|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-504 |
2.19e-137 |
|
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: 418.58 E-value: 2.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 191 GCIGLRNQGATCYMNSILQSFYFTTGFRRAVYNM-DVGTEPNESNIVLAMQRVFYELQMASEAVETNSL---TRAFGWDK 266
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIpPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELtdkTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 267 LDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVLGMDSLERAFEAY 346
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 347 TTSEILDDENKYDAGDHGLQ-RAEKGVKFVELPPILHVQLMRFQYCGVE---QKINERFSFPEKMNLASCCELG------ 416
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKvDAEKGVCFKKLPPVLTLQLKRFEFDFETmmrIKINDRFEFPLELDMEPYTEKGlakkeg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 417 --PMLTEEDCVYSLHAVLVHSGEFHGGHYVTYINVNLHEsavdptssaKWCKFDDDVVSRTTTDDAIVSNFGGEKTM--- 491
Cdd:cd02659 241 dsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDG---------KWYKFNDDVVTPFDPNDAEEECFGGEETQkty 311
|
330 340
....*....|....*....|..
gi 392920646 492 ---------NSSAYMLVYVRDN 504
Cdd:cd02659 312 dsgprafkrTTNAYMLFYERKS 333
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
4-1127 |
2.75e-131 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 427.36 E-value: 2.75e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 4 SPDPEDLLIVPTHDiPSYDESLdpfgpEGHLSLDIDCFSKFmsrsDNRIMSKPIIVRGIPWRILAIcrnQQGSrHSMNSR 83
Cdd:COG5077 17 SPDKSIGSILPQFD-PDVEELL-----EMSFTWKVKRWSEL----AKKVESPPFSVGGHTWKIILF---PQGN-NQCNVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 84 VnrsnfnfgfFLQCNNDELLQKRG-MWRCYGTAVLEVLNADGPSI--QKKIHHSFHNTEVDWGFSNYDQYDTLCNPKDG- 159
Cdd:COG5077 83 V---------YLEYEPQELEETGGkYYDCCAQFAFDISNPKYPTIeyINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 160 --YVVNDTIKLrcrfTADV-----PTGANYM----WDSKRHTGCIGLRNQGATCYMNSILQSFYFTTGFRRAVYNMDVGT 228
Cdd:COG5077 154 ppFLEEGTLVI----TVYVrvlkdPTGVLWHsflnYNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 229 EPNESNIVLAMQRVFYELQMASEAVETNSLTRAFGWDKLDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIPNLFRGNMK 308
Cdd:COG5077 230 PRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 309 SYIKCLDVDYESSRTESFYDVQLNVLGMDSLERAFEAYTTSEILDDENKYDAGDHGLQRAEKGVKFVELPPILHVQLMRF 388
Cdd:COG5077 310 SYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 389 QY---CGVEQKINERFSFPEKMNLAsccelgPMLTEE-------DCVYSLHAVLVHSGEFHGGHYVTYINvnlhesavdP 458
Cdd:COG5077 390 EYdfeRDMMVKINDRYEFPLEIDLL------PFLDRDadksensDAVYVLYGVLVHSGDLHEGHYYALLK---------P 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 459 TSSAKWCKFDDDVVSRTTTDDAIVSNFGGEKTMN------------SSAYMLVYVRDNAIDQFLAPIPDSQIPQSVSRTF 526
Cdd:COG5077 455 EKDGRWYKFDDTRVTRATEKEVLEENFGGDHPYKdkirdhsgikrfMSAYMLVYLRKSMLDDLLNPVAAVDIPPHVEEVL 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 527 EMERLHRNREKKKLEEEQLCMGIVLVTPDIVASNHSFDLVDqsivhdsiphetvwkhmFTAELyqfvHDRLFEKSAMQKI 606
Cdd:COG5077 535 SEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDYPD-----------------FSSEL----NDSGLAQFVIKRG 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 607 DMFdSDDEARQARRDNLRRIKSKKFNFRLWRMTDSYSLERTTQKLTSRLRPSefidCKTDTRLDTLLSQDFETI--YVEF 684
Cdd:COG5077 594 AKI-SDLRNNIAEHLNTPQSLYLREWTMIKRHNKTVRVDRPCNRVNITTREL----VGMNTRTGEELRSYLERIieHNQL 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 685 SNNIERPLceyDTARDLLFFVKYYDTMTDKFTIIGHTmfdcHKRFNLYRSMLCEMI--GLPADTELKYYMEHAASYLELV 762
Cdd:COG5077 669 DSQRKVAL---TKDGVINIFVKYFDYTTQPISGFGGL----HVNKFLKISSISPWIedSISSNLPLTLYEEIKPGMVDTI 741
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 763 DLTQNYSIGRLveeQDGGILVVEKV-----ETSTSTQNAKQKMNELFLDVEVEFvqSFYNKKPEEEPFEQFVKRICLDDK 837
Cdd:COG5077 742 GDNITFIGSEI---GTGDIICFEVPgavefDTSSAYDSALKLYDFLQGRVLVAF--RRFSDEYRENVFEFLLFIGDFYDD 816
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 838 LftvAEEIGARLNVDPKKVLIWTRVSGSRFEPFFddyMLNTCKGLMTRPVHDPRAYKRYRVQ-YAIMPFDIDEISKHRIq 916
Cdd:COG5077 817 L---CRNVSCKLHVTPFYLRGTKSTELEDRIRRV---VGSKSIFLLKEALSSSSEFRQAPVDfYEVLDVPLSELERKRL- 889
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 917 TKLFWqLPNG--HVEELTLFPLKEGTVIDIINEAKRYYPFVeggsgkfrllqigAPPLSNQRVYQIYGENTLISDLDQRT 994
Cdd:COG5077 890 IRLCF-LSNGyqHVYLAEFYVEKDYTAVDHLHIVVTKVGCT-------------DELKKSVLVYEVVNLRPVRGHSLKTL 955
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 995 MYKLALHCRL--EEVPIDELDMSPGEFLCPVVHFDREPTKLFGLSFVIKIRNNELMTEVRDRLRRKLNdVSDADFAKYKF 1072
Cdd:COG5077 956 IIDDNVRSTLygEVFPLEQEQLTTNEMCVVVQHFFKDLIRTHGIPFMFVIVPFETFLDTKVRLVARFG-YKYKLFSKIKL 1034
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 1073 ALLSRD---KLCRTIEFNNGEKVNLADMANQTtgvpqvYIGLDH--KSPIQHSSEAAIRI 1127
Cdd:COG5077 1035 FVGKSYtdgELDWPMSYFNDEDILYDLIERLD------YILLDHpdRLRSHSSYDRAIIM 1088
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
193-500 |
8.79e-81 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 266.62 E-value: 8.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 193 IGLRNQGATCYMNSILQSFYFTTGFRRAVYN----MDVGTEPNESNIVLAMQRVFYELQMAS--EAVETNSLTRAFGWD- 265
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRisplSEDSRYNKDINLLCALRDLFKALQKNSksSSVSPKMFKKSLGKLn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 266 -KLDAFNQHDVQEFCRVLLDNLETKMKG---TSEEKSIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVLGMDSLER 341
Cdd:pfam00443 81 pDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 342 ------AFEAYTTSEILDDENKYD-AGDHGLQRAEKGVKFVELPPILHVQLMRFQYCG-VEQKINERFSFPEKMNLAS-C 412
Cdd:pfam00443 161 taslqiCFLQFSKLEELDDEEKYYcDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRsTWEKLNTEVEFPLELDLSRyL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 413 CELGPMLTEEDCVYSLHAVLVHSGEFHGGHYVTYINvnlhesavdPTSSAKWCKFDDDVVSRTTTDDAIvsnfggektMN 492
Cdd:pfam00443 241 AEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK---------AYENNRWYKFDDEKVTEVDEETAV---------LS 302
|
....*...
gi 392920646 493 SSAYMLVY 500
Cdd:pfam00443 303 SSAYILFY 310
|
|
| MATH_HAUSP |
cd03772 |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ... |
30-179 |
6.74e-65 |
|
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: 215.40 E-value: 6.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 30 PEGHLSLDIDCFSKFmsrsDNRIMSKPIIVRGIPWRILAICRNQQGSrhsmnsrvNRSNFNFGFFLQCNNDELLQkrgMW 109
Cdd:cd03772 1 SEATFSFTVERFSRL----SESVLSPPCFVRNLPWKIMVMPRNYPDR--------NPHQKSVGFFLQCNAESDST---SW 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392920646 110 RCYGTAVLEVLNAD--GPSIQKKIHHSFHNTEVDWGFSNYDQYDTLCNPKDGYVVNDTIKLRCRFTADVPTG 179
Cdd:cd03772 66 SCHAQAVLRIINYKddEPSFSRRISHLFFSKENDWGFSNFMTWSEVTDPEKGFIEDDTITLEVYVQADAPHG 137
|
|
| USP7_C2 |
pfam14533 |
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ... |
897-1116 |
1.31e-54 |
|
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: 188.85 E-value: 1.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 897 RVQYAIMPFDIDEISkHRIQTKLFWQLPNG-HVEELTLFPLKEGTVIDIINEAKRYYPFVEGGSGKFRLLQIgapplSNQ 975
Cdd:pfam14533 1 ALYYEVLDISLSELE-NKKSIKVTWLSPGLkKEEELELLVPKNGTVADLLEELQKKVKLSEEGSGKIRLYEV-----SNH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 976 RVYQIYGENTLISDLDQrtmyklALHCRLEEVPIDELDMSPGEFLCPVVHFDREPTKLFGLSFVIKIRNNELMTEVRDRL 1055
Cdd:pfam14533 75 KIYKELSEDEPIDSLND------YLTLYAEEIPEEELNLDEGERLIPVFHFQKEPSRTHGIPFLFVLKPGEPFSDTKKRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392920646 1056 RRKLnDVSDADFAKYKFALLSRDKlcrTIEFNNGEKVNLaDMANQTTGVPqvYIGLDH--KSP 1116
Cdd:pfam14533 149 QKRL-GLPDKEFEKIKFALVQRGK---KPEYLEDDDVLF-DLLGQPDDLP--WLGLDHpdKTP 204
|
|
| MATH |
pfam00917 |
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ... |
38-168 |
4.37e-21 |
|
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This domain is hugely expanded in the nematode C. elegans.
Pssm-ID: 425944 [Multi-domain] Cd Length: 113 Bit Score: 89.62 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 38 IDCFSKFMsRSDNRImSKPIIVRGIPWRIlaicrnqqgsrhsmnsRVNRSNFNFGFFLQCNNDELLQkrGMWRCYGTAVL 117
Cdd:pfam00917 1 IKNFSKIK-EGESYY-SPVEERFNIPWRL----------------QIYRKGGFLGLYLHCDKEEELE--RGWSIETEFTL 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 392920646 118 EVLNADGPSIQKKIHHSFHN-TEVDWG-FSNYDQYDTLCNPKDGYVVNDTIKL 168
Cdd:pfam00917 61 KLVSSNGKSVTKTDTHVFEKpKGWGWGkFISWDDLEKDYLVDDSITVEAHVKI 113
|
|
| USP7_ICP0_bdg |
pfam12436 |
ICP0-binding domain of Ubiquitin-specific protease 7; This domain is one of two C-terminal ... |
679-860 |
1.19e-14 |
|
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: 74.85 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 679 TIYVEfsnnIERPLCEYDTARDLLFFVKYYDTMTDKFTIIGHTMFDCHKRFNLYRSMLCEMIGLPADTELKYYMEHAASY 758
Cdd:pfam12436 44 RLFLE----VAEELPPFDKNDDILLFLKYYDPEKQTLRGVGHVYVPKSSKVSDLVPIINERMGWPPDTPLLLYEEIKPNM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 759 LELVDLTQNYsigRLVEEQDGGILVVEKVETSTSTQ---NAKQKMNELFLDVEVEFVQSFynkKPEEEPFE-QFVKRICL 834
Cdd:pfam12436 120 IEIMKPKQTL---KKSELQDGDIICFQRELSEKEQDeypTAKDYYDFLLNRVEVTFRPKD---NPNDPGFTlELSKKMTY 193
|
170 180
....*....|....*....|....*.
gi 392920646 835 DDklftVAEEIGARLNVDPKKVLIWT 860
Cdd:pfam12436 194 DQ----LAEKVAERLGVDPTKLRFTT 215
|
|
| MATH |
smart00061 |
meprin and TRAF homology; |
38-147 |
3.37e-11 |
|
meprin and TRAF homology;
Pssm-ID: 214496 [Multi-domain] Cd Length: 95 Bit Score: 60.78 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 38 IDCFSKFMSRSDN-RIMSKPIIVRGIPWRIlaicrnqqgsrhsmnsRVNRSNFNFGFFLQCNNDELLQKrgMWRCYGTAV 116
Cdd:smart00061 3 SHTFKNVSRLEEGeSYFSPSEEHFNIPWRL----------------KIYRKNGFLSLYLHCEKEECDSR--KWSIEAEFT 64
|
90 100 110
....*....|....*....|....*....|.
gi 392920646 117 LEVLNADGPSIQKKIHHSFHNtEVDWGFSNY 147
Cdd:smart00061 65 LKLVSQNGKSLSKKDKHVFEK-PSGWGFSKF 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-504 |
2.19e-137 |
|
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: 418.58 E-value: 2.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 191 GCIGLRNQGATCYMNSILQSFYFTTGFRRAVYNM-DVGTEPNESNIVLAMQRVFYELQMASEAVETNSL---TRAFGWDK 266
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIpPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELtdkTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 267 LDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVLGMDSLERAFEAY 346
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 347 TTSEILDDENKYDAGDHGLQ-RAEKGVKFVELPPILHVQLMRFQYCGVE---QKINERFSFPEKMNLASCCELG------ 416
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKvDAEKGVCFKKLPPVLTLQLKRFEFDFETmmrIKINDRFEFPLELDMEPYTEKGlakkeg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 417 --PMLTEEDCVYSLHAVLVHSGEFHGGHYVTYINVNLHEsavdptssaKWCKFDDDVVSRTTTDDAIVSNFGGEKTM--- 491
Cdd:cd02659 241 dsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDG---------KWYKFNDDVVTPFDPNDAEEECFGGEETQkty 311
|
330 340
....*....|....*....|..
gi 392920646 492 ---------NSSAYMLVYVRDN 504
Cdd:cd02659 312 dsgprafkrTTNAYMLFYERKS 333
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
4-1127 |
2.75e-131 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 427.36 E-value: 2.75e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 4 SPDPEDLLIVPTHDiPSYDESLdpfgpEGHLSLDIDCFSKFmsrsDNRIMSKPIIVRGIPWRILAIcrnQQGSrHSMNSR 83
Cdd:COG5077 17 SPDKSIGSILPQFD-PDVEELL-----EMSFTWKVKRWSEL----AKKVESPPFSVGGHTWKIILF---PQGN-NQCNVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 84 VnrsnfnfgfFLQCNNDELLQKRG-MWRCYGTAVLEVLNADGPSI--QKKIHHSFHNTEVDWGFSNYDQYDTLCNPKDG- 159
Cdd:COG5077 83 V---------YLEYEPQELEETGGkYYDCCAQFAFDISNPKYPTIeyINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 160 --YVVNDTIKLrcrfTADV-----PTGANYM----WDSKRHTGCIGLRNQGATCYMNSILQSFYFTTGFRRAVYNMDVGT 228
Cdd:COG5077 154 ppFLEEGTLVI----TVYVrvlkdPTGVLWHsflnYNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 229 EPNESNIVLAMQRVFYELQMASEAVETNSLTRAFGWDKLDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIPNLFRGNMK 308
Cdd:COG5077 230 PRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 309 SYIKCLDVDYESSRTESFYDVQLNVLGMDSLERAFEAYTTSEILDDENKYDAGDHGLQRAEKGVKFVELPPILHVQLMRF 388
Cdd:COG5077 310 SYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 389 QY---CGVEQKINERFSFPEKMNLAsccelgPMLTEE-------DCVYSLHAVLVHSGEFHGGHYVTYINvnlhesavdP 458
Cdd:COG5077 390 EYdfeRDMMVKINDRYEFPLEIDLL------PFLDRDadksensDAVYVLYGVLVHSGDLHEGHYYALLK---------P 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 459 TSSAKWCKFDDDVVSRTTTDDAIVSNFGGEKTMN------------SSAYMLVYVRDNAIDQFLAPIPDSQIPQSVSRTF 526
Cdd:COG5077 455 EKDGRWYKFDDTRVTRATEKEVLEENFGGDHPYKdkirdhsgikrfMSAYMLVYLRKSMLDDLLNPVAAVDIPPHVEEVL 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 527 EMERLHRNREKKKLEEEQLCMGIVLVTPDIVASNHSFDLVDqsivhdsiphetvwkhmFTAELyqfvHDRLFEKSAMQKI 606
Cdd:COG5077 535 SEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDYPD-----------------FSSEL----NDSGLAQFVIKRG 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 607 DMFdSDDEARQARRDNLRRIKSKKFNFRLWRMTDSYSLERTTQKLTSRLRPSefidCKTDTRLDTLLSQDFETI--YVEF 684
Cdd:COG5077 594 AKI-SDLRNNIAEHLNTPQSLYLREWTMIKRHNKTVRVDRPCNRVNITTREL----VGMNTRTGEELRSYLERIieHNQL 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 685 SNNIERPLceyDTARDLLFFVKYYDTMTDKFTIIGHTmfdcHKRFNLYRSMLCEMI--GLPADTELKYYMEHAASYLELV 762
Cdd:COG5077 669 DSQRKVAL---TKDGVINIFVKYFDYTTQPISGFGGL----HVNKFLKISSISPWIedSISSNLPLTLYEEIKPGMVDTI 741
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 763 DLTQNYSIGRLveeQDGGILVVEKV-----ETSTSTQNAKQKMNELFLDVEVEFvqSFYNKKPEEEPFEQFVKRICLDDK 837
Cdd:COG5077 742 GDNITFIGSEI---GTGDIICFEVPgavefDTSSAYDSALKLYDFLQGRVLVAF--RRFSDEYRENVFEFLLFIGDFYDD 816
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 838 LftvAEEIGARLNVDPKKVLIWTRVSGSRFEPFFddyMLNTCKGLMTRPVHDPRAYKRYRVQ-YAIMPFDIDEISKHRIq 916
Cdd:COG5077 817 L---CRNVSCKLHVTPFYLRGTKSTELEDRIRRV---VGSKSIFLLKEALSSSSEFRQAPVDfYEVLDVPLSELERKRL- 889
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 917 TKLFWqLPNG--HVEELTLFPLKEGTVIDIINEAKRYYPFVeggsgkfrllqigAPPLSNQRVYQIYGENTLISDLDQRT 994
Cdd:COG5077 890 IRLCF-LSNGyqHVYLAEFYVEKDYTAVDHLHIVVTKVGCT-------------DELKKSVLVYEVVNLRPVRGHSLKTL 955
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 995 MYKLALHCRL--EEVPIDELDMSPGEFLCPVVHFDREPTKLFGLSFVIKIRNNELMTEVRDRLRRKLNdVSDADFAKYKF 1072
Cdd:COG5077 956 IIDDNVRSTLygEVFPLEQEQLTTNEMCVVVQHFFKDLIRTHGIPFMFVIVPFETFLDTKVRLVARFG-YKYKLFSKIKL 1034
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 1073 ALLSRD---KLCRTIEFNNGEKVNLADMANQTtgvpqvYIGLDH--KSPIQHSSEAAIRI 1127
Cdd:COG5077 1035 FVGKSYtdgELDWPMSYFNDEDILYDLIERLD------YILLDHpdRLRSHSSYDRAIIM 1088
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
193-500 |
8.79e-81 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 266.62 E-value: 8.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 193 IGLRNQGATCYMNSILQSFYFTTGFRRAVYN----MDVGTEPNESNIVLAMQRVFYELQMAS--EAVETNSLTRAFGWD- 265
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRisplSEDSRYNKDINLLCALRDLFKALQKNSksSSVSPKMFKKSLGKLn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 266 -KLDAFNQHDVQEFCRVLLDNLETKMKG---TSEEKSIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVLGMDSLER 341
Cdd:pfam00443 81 pDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 342 ------AFEAYTTSEILDDENKYD-AGDHGLQRAEKGVKFVELPPILHVQLMRFQYCG-VEQKINERFSFPEKMNLAS-C 412
Cdd:pfam00443 161 taslqiCFLQFSKLEELDDEEKYYcDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRsTWEKLNTEVEFPLELDLSRyL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 413 CELGPMLTEEDCVYSLHAVLVHSGEFHGGHYVTYINvnlhesavdPTSSAKWCKFDDDVVSRTTTDDAIvsnfggektMN 492
Cdd:pfam00443 241 AEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK---------AYENNRWYKFDDEKVTEVDEETAV---------LS 302
|
....*...
gi 392920646 493 SSAYMLVY 500
Cdd:pfam00443 303 SSAYILFY 310
|
|
| MATH_HAUSP |
cd03772 |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ... |
30-179 |
6.74e-65 |
|
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: 215.40 E-value: 6.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 30 PEGHLSLDIDCFSKFmsrsDNRIMSKPIIVRGIPWRILAICRNQQGSrhsmnsrvNRSNFNFGFFLQCNNDELLQkrgMW 109
Cdd:cd03772 1 SEATFSFTVERFSRL----SESVLSPPCFVRNLPWKIMVMPRNYPDR--------NPHQKSVGFFLQCNAESDST---SW 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392920646 110 RCYGTAVLEVLNAD--GPSIQKKIHHSFHNTEVDWGFSNYDQYDTLCNPKDGYVVNDTIKLRCRFTADVPTG 179
Cdd:cd03772 66 SCHAQAVLRIINYKddEPSFSRRISHLFFSKENDWGFSNFMTWSEVTDPEKGFIEDDTITLEVYVQADAPHG 137
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
194-501 |
2.69e-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: 206.95 E-value: 2.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFYFttgfrravynmdvgtepnesnivlamqrvfyelqmaseavetnsltrafgwdkldafNQH 273
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS---------------------------------------------------------EQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 274 DVQEFCRVLLDNLETKMKGTSEEKS--------IPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNV----LGMDSLER 341
Cdd:cd02257 24 DAHEFLLFLLDKLHEELKKSSKRTSdssslkslIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVSLED 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 342 AFEAYTTSEILDDENKYDAGDHGLQRAEKGVKFVELPPILHVQLMRFQYC--GVEQKINERFSFPEKMNLASCCELGPML 419
Cdd:cd02257 104 CLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNedGTKEKLNTKVSFPLELDLSPYLSEGEKD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 420 T---EEDCVYSLHAVLVHSGE-FHGGHYVTYINVNLHEsavdptssaKWCKFDDDVVSRTTTDDaiVSNFGGektMNSSA 495
Cdd:cd02257 184 SdsdNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDG---------KWYKFNDDKVTEVSEEE--VLEFGS---LSSSA 249
|
....*.
gi 392920646 496 YMLVYV 501
Cdd:cd02257 250 YILFYE 255
|
|
| USP7_C2 |
pfam14533 |
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ... |
897-1116 |
1.31e-54 |
|
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: 188.85 E-value: 1.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 897 RVQYAIMPFDIDEISkHRIQTKLFWQLPNG-HVEELTLFPLKEGTVIDIINEAKRYYPFVEGGSGKFRLLQIgapplSNQ 975
Cdd:pfam14533 1 ALYYEVLDISLSELE-NKKSIKVTWLSPGLkKEEELELLVPKNGTVADLLEELQKKVKLSEEGSGKIRLYEV-----SNH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 976 RVYQIYGENTLISDLDQrtmyklALHCRLEEVPIDELDMSPGEFLCPVVHFDREPTKLFGLSFVIKIRNNELMTEVRDRL 1055
Cdd:pfam14533 75 KIYKELSEDEPIDSLND------YLTLYAEEIPEEELNLDEGERLIPVFHFQKEPSRTHGIPFLFVLKPGEPFSDTKKRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392920646 1056 RRKLnDVSDADFAKYKFALLSRDKlcrTIEFNNGEKVNLaDMANQTTGVPqvYIGLDH--KSP 1116
Cdd:pfam14533 149 QKRL-GLPDKEFEKIKFALVQRGK---KPEYLEDDDVLF-DLLGQPDDLP--WLGLDHpdKTP 204
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-500 |
8.24e-50 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 179.54 E-value: 8.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFYFTTGFRRAVY-----------NMDVGTEPNESNIVLAMQRVFYELQMA-SEAVETNSLTRA 261
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnstedaelkNMPPDKPHEPQTIIDQLQLIFAQLQFGnRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 262 FGwdkLDAFNQHDVQEFCRVLLDNLETKMKGTSEEKS---IPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVLGMDS 338
Cdd:cd02668 81 LG---LDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLkniVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 339 LERAFEAYTTSEILDDENKYDAGDHG-LQRAEKGVKFVELPPILHVQLMRFQY---CGVEQKINERFSFPEKMNLASCCE 414
Cdd:cd02668 158 LEECIDEFLKEEQLTGDNQYFCESCNsKTDATRRIRLTTLPPTLNFQLLRFVFdrkTGAKKKLNASISFPEILDMGEYLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 415 LGPmltEEDCVYSLHAVLVHSG-EFHGGHYVTYINvnlhesavDPtSSAKWCKFDDDVVSRTTT---DDAIVSNFGGEK- 489
Cdd:cd02668 238 ESD---EGSYVYELSGVLIHQGvSAYSGHYIAHIK--------DE-QTGEWYKFNDEDVEEMPGkplKLGNSEDPAKPRk 305
|
330
....*....|....*...
gi 392920646 490 ------TMNSS-AYMLVY 500
Cdd:cd02668 306 seikkgTHSSRtAYMLVY 323
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-501 |
1.31e-40 |
|
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: 152.04 E-value: 1.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFYFTTGFRRAVYNMDVGTEPNESN--IVLAMQrvfyelQMASEAVETNSLTRA--FGWDKLDA 269
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALE------AHVERALASSGPGSAprIFSSNLKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 270 FN-------QHDVQEFCRVLLDNLE-TKMKGTSEEKSIP----------NLFRGNMKSYIKCLDVDYESSRTESFYDVQL 331
Cdd:cd02661 77 ISkhfrigrQEDAHEFLRYLLDAMQkACLDRFKKLKAVDpssqettlvqQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 332 NVLGMDSLERAFEAYTTSEILDDENKYDAGD-HGLQRAEKGVKFVELPPILHVQLMRFQYCGVEqKINERFSFPEKMNLA 410
Cdd:cd02661 157 DIKGADSLEDALEQFTKPEQLDGENKYKCERcKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGG-KINKQISFPETLDLS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 411 sccelgPMLT---EEDCVYSLHAVLVHSG-EFHGGHYVTYINvnlhesavdpTSSAKWCKFDDDVVSRTTTDDaivsnfg 486
Cdd:cd02661 236 ------PYMSqpnDGPLKYKLYAVLVHSGfSPHSGHYYCYVK----------SSNGKWYNMDDSKVSPVSIET------- 292
|
330
....*....|....*
gi 392920646 487 gekTMNSSAYMLVYV 501
Cdd:cd02661 293 ---VLSQKAYILFYI 304
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-500 |
1.32e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 144.17 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFYFTTGFRRAVYNMDVGTEPNESNIVLAMQRVFYELQMASEAVEtnSLTRAFgwdkLDA---- 269
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAE--APPDYF----LEAsrpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 270 -FN---QHDVQEFCRVLLDNLETkmkgtseekSIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVlgmDSLERAFEA 345
Cdd:cd02664 75 wFTpgsQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF---PSVQDLLNY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 346 YTTSEILDDENKYDAGD-HGLQRAEKGVKFVELPPILHVQLMRFQY---CGVEQKINERFSFPEKMNL-----------A 410
Cdd:cd02664 143 FLSPEKLTGDNQYYCEKcASLQDAEKEMKVTGAPEYLILTLLRFSYdqkTHVREKIMDNVSINEVLSLpvrveskssesP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 411 SCCELGPMLTEEDCV-----YSLHAVLVHSG-EFHGGHYVTY-----------INVNLHESAVDPTSSAKWCKFDDDVVS 473
Cdd:cd02664 223 LEKKEEESGDDGELVtrqvhYRLYAVVVHSGySSESGHYFTYardqtdadstgQECPEPKDAEENDESKNWYLFNDSRVT 302
|
330 340
....*....|....*....|....*...
gi 392920646 474 RTTTDDAI-VSNFGGEKTmnssAYMLVY 500
Cdd:cd02664 303 FSSFESVQnVTSRFPKDT----PYILFY 326
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-500 |
1.10e-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: 127.02 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFyfttgfrravynmdvgtepnesnivlamqrvfyelqmaseavetnsltrafgwdkldAFNQH 273
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL---------------------------------------------------------SADQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 274 DVQEFCRVLLDNLETKmkgtseeksIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNV------LGMDSLERAFEAYT 347
Cdd:cd02674 24 DAQEFLLFLLDGLHSI---------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLRLFT 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 348 TSEILDDENK-YDAGDHGLQRAEKGVKFVELPPILHVQLMRFQYCGVE-QKINERFSFP-EKMNLASCCELGPmlTEEDC 424
Cdd:cd02674 95 KEETLDGDNAwKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGStRKLTTPVTFPlNDLDLTPYVDTRS--FTGPF 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392920646 425 VYSLHAVLVHSGEFHGGHYVTYINVNlhesavdptSSAKWCKFDDDVVSRTTTDDAIvsnfggektmNSSAYMLVY 500
Cdd:cd02674 173 KYDLYAVVNHYGSLNGGHYTAYCKNN---------ETNDWYKFDDSRVTKVSESSVV----------SSSAYILFY 229
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-500 |
1.60e-30 |
|
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: 122.82 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFYFTTGFRRAVYNMD---VGTEPNESNIVLAMQRVFYELQMASEAVE----TNSLTRAF---- 262
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNparRGANQSSDNLTNALRDLFDTMDKKQEPVPpiefLQLLRMAFpqfa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 263 GWDKLDAFNQHDVQEFCRVLLDNLETKMKGTSEEKS-IPNLFRGNMKSYIKCLDVDY-ESSRTESFYDVQLN------VL 334
Cdd:cd02657 81 EKQNQGGYAQQDAEECWSQLLSVLSQKLPGAGSKGSfIDQLFGIELETKMKCTESPDeEEVSTESEYKLQCHisitteVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 335 GMDS-LERAF--EAYTTSEILDDENKYDagdhglqraeKGVKFVELPPILHVQLMRFQYCGVEQ---KINERFSFPEKMN 408
Cdd:cd02657 161 YLQDgLKKGLeeEIEKHSPTLGRDAIYT----------KTSRISRLPKYLTVQFVRFFWKRDIQkkaKILRKVKFPFELD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 409 LASCCelgpmltEEDCVYSLHAVLVHSGEF-HGGHYVTYINVNLHEsavdptssaKWCKFDDDVVSRTTTDDAIVSNFGG 487
Cdd:cd02657 231 LYELC-------TPSGYYELVAVITHQGRSaDSGHYVAWVRRKNDG---------KWIKFDDDKVSEVTEEDILKLSGGG 294
|
330
....*....|...
gi 392920646 488 EktmNSSAYMLVY 500
Cdd:cd02657 295 D---WHIAYILLY 304
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-501 |
6.75e-30 |
|
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: 121.71 E-value: 6.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSF--------YFTTGFRravYNMDVGTEPNESnIVLAMQRVFYELQmASEAVE----TNSLTRA 261
Cdd:cd02660 2 GLINLGATCFMNVILQALlhnpllrnYFLSDRH---SCTCLSCSPNSC-LSCAMDEIFQEFY-YSGDRSpygpINLLYLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 262 fgWDK---LDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIPN--------LFRGNMKSYIKCLDVDYESSRTESFYDVQ 330
Cdd:cd02660 77 --WKHsrnLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDEShcnciihqTFSGSLQSSVTCQRCGGVSTTVDPFLDLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 331 LNV---------------LGMDSLERAFEAYTTSEILDDENKYDAGDHGLQRAEKGVKFVELPPILHVQLMRFQY--CGV 393
Cdd:cd02660 155 LDIpnkstpswalgesgvSGTPTLSDCLDRFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHslNKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 394 EQKINERFSFPEKMNLASCCELGPMLT------EEDCVYSLHAVLVHSGEFHGGHYVTYINVNLHEsavdptssakWCKF 467
Cdd:cd02660 235 SRKIDTYVQFPLELNMTPYTSSSIGDTqdsnslDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQ----------WFKF 304
|
330 340 350
....*....|....*....|....*....|....
gi 392920646 468 DDDVVSRTTTddaivsnfggEKTMNSSAYMLVYV 501
Cdd:cd02660 305 DDAMITRVSE----------EEVLKSQAYLLFYH 328
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-500 |
2.15e-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: 119.34 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFYFttgfrravynmdvgtepneSNIVLAMQRVFYelQMASEAVETNSLTRAFGWDKLD----A 269
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-------------------ENLLTCLKDLFE--SISEQKKRTGVISPKKFITRLKreneL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 270 FN---QHDVQEFCRVLL----DNLETKMKGTSEEKSIPN-------------LFRGNMKSYIKCLDVDYESSRTESFYDV 329
Cdd:cd02663 60 FDnymHQDAHEFLNFLLneiaEILDAERKAEKANRKLNNnnnaepqptwvheIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 330 QLNVLGMDSLERAFEAYTTSEILDDENKYDAGD-HGLQRAEKGVKFVELPPILHVQLMRFQY---CGVEQKINERFSFPE 405
Cdd:cd02663 140 SIDVEQNTSITSCLRQFSATETLCGRNKFYCDEcCSLQEAEKRMKIKKLPKILALHLKRFKYdeqLNRYIKLFYRVVFPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 406 KMNLASCCELGpmlTEEDCVYSLHAVLVHSGE-FHGGHYVTYINvnlhesavdptSSAKWCKFDDDVVsrTTTDDAIVSN 484
Cdd:cd02663 220 ELRLFNTTDDA---ENPDRLYELVAVVVHIGGgPNHGHYVSIVK-----------SHGGWLLFDDETV--EKIDENAVEE 283
|
330
....*....|....*.
gi 392920646 485 FGGEKTMNSSAYMLVY 500
Cdd:cd02663 284 FFGDSPNQATAYVLFY 299
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-500 |
4.16e-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: 118.26 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFyFTTGFRRAVYNmdvgtePNESNIvlamqrvFYEL-QMASEavetnsltrafgwdkLDAFNQ 272
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNL-SQTPALRELLS------ETPKEL-------FSQVcRKAPQ---------------FKGYQQ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 273 HDVQEFCRVLLDNLETKmkgtseeksIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVL----GMDSLERAFEAYTT 348
Cdd:cd02667 52 QDSHELLRYLLDGLRTF---------IDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSdeikSECSIESCLKQFTE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 349 SEILDDENKYdaGDHGLQRAEKGVKFVELPPILHVQLMRFQ---YCGVeQKINERFSFPEKMNLASCCELGPMLTE--ED 423
Cdd:cd02667 123 VEILEGNNKF--ACENCTKAKKQYLISKLPPVLVIHLKRFQqprSANL-RKVSRHVSFPEILDLAPFCDPKCNSSEdkSS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 424 CVYSLHAVLVHSGEFHGGHYVTYINVN----------LHESAVDPT--SSAKWCKFDDDVVSRTTTddaivsnfggEKTM 491
Cdd:cd02667 200 VLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltKSKPAADEAgpGSGQWYYISDSDVREVSL----------EEVL 269
|
....*....
gi 392920646 492 NSSAYMLVY 500
Cdd:cd02667 270 KSEAYLLFY 278
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
194-502 |
2.63e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 101.42 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFYFTTgfrrAVYNMDVGTEPNESNivlAMQRV---------FYELQMASEAVETNSLTRaFGW 264
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYL----PKLDELLDDLSKELK---VLKNVirkpepdlnQEEALKLFTALWSSKEHK-VGW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 265 dKLDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIPnLFRGNMKSYIKCLDvDYESSRTEsfydvQLNVLGMDSLERAFE 344
Cdd:COG5533 73 -IPPMGSQEDAHELLGKLLDELKLDLVNSFTIRIFK-TTKDKKKTSTGDWF-DIIIELPD-----QTWVNNLKTLQEFID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 345 AYttSEILDDE----NKYDAGDHGLQRAEKGVKFVELPPILHVQLMRFQYCGVEQKI----NERFSFPEKMNlasccelG 416
Cdd:COG5533 145 NM--EELVDDEtgvkAKENEELEVQAKQEYEVSFVKLPKILTIQLKRFANLGGNQKIdtevDEKFELPVKHD-------Q 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 417 PMLTEEDCVYSLHAVLVHSGEFHGGHYVTYINVNlhesavdptssAKWCKFDDDVVSRTTTDDAIvsnfggeKTMNSSAY 496
Cdd:COG5533 216 ILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKG-----------GKWEKANDSDVTPVSEEEAI-------NEKAKNAY 277
|
....*.
gi 392920646 497 MLVYVR 502
Cdd:COG5533 278 LYFYER 283
|
|
| MATH |
pfam00917 |
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ... |
38-168 |
4.37e-21 |
|
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This domain is hugely expanded in the nematode C. elegans.
Pssm-ID: 425944 [Multi-domain] Cd Length: 113 Bit Score: 89.62 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 38 IDCFSKFMsRSDNRImSKPIIVRGIPWRIlaicrnqqgsrhsmnsRVNRSNFNFGFFLQCNNDELLQkrGMWRCYGTAVL 117
Cdd:pfam00917 1 IKNFSKIK-EGESYY-SPVEERFNIPWRL----------------QIYRKGGFLGLYLHCDKEEELE--RGWSIETEFTL 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 392920646 118 EVLNADGPSIQKKIHHSFHN-TEVDWG-FSNYDQYDTLCNPKDGYVVNDTIKL 168
Cdd:pfam00917 61 KLVSSNGKSVTKTDTHVFEKpKGWGWGkFISWDDLEKDYLVDDSITVEAHVKI 113
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-501 |
1.18e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 92.24 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 272 QHDVQEFCRVLLDNLETKMKGTSEEKSIPN--------LFRGnmKSYIKCLDVDYESSRTESFYDVQLNVLGMDSLERAF 343
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEksknpmvqLFYG--TFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHECL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 344 EAYTTSEILDDENKYDAGDHGLQRAekgvkFVELPPILHVQLMRFQY-CGVEQKINERFSFPekmnlasccelgPMLTEE 422
Cdd:cd02665 100 EAAMFEGEVELLPSDHSVKSGQERW-----FTELPPVLTFELSRFEFnQGRPEKIHDKLEFP------------QIIQQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392920646 423 DcvYSLHAVLVHSGEFHGGHYVTYINVNLHESavdptssakWCKFDDDVVSRTTTDDAIVSNFGGEKtmNSSAYMLVYV 501
Cdd:cd02665 163 P--YELHAVLVHEGQANAGHYWAYIYKQSRQE---------WEKYNDISVTESSWEEVERDSFGGGR--NPSAYCLMYI 228
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
193-500 |
1.21e-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: 94.57 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 193 IGLRNQGATCYMNSILQSFYFTTGFRRAVYNMdvgtepneSNIVLAMQrvfyELQMASEAVET--NSLTRAFGWDKL--- 267
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL--------VSLISSVE----QLQSSFLLNPEkyNDELANQAPRRLlna 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 268 --------DAFNQHDVQEFCRVLLDNLETKMKgtseeksipNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNV------ 333
Cdd:cd02671 93 lrevnpmyEGYLQHDAQEVLQCILGNIQELVE---------KDFQGQLVLRTRCLECETFTERREDFQDISVPVqesels 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 334 -------------LGMDSLERAFEAYTTSEILDDENKYDAGD-HGLQRAEKGVKFVELPPILHVQLMRFQYCGVE----- 394
Cdd:cd02671 164 kseesseispdpkTEMKTLKWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKLPEVITIHLKCFAANGSEfdcyg 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 395 --QKINERFSFPEKMnlaSCCELGPmlTEEDCVYSLHAVLVHSG-EFHGGHYVTYInvnlhesavdptssaKWCKFDDDV 471
Cdd:cd02671 244 glSKVNTPLLTPLKL---SLEEWST--KPKNDVYRLFAVVMHSGaTISSGHYTAYV---------------RWLLFDDSE 303
|
330 340
....*....|....*....|....*....
gi 392920646 472 VsRTTTDDAIVSNFGGEKTMNSSAYMLVY 500
Cdd:cd02671 304 V-KVTEEKDFLEALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-500 |
1.66e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 92.04 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSfyfttgfrravynmdvgtepnesnivLAmqrvfyelqmaseavetnSLTRAFGWdkLDAF-NQ 272
Cdd:cd02662 1 GLVNLGNTCFMNSVLQA--------------------------LA------------------SLPSLIEY--LEEFlEQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 273 HDVQEFCRVLLDNLETKMKgtseeksipNLFRGNMKSYIKCLDVDYESS-RTESFYDVQLNVL--GMDS---LERAFEAY 346
Cdd:cd02662 35 QDAHELFQVLLETLEQLLK---------FPFDGLLASRIVCLQCGESSKvRYESFTMLSLPVPnqSSGSgttLEHCLDDF 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 347 TTSEILDDENKYdagdhglqraEKGVKFVELPPILHVQLMRFQY--CGVEQKINERFSFPEkmnlasccELGPMLteedc 424
Cdd:cd02662 106 LSTEIIDDYKCD----------RCQTVIVRLPQILCIHLSRSVFdgRGTSTKNSCKVSFPE--------RLPKVL----- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 425 vYSLHAVLVHSGEFHGGHYVTY-----------INVNLHESAVDPTSSAKWCKFDDDVVSRTTTDDAIvsnfggektMNS 493
Cdd:cd02662 163 -YRLRAVVVHYGSHSSGHYVCYrrkplfskdkePGSFVRMREGPSSTSHPWWRISDTTVKEVSESEVL---------EQK 232
|
....*..
gi 392920646 494 SAYMLVY 500
Cdd:cd02662 233 SAYMLFY 239
|
|
| USP7_ICP0_bdg |
pfam12436 |
ICP0-binding domain of Ubiquitin-specific protease 7; This domain is one of two C-terminal ... |
679-860 |
1.19e-14 |
|
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: 74.85 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 679 TIYVEfsnnIERPLCEYDTARDLLFFVKYYDTMTDKFTIIGHTMFDCHKRFNLYRSMLCEMIGLPADTELKYYMEHAASY 758
Cdd:pfam12436 44 RLFLE----VAEELPPFDKNDDILLFLKYYDPEKQTLRGVGHVYVPKSSKVSDLVPIINERMGWPPDTPLLLYEEIKPNM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 759 LELVDLTQNYsigRLVEEQDGGILVVEKVETSTSTQ---NAKQKMNELFLDVEVEFVQSFynkKPEEEPFE-QFVKRICL 834
Cdd:pfam12436 120 IEIMKPKQTL---KKSELQDGDIICFQRELSEKEQDeypTAKDYYDFLLNRVEVTFRPKD---NPNDPGFTlELSKKMTY 193
|
170 180
....*....|....*....|....*.
gi 392920646 835 DDklftVAEEIGARLNVDPKKVLIWT 860
Cdd:pfam12436 194 DQ----LAEKVAERLGVDPTKLRFTT 215
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
193-501 |
2.82e-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: 75.61 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 193 IGLRNQGATCYMNSILQSFYFTTGFRRAVYNMDvGTEPNESNIVLAMQRV------FYELQMASEAV-ETNSL------- 258
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFD-ESKAELASDYPTERRIggrevsRSELQRSNQFVyELRSLfndlihs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 259 -TRAFGWDK---LDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIP-------------NLFRGNMK-SYIKCLDVDYES 320
Cdd:cd02666 81 nTRSVTPSKelaYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPdteddkeqsdlikRLFSGKTKqQLVPESMGNQPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 321 SRTESFYDVQLNVlgmDSLERAFEAYTTSEILDdenKYDAGDHGLQRAEKGvkfvELPPILHVQLMRFQYCGVE------ 394
Cdd:cd02666 161 VRTKTERFLSLLV---DVGKKGREIVVLLEPKD---LYDALDRYFDYDSLT----KLPQRSQVQAQLAQPLQRElismdr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 395 ---QKINERFSFPEKMNLASCCELGPMLTEE----------------DCVYSLHAVLVHSGEFHGGHYVTYINvnlhesa 455
Cdd:cd02666 231 yelPSSIDDIDELIREAIQSESSLVRQAQNElaelkheiekqfddlkSYGYRLHAVFIHRGEASSGHYWVYIK------- 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 392920646 456 vDPTSSAKWcKFDDDVVSRTTTDDAIvsnfggEKTMNSSA--YMLVYV 501
Cdd:cd02666 304 -DFEENVWR-KYNDETVTVVPASEVF------LFTLGNTAtpYFLVYV 343
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
194-469 |
1.39e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 73.07 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFYFTTGFRravyNMDV---GTE-PNESNIVLAMQRVFYELQMA----------SEAVETNSLT 259
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLR----NLALshlATEcLKEHCLLCELGFLFDMLEKAkgkncqasnfLRALSSIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 260 RAFG-----WDKLDAFN-QHDVQEFCRVLLDNL-----ETKMKGTSEEKSIPNLFRGNMKSYIKCLDVDYESSRTESFYD 328
Cdd:pfam13423 78 SALGlldedRETNSAISlSSLIQSFNRFLLDQLsseenSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 329 VQLNVLGM-DSLERAFEAYTTSEIL--------------DDENKYdagdhglQRAEKGVKFVELPPIL--HVQLMRFQYC 391
Cdd:pfam13423 158 LDLIYPRKpSSNNKKPPNQTFSSILkssleretttkawcEKCKRY-------QPLESRRTVRNLPPVLslNAALTNEEWR 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392920646 392 GVEQKINErfsFPEKMNLASCCELGpmLTEEDCVYSLHAVLVH-SGEFHGGHYVTYINVNlHESAVDPTSSaKWCKFDD 469
Cdd:pfam13423 231 QLWKTPGW---LPPEIGLTLSDDLQ--GDNEIVKYELRGVVVHiGDSGTSGHLVSFVKVA-DSELEDPTES-QWYLFND 302
|
|
| MATH |
cd00121 |
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ... |
32-173 |
4.30e-13 |
|
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: 67.02 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 32 GHLSLDIDCFSKFMSRSdnrIMSKPIIVRGIPWRILAICRNQqgsrhsmnsrvNRSNFNFGFFLQCNNDELLqkRGMWRC 111
Cdd:cd00121 1 GKHTWKIVNFSELEGES---IYSPPFEVGGYKWRIRIYPNGD-----------GESGDYLSLYLELDKGESD--LEKWSV 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392920646 112 YGTAVLEVLNAD-GPSIQKKIHHSFHN-TEVDWGFSNYDQYDTLCNPkdGYVVNDTIKLRCRFT 173
Cdd:cd00121 65 RAEFTLKLVNQNgGKSLSKSFTHVFFSeKGSGWGFPKFISWDDLEDS--YYLVDDSLTIEVEVK 126
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-500 |
6.66e-13 |
|
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: 70.81 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 194 GLRNQGATCYMNSILQSFYFTTGFRR------AVYNMDVgTEPNESnivLAMQ-----------RVFYELQMASEAVETN 256
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWryddleNKFPSDV-VDPAND---LNCQlikladgllsgRYSKPASLKSENDPYQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 257 SLTRAFGWDKLDAFN--------QHDVQEFCRVLLDNLETKMKGTSEEKsIPNLFRGNMKSYIKCLDVDYESSRTESFYD 328
Cdd:cd02658 77 VGIKPSMFKALIGKGhpefstmrQQDALEFLLHLIDKLDRESFKNLGLN-PNDLFKFMIEDRLECLSCKKVKYTSELSEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 329 VQLNVLGMD--------------SLERAFEAYTTSEILDDenkYDAGDHGLQRAEKGVKFVELPPILHVQLMRFQYC--G 392
Cdd:cd02658 156 LSLPVPKDEatekeegelvyepvPLEDCLKAYFAPETIED---FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLenW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 393 VEQKINERFSFPEkmnlasccELGPMlteedcVYSLHAVLVHSG-EFHGGHYVTYInvnlhESAVDPTSsaKWCKFDDDV 471
Cdd:cd02658 233 VPKKLDVPIDVPE--------ELGPG------KYELIAFISHKGtSVHSGHYVAHI-----KKEIDGEG--KWVLFNDEK 291
|
330 340
....*....|....*....|....*....
gi 392920646 472 VsrtttddAIVSNFGGEKTMnssAYMLVY 500
Cdd:cd02658 292 V-------VASQDPPEMKKL---GYIYFY 310
|
|
| MATH |
smart00061 |
meprin and TRAF homology; |
38-147 |
3.37e-11 |
|
meprin and TRAF homology;
Pssm-ID: 214496 [Multi-domain] Cd Length: 95 Bit Score: 60.78 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 38 IDCFSKFMSRSDN-RIMSKPIIVRGIPWRIlaicrnqqgsrhsmnsRVNRSNFNFGFFLQCNNDELLQKrgMWRCYGTAV 116
Cdd:smart00061 3 SHTFKNVSRLEEGeSYFSPSEEHFNIPWRL----------------KIYRKNGFLSLYLHCEKEECDSR--KWSIEAEFT 64
|
90 100 110
....*....|....*....|....*....|.
gi 392920646 117 LEVLNADGPSIQKKIHHSFHNtEVDWGFSNY 147
Cdd:smart00061 65 LKLVSQNGKSLSKKDKHVFEK-PSGWGFSKF 94
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
338-504 |
6.44e-08 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 56.82 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 338 SLERAFEAYTTSEILDDENK-YDAGDHGLQRAEKGVKFVELPPILHVQLMRFQYC-GVEQKINERFSFP-EKMNLASccE 414
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSwYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVrSFRDKIDDLVEYPiDDLDLSG--V 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 415 LGPMLTEEdCVYSLHAVLVHSGEFHGGHYVTYinvnlhesaVDPTSSAKWCKFDDDVVSRTTTDDAIvsnfggektmNSS 494
Cdd:COG5560 754 EYMVDDPR-LIYDLYAVDNHYGGLSGGHYTAY---------ARNFANNGWYLFDDSRITEVDPEDSV----------TSS 813
|
170
....*....|
gi 392920646 495 AYMLVYVRDN 504
Cdd:COG5560 814 AYVLFYRRKS 823
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
374-500 |
4.76e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 49.06 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 374 FVELPPILHVQLMRF-QYCGVEQKINERFSFPEKMNLAS--------CCELGPMLTEEDCVY-----------SLHAVLV 433
Cdd:cd02670 95 FAKAPSCLIICLKRYgKTEGKAQKMFKKILIPDEIDIPDfvaddpraCSKCQLECRVCYDDKdfsptcgkfklSLCSAVC 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392920646 434 HSG-EFHGGHYVTYINVN--LHESAVDPTSSAKWCKFDD-DVVSRTTTDDAIVSNFggektMNSSAYMLVY 500
Cdd:cd02670 175 HRGtSLETGHYVAFVRYGsySLTETDNEAYNAQWVFFDDmADRDGVSNGFNIPAAR-----LLEDPYMLFY 240
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
183-331 |
6.52e-04 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 44.10 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 183 MWDSKRHTGCIGLRNQGATCYMNSILQSFYFTTGFRRAVYNMDVGTEPNESNiVLAMQ----RVFYELQMASEAVETNSL 258
Cdd:COG5560 256 NRSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEN-PLGMHgsvaSAYADLIKQLYDGNLHAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 259 TRAFGWDKLDAFN-------QHDVQEFCRVLLDNL----------------------ETKMKGTSEEK----------SI 299
Cdd:COG5560 335 TPSGFKKTIGSFNeefsgydQQDSQEFIAFLLDGLhedlnriikkpytskpdlspgdDVVVKKKAKECwwehlkrndsII 414
|
170 180 190
....*....|....*....|....*....|..
gi 392920646 300 PNLFRGNMKSYIKCLDVDYESSRTESFYDVQL 331
Cdd:COG5560 415 TDLFQGMYKSTLTCPGCGSVSITFDPFMDLTL 446
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
267-500 |
2.01e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 41.36 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 267 LDAFNQHDVQEFCRVLLDNLETKMKGTSEEK-----SIPNL-----FRGNMKSYIKCLDVDYESSRTES--FYDVQLNVL 334
Cdd:cd02673 28 FDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVppsniEIKRLnpleaFKYTIESSYVCIGCSFEENVSDVgnFLDVSMIDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 335 GMDSLER-AFEAYTTSEIlddENKYDAGDHglQRAEKGVKFVELPPILHVQLMRFQycgveqkinERFSFPEkmNLASCC 413
Cdd:cd02673 108 KLDIDELlISNFKTWSPI---EKDCSSCKC--ESAISSERIMTFPECLSINLKRYK---------LRIATSD--YLKKNE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920646 414 ELGPMLTEEDCVYSLHAVLVHSGEF-HGGHYVTYINvnlhesavDPTSSAKWCKFDDDVVSRTTTDDAIvsnfggeKTMN 492
Cdd:cd02673 172 EIMKKYCGTDAKYSLVAVICHLGESpYDGHYIAYTK--------ELYNGSSWLYCSDDEIRPVSKNDVS-------TNAR 236
|
....*...
gi 392920646 493 SSAYMLVY 500
Cdd:cd02673 237 SSGYLIFY 244
|
|
| |
