*....|....
gi 1958776447 1380 IK----DRRGCGKGKWYKFNDTVI 1399
Cdd:pfam13423 282 VKvadsELEDPTESQWYLFNDFLV 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1242-1448 |
3.11e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 75.30 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1242 SLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRfgFDWESGRSIKYDEQIRFPWM-LNMEPY 1320
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPIDdLDLSGV 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1321 TVAGMarqdsSSEVGengrnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDrrgCGKGKWYKFNDTVIE 1400
Cdd:COG5560 754 EYMVD-----DPRLI-----------------------YDLYAVDNHYGGLSGGHYTAYARN---FANNGWYLFDDSRIT 802
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958776447 1401 EFDLNDETLEyecfggeyrpkvydqtnpypdvrrrywNAYMLFYQRVS 1448
Cdd:COG5560 803 EVDPEDSVTS---------------------------SAYVLFYRRKS 823
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1095-1396 |
1.88e-11 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 67.13 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQL-YMQPGLPESLLsvdddTDNPDDSVFYQV-----QSLFGHLMESKLQYYVPENFWKIFKMWN 1168
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLD-----DLSKELKVLKNVirkpePDLNQEEALKLFTALWSSKEHKVGWIPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1169 KElyvrEQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTfqgiysdqkicKDCPHRYEREeaFMALNLGVTSCQSLEIS-- 1246
Cdd:COG5533 76 MG----SQEDAHELLGKLLDELKLDLVNSFTIRIFKTT-----------KDKKKTSTGD--WFDIIIELPDQTWVNNLkt 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1247 LDQFvrgevLEGSNAYYCEKC-------KEKRITVKR---TCIKSLPSVLVIHLMRFGFDwesGRSIKYDEQIRfpwmln 1316
Cdd:COG5533 139 LQEF-----IDNMEELVDDETgvkakenEELEVQAKQeyeVSFVKLPKILTIQLKRFANL---GGNQKIDTEVD------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1317 mEPYTVAgmARQDSSSEVGENGRnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDrrgcgKGKWYKFND 1396
Cdd:COG5533 205 -EKFELP--VKHDQILNIVKETY-------------------YDLVGFVLHQGSLEGGHYIAYVKK-----GGKWEKAND 257
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1095-1423 |
3.07e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 62.58 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1095 GLRNGGATCYMNAVFQQLYMQpglpesllsvdddtdnpddsvfyqvqslfghlmesklQYYVPENFWKIFKmWnkelyvr 1174
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLFSQ-------------------------------------QQDVSEFTHLLLD-W------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1175 eQQDAYEFFTSLIDQMDEYLKKMgrEQIFKNTF--QGIYSDQKICKDcphryereEAFMALNLGVTSCQSLEISLD-QFV 1251
Cdd:cd02665 36 -LEDAFQAAAEAISPGEKSKNPM--VQLFYGTFltEGVLEGKPFCNC--------ETFGQYPLQVNGYGNLHECLEaAMF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1252 RGEVlEGSNAYYCEKCKEKRITVKrtciksLPSVLVIHLMRFGFDweSGRSIKYDEQIRFPWMLNMEPYtvagmarqdss 1331
Cdd:cd02665 105 EGEV-ELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFN--QGRPEKIHDKLEFPQIIQQVPY----------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1332 sevgengrnmdqggggsprkkvaltenyELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLndETLEY 1411
Cdd:cd02665 165 ----------------------------ELHAVLVHEGQANAGHYWAYIYKQS---RQEWEKYNDISVTESSW--EEVER 211
|
330
....*....|..
gi 1958776447 1412 ECFGGEYRPKVY 1423
Cdd:cd02665 212 DSFGGGRNPSAY 223
|
|
| Ubl_ubiquitin_like |
cd17039 |
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
367-437 |
6.12e-08 |
|
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.
Pssm-ID: 340559 [Multi-domain] Cd Length: 68 Bit Score: 51.44 E-value: 6.12e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776447 367 LNVTYESTKdTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLtvnKDQKLLHQLGFSDEQVLTV 437
Cdd:cd17039 1 ITVKTLDGK-TYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKEL---KDDKTLSDYGIKDGSTIHL 67
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1175-1445 |
1.86e-07 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 54.46 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1175 EQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKickdcphRYEREEAFMalnlgvtSCQSLEISLDQFVRGE 1254
Cdd:cd02670 22 EQQDPEEFFNFITDKLLMPLLEP---------KVDIIHGGK-------KDQDDDKLV-------NERLLQIPVPDDDDGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1255 VLEgsnayyCEKCKEKRITVKRtcIKSLPSVLVIHLMRFGfdWESGRSIKYDEQIRFPWMLNMePYTVAGMARQDS--SS 1332
Cdd:cd02670 79 GIT------LEQCLEQYFNNSV--FAKAPSCLIICLKRYG--KTEGKAQKMFKKILIPDEIDI-PDFVADDPRACSkcQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1333 EVGENGRNMDQGGGGSPRKKValtenyeLVGVIVHSGQA-HAGHYYSFIK--------DRRGCGKGKWYKFNDtvieefd 1403
Cdd:cd02670 148 ECRVCYDDKDFSPTCGKFKLS-------LCSAVCHRGTSlETGHYVAFVRygsyslteTDNEAYNAQWVFFDD------- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958776447 1404 LNDetleyecfggeyRPKVYDQTNpYPDVRRRYWnAYMLFYQ 1445
Cdd:cd02670 214 MAD------------RDGVSNGFN-IPAARLLED-PYMLFYQ 241
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1359-1409 |
2.59e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 51.72 E-value: 2.59e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958776447 1359 YELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVIEEFDLNDETL 1409
Cdd:cd02666 281 YRLHAVFIHRGEASSGHYWVYIKDF---EENVWRKYNDETVTVVPASEVFL 328
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1241-1412 |
5.55e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 44.04 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1241 QSLEISLDQFVrgevlegSNAYYCEKCKEKRITVKRTCIKSLP----SVLVIHLMRFGfdweSGRSIKYDEQIRFPWMLN 1316
Cdd:cd02672 121 QLLKRSLDLEK-------VTKAWCDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTN----GEFDDINVVLPSGKVMQN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1317 MEPYtvagmARQDSSSEVGENGRNMdqggggsprkkvalTENYELVGVIVH-SGQAHAGHYYSF-IKDRRGCGKGKWYKF 1394
Cdd:cd02672 190 KVSP-----KAIDHDKLVKNRGQES--------------IYKYELVGYVCEiNDSSRGQHNVVFvIKVNEESTHGRWYLF 250
|
170
....*....|....*...
gi 1958776447 1395 NDTVIEEFDLNDETLEYE 1412
Cdd:cd02672 251 NDFLVTPVSELAYILLYQ 268
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1092-1197 |
2.37e-03 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 42.95 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1092 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLS---VDDDTDNPDDSVFYQVQSLFGHLMES----KLQYYVPENFWKIF 1164
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSdeyEESINEENPLGMHGSVASAYADLIKQlydgNLHAFTPSGFKKTI 343
|
90 100 110
....*....|....*....|....*....|...
gi 1958776447 1165 KMWNKELYVREQQDAYEFFTSLIDQMDEYLKKM 1197
Cdd:COG5560 344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI 376
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1054-1401 |
2.44e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 42.69 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1054 PSNLQIITKELLSMHHQPDPALTKE----FDYLPPV-----DSRSISGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLS 1124
Cdd:cd02669 71 PDNYEIIDSSLDDIKYVLNPTYTKEqisdLDRDPKLsrdldGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1125 V-DDDTDNPDDSVFYQVQS-LFGHLMESKL--QYYVPENFWKIFKMW-NKELYVREQQDAYEFFTSLIDQMDEYLKKMGR 1199
Cdd:cd02669 151 YeNYENIKDRKSELVKRLSeLIRKIWNPRNfkGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1200 --EQIFKNTFQG---IYSdQKIckdcPHRYEREEAFMALNLGVTSCQS-----LEISLD-----------------QFVR 1252
Cdd:cd02669 231 pnSSIIHDCFQGkvqIET-QKI----KPHAEEEGSKDKFFKDSRVKKTsvspfLLLTLDlpppplfkdgneeniipQVPL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776447 1253 GEVLEGsnaYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFgfdwESGRSIKYDEQ--IRFPWMLNMEPYTVAGMARQDS 1330
Cdd:cd02669 306 KQLLKK---YDGKTETELKDSLKRYLISRLPKYLIFHIKRF----SKNNFFKEKNPtiVNFPIKNLDLSDYVHFDKPSLN 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776447 1331 SSevgengrnmdqggggsprkkvaltENYELVGVIVHSGQAH-AGHYYSFIKDRrgcGKGKWYKFNDTVIEE 1401
Cdd:cd02669 379 LS------------------------TKYNLVANIVHEGTPQeDGTWRVQLRHK---STNKWFEIQDLNVKE 423
|
|
| Ubl_AtNPL4_like |
cd17055 |
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ... |
374-428 |
8.83e-03 |
|
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins; The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2.
Pssm-ID: 340575 Cd Length: 73 Bit Score: 36.81 E-value: 8.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776447 374 TKD-TFTVEAHSNETIGSVRWKIAKQLCSPVDNIQI--FTNDSLLTvNKDQKLLHQLG 428
Cdd:cd17055 7 SRDgTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLslDPGPDLLT-AKSSATLSQLG 63
|
|
| |
