|
Name |
Accession |
Description |
Interval |
E-value |
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1-1229 |
0e+00 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 1580.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 1 MSSEDELGSIGTVFPGSPiDKSIGSILPQFDEEVETLLEDSFTWNIPDWNELTNpKYNSPRFRIGDFEWDILLFPQGNHN 80
Cdd:COG5077 1 MSSEDELGSIGEVFPGSP-DKSIGSILPQFDPDVEELLEMSFTWKVKRWSELAK-KVESPPFSVGGHTWKIILFPQGNNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 81 KGVAVYLEPHPEEkLDETTGEmvpvdpDWYCCAQFAIGISRPGNgDTINLINKSHHRFNALDTDWGFANLIDLNNLKHPS 160
Cdd:COG5077 79 CNVSVYLEYEPQE-LEETGGK------YYDCCAQFAFDISNPKY-PTIEYINKSHHRFSMESTDWGFTNFIDLNKLIEPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 161 KGRPlSFLNEGTLNITAYVRILKDPTGVLWHNFLNYDSKKVTGYVGFRNQGATCYLNSLLQSYFFTKYFRKLVYEIPTEH 240
Cdd:COG5077 151 PGRP-PFLEEGTLVITVYVRVLKDPTGVLWHSFLNYNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 241 ESPNNSVPLALQRAFYQLQVSDIPLDTLELTRSFGWDTAESFTQHDVQELNRILMDRLENNMKGTPVEGKLNEIFVGKMK 320
Cdd:COG5077 230 PRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 321 SYIKCINVDYESARVEDFWDLQLNVKNFKNLQESFDNYIEMELMNGENQYAAQDYGLQDAQKGVIFESFPPVLHLQLKRF 400
Cdd:COG5077 310 SYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 401 EYDFNYDQMVKVNDKYEFPETIDLSPFVDKDVLKktldSENKDknpYVYNLHGVLVHSGDISTGHYYTLIKPGVEDQWYR 480
Cdd:COG5077 390 EYDFERDMMVKINDRYEFPLEIDLLPFLDRDADK----SENSD---AVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 481 FDDERVWRVTKKQVFQENFGCDRLPDEKVRTMTRdeyqnyiIQRHTSAYMLVYIRQEQEEDLLRPVLESDVPKHVITRVR 560
Cdd:COG5077 463 FDDTRVTRATEKEVLEENFGGDHPYKDKIRDHSG-------IKRFMSAYMLVYLRKSMLDDLLNPVAAVDIPPHVEEVLS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 561 EEIKERETKEKEIREAHLYVTLRLHSIKEFIHYEGFDYFAhdgfrlFAEELNDSGLQQINLKvlRTTKLSDIFASIKETM 640
Cdd:COG5077 536 EEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDYPD------FSSELNDSGLAQFVIK--RGAKISDLRNNIAEHL 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 641 NIPQERDVKYWKMDYRRNSTLRLTQPINfeSVNITLQEALKkekkrtMQTQYGEegvasteeddkallETVSFLDLFIEE 720
Cdd:COG5077 608 NTPQSLYLREWTMIKRHNKTVRVDRPCN--RVNITTRELVG------MNTRTGE--------------ELRSYLERIIEH 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 721 pylelqflnklkeasliskaqldDELISTIRTNLpeltkggiepvfaTDNKSNLLFVKSYDPHTQKLLGFGHFAVNQLQQ 800
Cdd:COG5077 666 -----------------------NQLDSQRKVAL-------------TKDGVINIFVKYFDYTTQPISGFGGLHVNKFLK 709
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 801 LSDLSAIIEDSISSNEKLTFYEEVQPGTINEIYMKETIYDADIDTGDIVSFEVPGAVLPDTFPVYATIKDFYSYLRYRVK 880
Cdd:COG5077 710 ISSISPWIEDSISSNLPLTLYEEIKPGMVDTIGDNITFIGSEIGTGDIICFEVPGAVEFDTSSAYDSALKLYDFLQGRVL 789
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 881 LKFSKFdgsSEEYGVSneipeSFEFWISAYAPYDDLARMVSKYAHVKPEYLKIFALYS---NGRFVLKSTS--LLNDYLL 955
Cdd:COG5077 790 VAFRRF---SDEYREN-----VFEFLLFIGDFYDDLCRNVSCKLHVTPFYLRGTKSTEledRIRRVVGSKSifLLKEALS 861
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 956 KDFNCDQIPPFAFEVLSVPLKELERLRPIKLYWLKNSYIHYQCFEFEVANDYTESQFLEKVQHKIGFTDEEKENILLWTN 1035
Cdd:COG5077 862 SSSEFRQAPVDFYEVLDVPLSELERKRLIRLCFLSNGYQHVYLAEFYVEKDYTAVDHLHIVVTKVGCTDELKKSVLVYEV 941
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 1036 TNFQFQGLLSDQNTFKDVSKNSLLFGRILPeesklfkelnrLENVQTSSLEDFmddenatdrpmddeqdlgmaiehsedm 1115
Cdd:COG5077 942 VNLRPVRGHSLKTLIIDDNVRSTLYGEVFP-----------LEQEQLTTNEMC--------------------------- 983
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 1116 kgriVVVQQYFKDLENRHGISFLFNLIPDETFPKTKDRLHAKFGLGQKEFSKIKLSIGYSTEEGTVFRSLQGFSDEEldk 1195
Cdd:COG5077 984 ----VVVQHFFKDLIRTHGIPFMFVIVPFETFLDTKVRLVARFGYKYKLFSKIKLFVGKSYTDGELDWPMSYFNDED--- 1056
|
1210 1220 1230
....*....|....*....|....*....|....
gi 767199261 1196 vILYDIMSNLDYIYMDHPDRLRSHSSYDRPMIIK 1229
Cdd:COG5077 1057 -ILYDLIERLDYILLDHPDRLRSHSSYDRAIIMK 1089
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
203-538 |
8.07e-159 |
|
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: 477.13 E-value: 8.07e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 203 GYVGFRNQGATCYLNSLLQSYFFTKYFRKLVYEIPTEHESPNN-SVPLALQRAFYQLQVSDIPLDTLEL---TRSFGWDT 278
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNkSVPLALQRLFLFLQLSESPVKTTELtdkTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 279 AESFTQHDVQELNRILMDRLENNMKGTPVEGKLNEIFVGKMKSYIKCINVDYESARVEDFWDLQLNVKNFKNLQESFDNY 358
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 359 IEMELMNGENQYAAQDYGLQ-DAQKGVIFESFPPVLHLQLKRFEYDFNYDQMVKVNDKYEFPETIDLSPFVDKDVLKKTL 437
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKvDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 438 DSENKDKNPYVYNLHGVLVHSGDISTGHYYTLIKPGVEDQWYRFDDERVWRVTKKQVFQENFGCDRLPDEKVRTMTRdey 517
Cdd:cd02659 241 DSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGEETQKTYDSGPRA--- 317
|
330 340
....*....|....*....|.
gi 767199261 518 qnyiIQRHTSAYMLVYIRQEQ 538
Cdd:cd02659 318 ----FKRTTNAYMLFYERKSP 334
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
205-533 |
1.43e-79 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 263.92 E-value: 1.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 205 VGFRNQGATCYLNSLLQSYFFTKYFRKLVYEIPTEHE----SPNNSVPLALQRAFYQLQ--VSDIPLDTLELTRSFGWDT 278
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEdsryNKDINLLCALRDLFKALQknSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 279 AE--SFTQHDVQELNRILMDRLENNMKG---TPVEGKLNEIFVGKMKSYIKCINVDYESARVEDFWDLQLNVKNFKNL-- 351
Cdd:pfam00443 81 PDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAElk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 352 -----QESFDNYIEMELMNGENQYAAQDYGLQDAQKGVIFESFPPVLHLQLKRFEYdfNYDQMVKVNDKYEFPETIDLSP 426
Cdd:pfam00443 161 taslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY--NRSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 427 FVDKDVLKKTldsenkdKNPYVYNLHGVLVHSGDISTGHYYTLIKPGVEDQWYRFDDERVWRVTKKQVFQEnfgcdrlpd 506
Cdd:pfam00443 239 YLAEELKPKT-------NNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS--------- 302
|
330 340
....*....|....*....|....*..
gi 767199261 507 ekvrtmtrdeyqnyiiqrhTSAYMLVY 533
Cdd:pfam00443 303 -------------------SSAYILFY 310
|
|
| MATH_Ubp21p |
cd03775 |
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ... |
40-180 |
5.89e-71 |
|
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with similarity to Ubp21p of fission yeast. Ubp21p is a deubiquitinating enzyme that may be involved in the regulation of the protein kinase Prp4p, which controls the formation of active spliceosomes. Members of this family are similar to human HAUSP (Herpesvirus-associated ubiquitin-specific protease) in that they contain an N-terminal MATH domain and a C-terminal catalytic protease (C19 family) domain. HAUSP is also an ubiquitin-specific protease that specifically catalyzes the deubiquitylation of p53 and MDM2. The MATH domain of HAUSP contains the binding site for p53 and MDM2. Similarly, the MATH domain of members in this family may be involved in substrate binding.
Pssm-ID: 239744 Cd Length: 134 Bit Score: 232.63 E-value: 5.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 40 DSFTWNIPDWNELtNPKYNSPRFRIGDFEWDILLFPQGNH-NKGVAVYLEPHPEEKLDEttgemvPVDPDWYCCAQFAIG 118
Cdd:cd03775 1 QSFTWRIKNWSEL-EKKVHSPKFKCGGFEWRILLFPQGNSqTGGVSIYLEPHPEEEEKA------PLDEDWSVCAQFALV 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767199261 119 ISRPGNgDTINLINKSHHRFNALDTDWGFANLIDLNNLKHPSKGRPLSFLNEGTLNITAYVR 180
Cdd:cd03775 74 ISNPGD-PSIQLSNVAHHRFNAEDKDWGFTRFIELRKLAHRTPDKPSPFLENGELNITVYVR 134
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
206-534 |
6.28e-60 |
|
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: 206.18 E-value: 6.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFFTkyfrklvyeiptehespnnsvplalqrafyqlqvsdipldtleltrsfgwdtaesftQH 285
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFSE---------------------------------------------------------QQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 286 DVQELNRILMDRLENNMKGTPVEGK--------LNEIFVGKMKSYIKCINVDYESARVEDFWDLQLNV----KNFKNLQE 353
Cdd:cd02257 24 DAHEFLLFLLDKLHEELKKSSKRTSdssslkslIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVSLED 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 354 SFDNYIEMELMNGENQYAAQDYGLQDAQKGVIFESFPPVLHLQLKRFEYDFNYdQMVKVNDKYEFPETIDLSPFVDKDvl 433
Cdd:cd02257 104 CLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDG-TKEKLNTKVSFPLELDLSPYLSEG-- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 434 kktLDSENKDKNPYVYNLHGVLVHSGD-ISTGHYYTLIKPGVEDQWYRFDDERVWRVTKKQVFQEnfgcdrlpdekvrtm 512
Cdd:cd02257 181 ---EKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEF--------------- 242
|
330 340
....*....|....*....|..
gi 767199261 513 trdeyqnyiIQRHTSAYMLVYI 534
Cdd:cd02257 243 ---------GSLSSSAYILFYE 255
|
|
| USP7_C2 |
pfam14533 |
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ... |
965-1217 |
2.21e-58 |
|
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific proteases has no known function.
Pssm-ID: 464201 Cd Length: 204 Bit Score: 199.63 E-value: 2.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 965 PFAFEVLSVPLKELERLRPIKLYWLKNSYIHYQCFEFEVANDYTESQFLEKVQHKIGFTDEEKENILLWTNTNFQFQGLL 1044
Cdd:pfam14533 1 ALYYEVLDISLSELENKKSIKVTWLSPGLKKEEELELLVPKNGTVADLLEELQKKVKLSEEGSGKIRLYEVSNHKIYKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 1045 SDQNTFKDVSKNSLLFGRILPEEsklfkELNRlenvqtssledfmddenatdrpmddeqdlgmaiehseDMKGRIVVVQQ 1124
Cdd:pfam14533 81 SEDEPIDSLNDYLTLYAEEIPEE-----ELNL-------------------------------------DEGERLIPVFH 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 1125 YFKDLENRHGISFLFNLIPDETFPKTKDRLHAKFGLGQKEFSKIKLSIgysteegtVFRSLQG-FSDEELdkvILYDIMS 1203
Cdd:pfam14533 119 FQKEPSRTHGIPFLFVLKPGEPFSDTKKRLQKRLGLPDKEFEKIKFAL--------VQRGKKPeYLEDDD---VLFDLLG 187
|
250
....*....|....*..
gi 767199261 1204 ---NLDYIYMDHPDRLR 1217
Cdd:pfam14533 188 qpdDLPWLGLDHPDKTP 204
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-533 |
3.57e-52 |
|
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: 186.47 E-value: 3.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFFTKYFRKLVYEIPT----EHESPNNSVPLA-------LQRAFYQLQVSDIP-LDTLELTRS 273
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNStedaELKNMPPDKPHEpqtiidqLQLIFAQLQFGNRSvVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 274 FGWDTAEsftQHDVQELNRILMDRLENNM-KGTPVEGK--LNEIFVGKMKSYIKCINVDYESARVEDFWDLQLNVKNFKN 350
Cdd:cd02668 81 LGLDTGQ---QQDAQEFSKLFLSLLEAKLsKSKNPDLKniVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 351 LQESFDNYIEMELMNGENQYAAQDYG-LQDAQKGVIFESFPPVLHLQLKRFEYDFNYDQMVKVNDKYEFPETIDLSPFVD 429
Cdd:cd02668 158 LEECIDEFLKEEQLTGDNQYFCESCNsKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 430 KdvlkktldsenKDKNPYVYNLHGVLVHSG-DISTGHYYTLIKPGVEDQWYRFDDERVWRVTKKQvFQENfgcdrlPDEK 508
Cdd:cd02668 238 E-----------SDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKP-LKLG------NSED 299
|
330 340
....*....|....*....|....*..
gi 767199261 509 VRTMTRDEYQNyiiQRHTS--AYMLVY 533
Cdd:cd02668 300 PAKPRKSEIKK---GTHSSrtAYMLVY 323
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-495 |
2.49e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 140.70 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFFTKYFRKLVYEIPTEHESPNNSVPLALQRAFYQLQVSD-----IPLDTLELTRsfgwdtAE 280
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQrraeaPPDYFLEASR------PP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 281 SFT---QHDVQELNRILMDRLEnnmkgTPVEgklnEIFVGKMKSYIKCINVDYESARVEDFWDLQLnvkNFKNLQESFDN 357
Cdd:cd02664 75 WFTpgsQQDCSEYLRYLLDRLH-----TLIE----KMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SFPSVQDLLNY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 358 YIEMELMNGENQYAAQD-YGLQDAQKGVIFESFPPVLHLQLKRFEYDFNYDQMVKVNDKYEFPETIDL--------SPFV 428
Cdd:cd02664 143 FLSPEKLTGDNQYYCEKcASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLpvrvesksSESP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 429 DKDVLKKTLDSENKDKNPYVYNLHGVLVHSGDIS-TGHYYTLIKPGV--------------------EDQWYRFDDERVW 487
Cdd:cd02664 223 LEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSSeSGHYFTYARDQTdadstgqecpepkdaeendeSKNWYLFNDSRVT 302
|
....*...
gi 767199261 488 RVTKKQVF 495
Cdd:cd02664 303 FSSFESVQ 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-498 |
3.90e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 139.33 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFFTKYFrkLVYEIPTEHESPNNS------------VPLALQRAFYQLQVSDIPLDTLELTRS 273
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPL--ANYLLSREHSKDCCNegfcmmcaleahVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 274 FGWDtaesfTQHDVQELNRILMDRLENN-MKGTPVEGKLN----------EIFVGKMKSYIKCINVDYESARVEDFWDLQ 342
Cdd:cd02661 81 FRIG-----RQEDAHEFLRYLLDAMQKAcLDRFKKLKAVDpssqettlvqQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 343 LNVKNFKNLQESFDNYIEMELMNGENQYAAQD-YGLQDAQKGVIFESFPPVLHLQLKRFEYdFNYDqmvKVNDKYEFPET 421
Cdd:cd02661 156 LDIKGADSLEDALEQFTKPEQLDGENKYKCERcKKKVKASKQLTIHRAPNVLTIHLKRFSN-FRGG---KINKQISFPET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 422 IDLSPFVdkdvlkktldSENKDkNPYVYNLHGVLVHSG-DISTGHYYTLIK--PGvedQWYRFDDERVWRVTKKQVFQEN 498
Cdd:cd02661 232 LDLSPYM----------SQPND-GPLKYKLYAVLVHSGfSPHSGHYYCYVKssNG---KWYNMDDSKVSPVSIETVLSQK 297
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-498 |
1.67e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 138.27 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFFTKYFRKlvYEIPTEHE------SPNNSVPLALQRAFYQLQVSD-----IPLDTLELTrsf 274
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRN--YFLSDRHSctclscSPNSCLSCAMDEIFQEFYYSGdrspyGPINLLYLS--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 275 gWDTAES---FTQHDVQELNRILMDRL-ENNMKGTPVEGKLNE-------IFVGKMKSYIKCINVDYESARVEDFWDLQL 343
Cdd:cd02660 77 -WKHSRNlagYSQQDAHEFFQFLLDQLhTHYGGDKNEANDESHcnciihqTFSGSLQSSVTCQRCGGVSTTVDPFLDLSL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 344 NVKN---------------FKNLQESFDNYIEMELMnGENQYAAQDYG-LQDAQKGVIFESFPPVLHLQLKRFEYdFNYD 407
Cdd:cd02660 156 DIPNkstpswalgesgvsgTPTLSDCLDRFTRPEKL-GDFAYKCSGCGsTQEATKQLSIKKLPPVLCFQLKRFEH-SLNK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 408 QMVKVNDKYEFPETIDLSPFVDkdVLKKTLDSENKDKNPYVYNLHGVLVHSGDISTGHYYTLIKPGvEDQWYRFDDERVW 487
Cdd:cd02660 234 TSRKIDTYVQFPLELNMTPYTS--SSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMIT 310
|
330
....*....|.
gi 767199261 488 RVTKKQVFQEN 498
Cdd:cd02660 311 RVSEEEVLKSQ 321
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
283-494 |
2.24e-32 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 126.25 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 283 TQHDVQELNRILMDRLENnmkgtpvegKLNEIFVGKMKSYIKCINVDYESARVEDFWDLQLNV------KNFKNLQESFD 356
Cdd:cd02674 21 DQQDAQEFLLFLLDGLHS---------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 357 NYIEMELMNGENQ-YAAQDYGLQDAQKGVIFESFPPVLHLQLKRFEYDFNYdqMVKVNDKYEFP-ETIDLSPFVDkdvlk 434
Cdd:cd02674 92 LFTKEETLDGDNAwKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGS--TRKLTTPVTFPlNDLDLTPYVD----- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 435 ktldsENKDKNPYVYNLHGVLVHSGDISTGHYYTLIKPGVEDQWYRFDDERVWRVTKKQV 494
Cdd:cd02674 165 -----TRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSV 219
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-477 |
1.03e-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: 119.80 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFFTKYFRKLVYEIPTEhespnnsvplalqrAFYQLQVSDIPLdtleltrsfgwdtaESFTQH 285
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAPQF--------------KGYQQQ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 286 DVQELNRILMDRLENNMKgtpvegklnEIFVGKMKSYIKCINVDYESARVEDFWDLQLNV----KNFKNLQESFDNYIEM 361
Cdd:cd02667 53 DSHELLRYLLDGLRTFID---------SIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRsdeiKSECSIESCLKQFTEV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 362 ELMNGENQYAAQDygLQDAQKGVIFESFPPVLHLQLKRFEYDfNYDQMVKVNDKYEFPETIDLSPFVDKdvlkKTLDSEN 441
Cdd:cd02667 124 EILEGNNKFACEN--CTKAKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFCDP----KCNSSED 196
|
250 260 270
....*....|....*....|....*....|....*.
gi 767199261 442 KDKnpYVYNLHGVLVHSGDISTGHYYTLIKPGVEDQ 477
Cdd:cd02667 197 KSS--VLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQ 230
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-495 |
4.52e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 118.57 E-value: 4.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFFTKYFR--KLVYEIPTEHESPNNSVPlalQRAFYQLQVSDIPLdtleltrsFgwdtaESFT 283
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLTclKDLFESISEQKKRTGVIS---PKKFITRLKRENEL--------F-----DNYM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 284 QHDVQE-----LNRI------------LMDRLENNMKGTPVEGKLNEIFVGKMKSYIKCINVDYESARVEDFWDLQLNVK 346
Cdd:cd02663 65 HQDAHEflnflLNEIaeildaerkaekANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 347 NFKNLQESFDNYIEMELMNGENQYAAQD-YGLQDAQKGVIFESFPPVLHLQLKRFEYDFNYDQMVKVNDKYEFPETidLS 425
Cdd:cd02663 145 QNTSITSCLRQFSATETLCGRNKFYCDEcCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLE--LR 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767199261 426 PFvdkdvlKKTLDSENKDKnpyVYNLHGVLVHSGD-ISTGHYYTLIKpgVEDQWYRFDDERVWRVTKKQVF 495
Cdd:cd02663 223 LF------NTTDDAENPDR---LYELVAVVVHIGGgPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAVE 282
|
|
| USP7_ICP0_bdg |
pfam12436 |
ICP0-binding domain of Ubiquitin-specific protease 7; This domain is one of two C-terminal ... |
648-934 |
6.95e-21 |
|
ICP0-binding domain of Ubiquitin-specific protease 7; This domain is one of two C-terminal domains on the much longer ubiquitin-specific proteases. This particular one is found to interact with the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110.
Pssm-ID: 463580 [Multi-domain] Cd Length: 239 Bit Score: 92.96 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 648 VKYWKMDYRRNSTLRLTQPINFESVNITLQEALKKEKKRTMqtqygeegvasteeddkalletvsflDLFIeepYLELqf 727
Cdd:pfam12436 1 IRLWPMVNRQNKTVRPDQPLPEADPAKTVEEIRDKMATRDN--------------------------PLRL---FLEV-- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 728 lnklkeasliskaqlddelistirtnLPELtkggiePVFaTDNKSNLLFVKSYDPHTQKLLGFGHFAVNQLQQLSDLSAI 807
Cdd:pfam12436 50 --------------------------AEEL------PPF-DKNDDILLFLKYYDPEKQTLRGVGHVYVPKSSKVSDLVPI 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 808 IED--SISSNEKLTFYEEVQPGTINEIYMKETIYDADIDTGDIVSFEVPgavLPDTFPV-YATIKDFYSYLRYRVKLKFS 884
Cdd:pfam12436 97 INErmGWPPDTPLLLYEEIKPNMIEIMKPKQTLKKSELQDGDIICFQRE---LSEKEQDeYPTAKDYYDFLLNRVEVTFR 173
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767199261 885 KFDGSSEeygvsneipESFEFWISAYAPYDDLARMVSKYAHVKPEYLKIF 934
Cdd:pfam12436 174 PKDNPND---------PGFTLELSKKMTYDQLAEKVAERLGVDPTKLRFT 214
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
204-497 |
4.61e-20 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 93.03 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 204 YVGFRNQGATCYLNSLLQSYFFTKYFRKLVYEIPTEHESPNN--SVPLALQRAFYQLQVSDIPLDTLELTRSFGwDTAES 281
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQlqSSFLLNPEKYNDELANQAPRRLLNALREVN-PMYEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 282 FTQHDVQElnrILMDRLENnmkgtpVEGKLNEIFVGKMKSYIKCINVDYESARVEDFWDLQLNVK--------------- 346
Cdd:cd02671 103 YLQHDAQE---VLQCILGN------IQELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQeselskseesseisp 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 347 ----NFKNLQESFDNYIEMELMNGENQYAAQD-YGLQDAQKGVIFESFPPVLHLQLKRF----EYDFNYDQMVKVNdkye 417
Cdd:cd02671 174 dpktEMKTLKWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKLPEVITIHLKCFaangSEFDCYGGLSKVN---- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 418 fpeTIDLSPFvdkdvlkkTLDSENKDKNP--YVYNLHGVLVHSG-DISTGHYYTLIKpgvedqWYRFDDERVwRVTKKQV 494
Cdd:cd02671 250 ---TPLLTPL--------KLSLEEWSTKPknDVYRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEV-KVTEEKD 311
|
...
gi 767199261 495 FQE 497
Cdd:cd02671 312 FLE 314
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
206-486 |
7.21e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 88.32 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFF------------TKYFRKLVYEIPTEHESPNNSVPLALqraFYQLQVSDIPldtleltrS 273
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALylpkldellddlSKELKVLKNVIRKPEPDLNQEEALKL---FTALWSSKEH--------K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 274 FGWdTAESFTQHDVQELNRILMDRLENNMKGTpVEGKLNEIFVGKMKSYIKCINvDYESARVEDFWDlqlnvKNFKNLQE 353
Cdd:COG5533 70 VGW-IPPMGSQEDAHELLGKLLDELKLDLVNS-FTIRIFKTTKDKKKTSTGDWF-DIIIELPDQTWV-----NNLKTLQE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 354 SFDNYIEM---ELM--NGENQyaaQDYGLQDAQKGVIFESFPPVLHLQLKRFEYDfNYDQMVK--VNDKYEFPETIDlsp 426
Cdd:COG5533 142 FIDNMEELvddETGvkAKENE---ELEVQAKQEYEVSFVKLPKILTIQLKRFANL-GGNQKIDteVDEKFELPVKHD--- 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 427 fvdkdvlKKTLDSENkdknpYVYNLHGVLVHSGDISTGHYYTLIKPGveDQWYRFDDERV 486
Cdd:COG5533 215 -------QILNIVKE-----TYYDLVGFVLHQGSLEGGHYIAYVKKG--GKWEKANDSDV 260
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
283-534 |
3.40e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 82.22 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 283 TQHDVQELNRILMDRLENNMKG-----TPVEGKLN---EIFVGKmkSYIKCINVDYESARVEDFWDLQLNVKNFKNLQES 354
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFQAaaeaiSPGEKSKNpmvQLFYGT--FLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 355 fdnyIEMELMNGENQYAAQDYGLQDAQKGvIFESFPPVLHLQLKRFEydFNYDQMVKVNDKYEFPETIDLSPfvdkdvlk 434
Cdd:cd02665 99 ----LEAAMFEGEVELLPSDHSVKSGQER-WFTELPPVLTFELSRFE--FNQGRPEKIHDKLEFPQIIQQVP-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 435 ktldsenkdknpyvYNLHGVLVHSGDISTGHYYTLIKPGVEDQWYRFDDERVWRVTKKQVFQENFGCDRLPdekvrtmtr 514
Cdd:cd02665 164 --------------YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNP--------- 220
|
250 260
....*....|....*....|
gi 767199261 515 deyqnyiiqrhtSAYMLVYI 534
Cdd:cd02665 221 ------------SAYCLMYI 228
|
|
| MATH |
cd00121 |
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ... |
41-180 |
2.42e-16 |
|
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains.
Pssm-ID: 238068 Cd Length: 126 Bit Score: 76.65 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 41 SFTWNIPDWNELTNPKYNSPRFRIGDFEWDILLFPQGNHNKG--VAVYLEPHPEEKLdettgemvpvDPDWYCCAQFAIG 118
Cdd:cd00121 2 KHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESGdyLSLYLELDKGESD----------LEKWSVRAEFTLK 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767199261 119 ISRPGNGDTInLINKSHHRFNALDTDWGFANLIDLNNLKHPskgrplSFLNEGTLNITAYVR 180
Cdd:cd00121 72 LVNQNGGKSL-SKSFTHVFFSEKGSGWGFPKFISWDDLEDS------YYLVDDSLTIEVEVK 126
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-494 |
3.32e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 76.64 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFFTKYFRKLvyeiptehespnnsvplalqrafyqlqvsdipldtLELTRSfgwdtaesftQH 285
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-----------------------------------LEEFLE----------QQ 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 286 DVQELNRILMDRLENNMKgTPVEGKLNEIfvgkmksyIKCINVDYESA-RVEDFWDLQLNVKNfknlQESFDNYIEMELM 364
Cdd:cd02662 36 DAHELFQVLLETLEQLLK-FPFDGLLASR--------IVCLQCGESSKvRYESFTMLSLPVPN----QSSGSGTTLEHCL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 365 NGENQYAA-QDYGLQDAQKGVIfeSFPPVLHLQLKRFEYDfNYDQMVKVNDKYEFPETIdlspfvdkdvlkktldsenkd 443
Cdd:cd02662 103 DDFLSTEIiDDYKCDRCQTVIV--RLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERL--------------------- 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767199261 444 kNPYVYNLHGVLVHSGDISTGHY-----YTLIKPGVE---------------DQWYRFDDERVWRVTKKQV 494
Cdd:cd02662 159 -PKVLYRLRAVVVHYGSHSSGHYvcyrrKPLFSKDKEpgsfvrmregpsstsHPWWRISDTTVKEVSESEV 228
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-494 |
4.05e-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 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: 77.76 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFFTKYFR-KLVYEIPTEHESPNNSVPL--ALQRAFYQLQVSDIPLDTLELTRSFGwDTAESF 282
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRdALKNYNPARRGANQSSDNLtnALRDLFDTMDKKQEPVPPIEFLQLLR-MAFPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 283 T---------QHDVQELNRILMDRLENNMKGTPVEG-KLNEIFVGKMKSYIKCI-NVDYESARVEDFWDLQLNVkNFKNL 351
Cdd:cd02657 80 AekqnqggyaQQDAEECWSQLLSVLSQKLPGAGSKGsFIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQCHI-SITTE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 352 QESFDNYIEMELmnGENQYAAQDYGLQDA--QKGVIFESFPPVLHLQLKRFEYDFNYDQMVKVNDKYEFPETIDLSPFVD 429
Cdd:cd02657 159 VNYLQDGLKKGL--EEEIEKHSPTLGRDAiyTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLYELCT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767199261 430 kdvlkktldsenkdkNPYVYNLHGVLVHSG-DISTGHYYTLIKPGVEDQWYRFDDERVWRVTKKQV 494
Cdd:cd02657 237 ---------------PSGYYELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDI 287
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
205-505 |
7.70e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 74.45 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 205 VGFRNQGATCYLNSLLQSYFFTKYFRKLVYEI-----------PTEHESPNNSV-PLALQRA----------FYQLQVSD 262
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFdeskaelasdyPTERRIGGREVsRSELQRSnqfvyelrslFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 263 IPLDT--LELTRSfgwdtaeSFTQHDVQELNRILMDRLENNMKGTPVEGK--------------LNEIFVGKMKSYIKCI 326
Cdd:cd02666 82 TRSVTpsKELAYL-------ALRQQDVTECIDNVLFQLEVALEPISNAFAgpdteddkeqsdliKRLFSGKTKQQLVPES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 327 NVDYESARVEDFWDLQLNVKNFKNLQESFDNYIEMELmngenqYAAQDYGLQDaqkgVIFESFPPVLHLQLKRfeyDFNY 406
Cdd:cd02666 155 MGNQPSVRTKTERFLSLLVDVGKKGREIVVLLEPKDL------YDALDRYFDY----DSLTKLPQRSQVQAQL---AQPL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 407 DQMVKVNDKYEFPETIDLS-----------------PFVDKDVLKKTLDSENKDKNPYVYNLHGVLVHSGDISTGHYYTL 469
Cdd:cd02666 222 QRELISMDRYELPSSIDDIdelireaiqsesslvrqAQNELAELKHEIEKQFDDLKSYGYRLHAVFIHRGEASSGHYWVY 301
|
330 340 350
....*....|....*....|....*....|....*.
gi 767199261 470 IKPGVEDQWYRFDDERVWRVTKKQVFQENFGCDRLP 505
Cdd:cd02666 302 IKDFEENVWRKYNDETVTVVPASEVFLFTLGNTATP 337
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
205-483 |
1.09e-11 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 67.30 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 205 VGFRNQGATCYLNSLLQSYFFTKYFRKLV-----YEIPTEH----E----------------SPNNsvplaLQRAFyqlq 259
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAlshlaTECLKEHcllcElgflfdmlekakgkncQASN-----FLRAL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 260 vSDIPL-DTLELTRSFGWDTAESFTQHDVQELNRILMDRL---ENNMKGTPVEGK--LNEIFVGKMKSYIKCINVDYESA 333
Cdd:pfam13423 72 -SSIPEaSALGLLDEDRETNSAISLSSLIQSFNRFLLDQLsseENSTPPNPSPAEspLEQLFGIDAETTIRCSNCGHESV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 334 RVEDFWDLQLNV------KNFKNLQESFDNYIEMELMNGENQYAAQDY--GLQDAQKGVIFESFPPVLHLQLKRFEYDFN 405
Cdd:pfam13423 151 RESSTHVLDLIYprkpssNNKKPPNQTFSSILKSSLERETTTKAWCEKckRYQPLESRRTVRNLPPVLSLNAALTNEEWR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 406 YDQMVKVndkyEFPETIDLSpfvdkdvlkkTLDSENKDKNPYVYNLHGVLVHSGDIST-GHYYTLIK-------PGVEDQ 477
Cdd:pfam13423 231 QLWKTPG----WLPPEIGLT----------LSDDLQGDNEIVKYELRGVVVHIGDSGTsGHLVSFVKvadseleDPTESQ 296
|
....*.
gi 767199261 478 WYRFDD 483
Cdd:pfam13423 297 WYLFND 302
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
206-486 |
1.85e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 66.58 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 206 GFRNQGATCYLNSLLQSYFFTKYFRKLVYEIPTEHESPNN----------------------SVPLAL--QRAFYQLQVS 261
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVdpandlncqlikladgllsgrySKPASLksENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 262 DIPLDTLeltrsFGWDTAESFT--QHDVQELNRILMDRLENNMKGTPVEgKLNEIFVGKMKSYIKCIN---VDYeSARVE 336
Cdd:cd02658 81 PSMFKAL-----IGKGHPEFSTmrQQDALEFLLHLIDKLDRESFKNLGL-NPNDLFKFMIEDRLECLSckkVKY-TSELS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 337 DFWDLQLNVKNFKNLQESFDNYIEMELMNGENQYAA----QDYGLQDAQKGVI-----FESFPPVLHLQLKRFEYDFNYD 407
Cdd:cd02658 154 EILSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFApetiEDFCSTCKEKTTAtkttgFKTFPDYLVINMKRFQLLENWV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 408 qmvkvndkyefPETIDLSPFVDKDvlkktLDSENkdknpyvYNLHGVLVHSG-DISTGHYYTLIKPGV--EDQWYRFDDE 484
Cdd:cd02658 234 -----------PKKLDVPIDVPEE-----LGPGK-------YELIAFISHKGtSVHSGHYVAHIKKEIdgEGKWVLFNDE 290
|
..
gi 767199261 485 RV 486
Cdd:cd02658 291 KV 292
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
385-483 |
1.30e-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: 54.07 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 385 IFESFPPVLHLQLKRFEYDFNYDQmvKVNDKYEFPETIDLSPFVDKDVLKKTLDS-------ENKDKNP----YVYNLHG 453
Cdd:cd02670 94 VFAKAPSCLIICLKRYGKTEGKAQ--KMFKKILIPDEIDIPDFVADDPRACSKCQlecrvcyDDKDFSPtcgkFKLSLCS 171
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767199261 454 VLVHSG-DISTGHYYTLIK-----------PGVEDQWYRFDD 483
Cdd:cd02670 172 AVCHRGtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDD 213
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
380-489 |
1.46e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 56.04 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 380 AQKGVIFESFPPVLHLQLKRFEYDFNYDQmvKVNDKYEFPetidlspfVDKDVLKKTLDSenKDKNPYVYNLHGVLVHSG 459
Cdd:COG5560 707 ASKQMELWRLPMILIIHLKRFSSVRSFRD--KIDDLVEYP--------IDDLDLSGVEYM--VDDPRLIYDLYAVDNHYG 774
|
90 100 110
....*....|....*....|....*....|
gi 767199261 460 DISTGHYYTLIKPGVEDQWYRFDDERVWRV 489
Cdd:COG5560 775 GLSGGHYTAYARNFANNGWYLFDDSRITEV 804
|
|
| MATH |
smart00061 |
meprin and TRAF homology; |
42-151 |
3.22e-05 |
|
meprin and TRAF homology;
Pssm-ID: 214496 [Multi-domain] Cd Length: 95 Bit Score: 43.83 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 42 FTWNIPDW-NELTNPKYNSPRFRIGDFEWDILLFPQGNHnkgVAVYLEPHPEEKLDEttgemvpvdpDWYCCAQFAIGIS 120
Cdd:smart00061 2 LSHTFKNVsRLEEGESYFSPSEEHFNIPWRLKIYRKNGF---LSLYLHCEKEECDSR----------KWSIEAEFTLKLV 68
|
90 100 110
....*....|....*....|....*....|.
gi 767199261 121 RPgNGDtiNLINKSHHRFNAlDTDWGFANLI 151
Cdd:smart00061 69 SQ-NGK--SLSKKDKHVFEK-PSGWGFSKFI 95
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
195-258 |
3.44e-03 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 41.79 E-value: 3.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767199261 195 NYDSKKVTGYVGFRNQGATCYLNSLLQ----SYFFTKYFRKLVYEiptehESPNNSVPLA----LQRAFYQL 258
Cdd:COG5560 256 NRSINKEAGTCGLRNLGNTCYMNSALQclmhTWELRDYFLSDEYE-----ESINEENPLGmhgsVASAYADL 322
|
|
| MATH_HAUSP |
cd03772 |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ... |
39-187 |
6.76e-03 |
|
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, N-terminal MATH (TRAF-like) domain; composed of proteins similar to human HAUSP, an enzyme that specifically catalyzes the deubiquitylation of p53 and MDM2, hence playing an important role in the p53-MDM2 pathway. It contains an N-terminal TRAF-like domain and a C-terminal catalytic protease (C19 family) domain. The tumor suppressor p53 protein is a transcription factor that responds to many cellular stress signals and is regulated primarily through ubiquitylation and subsequent degradation. MDM2 is a RING-finger E3 ubiquitin ligase that promotes p53 ubiquitinylation. p53 and MDM2 bind to the same site in the N-terminal TRAF-like domain of HAUSP in a mutually exclusive manner. HAUSP also interacts with the Epstein-Barr nuclear antigen 1 (EBNA1) protein of the Epstein-Barr virus (EBV), which efficiently immortalizes infected cells predisposing the host to a variety of cancers. EBNA1 plays several important roles in EBV latent infection and cellular transformation. It binds the same pocket as p53 in the HAUSP TRAF-like domain. Through interactions with p53, MDM2 and EBNA1, HAUSP plays a role in cell proliferation, apoptosis and EBV-mediated immortalization.
Pssm-ID: 239741 Cd Length: 137 Bit Score: 38.20 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767199261 39 EDSFTWNIPDWNELTNPKYNSPRFrIGDFEWDILLFP-----QGNHNKGVAVYLEPHPEEKLdettgemvpvdPDWYCCA 113
Cdd:cd03772 2 EATFSFTVERFSRLSESVLSPPCF-VRNLPWKIMVMPrnypdRNPHQKSVGFFLQCNAESDS-----------TSWSCHA 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767199261 114 QFAIG-ISRPGNGDTInlINKSHHRFNALDTDWGFANLIDLNNLKHPSKGrplsFLNEGTlnITAYVRILKD-PTG 187
Cdd:cd03772 70 QAVLRiINYKDDEPSF--SRRISHLFFSKENDWGFSNFMTWSEVTDPEKG----FIEDDT--ITLEVYVQADaPHG 137
|
|
| |
