|
Name |
Accession |
Description |
Interval |
E-value |
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
96-1141 |
0e+00 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 660.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 96 AEEDMEDdtswRSEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMvmprFYPDRPHQKSVGFFL----QCNAESDSTSW 171
Cdd:COG5077 29 FDPDVEE----LLEMSFTWKVKRWSELAKKVESPPFSVGGHTWKII----LFPQGNNQCNVSVYLeyepQELEETGGKYY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 172 SCHAQAVLKIINYRDDDKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKG---FIDDDKVTFEVFVQA-DAPHGVAW- 246
Cdd:COG5077 101 DCCAQFAFDISNPKYPTIEYINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGrppFLEEGTLVITVYVRVlKDPTGVLWh 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 247 -----DSKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKLT 321
Cdd:COG5077 181 sflnyNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 322 KSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKGKKNI 401
Cdd:COG5077 261 RSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 402 FESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKT 481
Cdd:COG5077 341 QESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 482 DPK---DPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGG----HD---DDLSVRHC 551
Cdd:COG5077 421 ADKsenSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpyKDkirDHSGIKRF 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 552 TNAYMLVYIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQKRKERQEAHLYMQVQIVAEDQFCGHQGNDMYD----E 627
Cdd:COG5077 501 MSAYMLVYLRKSMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDYPDfsseL 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 628 EKVRYTVFKVLKNSSLAEFVQSLSQTMGFPQD-QIRLWPMQARSNGTKRPAMLDNEAdgNKTMIELSDNEN--------P 698
Cdd:COG5077 581 NDSGLAQFVIKRGAKISDLRNNIAEHLNTPQSlYLREWTMIKRHNKTVRVDRPCNRV--NITTRELVGMNTrtgeelrsY 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 699 WTIFLETVdpELAAS-GATLpkfDKDHDVMLFLKMYDPKTRSLNYCGHIYTPISCKIRDLLPVMCDRagFIQDTSLILYE 777
Cdd:COG5077 659 LERIIEHN--QLDSQrKVAL---TKDGVINIFVKYFDYTTQPISGFGGLHVNKFLKISSISPWIEDS--ISSNLPLTLYE 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 778 EVKPNLTERIQDyDVSLDKAldELMDGDIIVFQK-DDPENDNSE-LPTAKEYFRDLYHRVDVIFCDKTIPNDPG-FVVTL 854
Cdd:COG5077 732 EIKPGMVDTIGD-NITFIGS--EIGTGDIICFEVpGAVEFDTSSaYDSALKLYDFLQGRVLVAFRRFSDEYRENvFEFLL 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 855 SNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRHNYEGTLRD-LLQFFKPRQPKKLYYQQLKMKITDFENRR 933
Cdd:COG5077 809 FIGDFYDDLCRNVSCKLHVTPFYLRGTKSTELEDRIRRVVGSKSIFLLKEaLSSSSEFRQAPVDFYEVLDVPLSELERKR 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 934 SFKCIWL-NSQFREEEITLYPDKHGCVRDLLEECKKAVELGDKASGRLRLLEIVSYKIIGVHQEDELLECLSPATsrTFR 1012
Cdd:COG5077 889 LIRLCFLsNGYQHVYLAEFYVEKDYTAVDHLHIVVTKVGCTDELKKSVLVYEVVNLRPVRGHSLKTLIIDDNVRS--TLY 966
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 1013 IEEIPLDQVDIdKENEMLITVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEKEFEKFKFAIV-------M 1085
Cdd:COG5077 967 GEVFPLEQEQL-TTNEMCVVVQHFFKDLIRTHGIPFMFVIVPFETFLDTKVRLVARFGYKYKLFSKIKLFVGksytdgeL 1045
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*.
gi 568995352 1086 MGRHQYINEDEYEVNLkdFEPQPGNMshprpwlgLDHfnkAPKRSRYTYLEKAIKI 1141
Cdd:COG5077 1046 DWPMSYFNDEDILYDL--IERLDYIL--------LDH---PDRLRSHSSYDRAIIM 1088
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
253-564 |
3.46e-161 |
|
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: 480.99 E-value: 3.46e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 253 GYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMM-PTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKL---TKSFGWET 328
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIpPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELtdkTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 329 LDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKGKKNIFESFVDY 408
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 409 VAVEQLDGDNKYDAGEHGLQ-EAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKT------ 481
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKvDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGlakkeg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 482 ----DPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDD-------DLSVRH 550
Cdd:cd02659 241 dsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGEETqktydsgPRAFKR 320
|
330
....*....|....
gi 568995352 551 CTNAYMLVYIRESK 564
Cdd:cd02659 321 TTNAYMLFYERKSP 334
|
|
| USP7_ICP0_bdg |
pfam12436 |
ICP0-binding domain of Ubiquitin-specific protease 7; This domain is one of two C-terminal ... |
661-906 |
1.31e-106 |
|
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: 333.71 E-value: 1.31e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 661 IRLWPMQARSNGTKRPAMLDNEADGNKTMIELSDN----ENPWTIFLETVDPelaasgatLPKFDKDHDVMLFLKMYDPK 736
Cdd:pfam12436 1 IRLWPMVNRQNKTVRPDQPLPEADPAKTVEEIRDKmatrDNPLRLFLEVAEE--------LPPFDKNDDILLFLKYYDPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 737 TRSLNYCGHIYTPISCKIRDLLPVMCDRAGFIQDTSLILYEEVKPNLTErIQDYDVSLDKAldELMDGDIIVFQKDDPEN 816
Cdd:pfam12436 73 KQTLRGVGHVYVPKSSKVSDLVPIINERMGWPPDTPLLLYEEIKPNMIE-IMKPKQTLKKS--ELQDGDIICFQRELSEK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 817 DNSELPTAKEYFRDLYHRVDVIFCDKTIPNDPGFVVTLSNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRH 896
Cdd:pfam12436 150 EQDEYPTAKDYYDFLLNRVEVTFRPKDNPNDPGFTLELSKKMTYDQLAEKVAERLGVDPTKLRFTTVNNYSGQPKTPIKR 229
|
250
....*....|
gi 568995352 897 NYEGTLRDLL 906
Cdd:pfam12436 230 NPNQTLKDIL 239
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
255-559 |
6.46e-87 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 283.56 E-value: 6.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 255 VGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDS----SKSVPLALQRVFYELQH--SDKPVGTKKLTKSFGW-- 326
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSrynkDINLLCALRDLFKALQKnsKSSSVSPKMFKKSLGKln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 327 ETLDSFMQHDVQELCRVLLDNVENKMKG---TCVEGTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKGKKN--- 400
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 401 ---IFESFVDYVAVEQLDGDNKYD-AGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpqTDQNIKINDRFEFPEQLPLDE 476
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYcDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 477 FLQKTDPKDPAN---YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHnygghdddlsvrhcTN 553
Cdd:pfam00443 239 YLAEELKPKTNNlqdYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS--------------SS 304
|
....*.
gi 568995352 554 AYMLVY 559
Cdd:pfam00443 305 AYILFY 310
|
|
| MATH_HAUSP |
cd03772 |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ... |
108-243 |
1.96e-83 |
|
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: 267.01 E-value: 1.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 108 SEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRFYPDR-PHQKSVGFFLQCNAESDSTSWSCHAQAVLKIINYRD 186
Cdd:cd03772 1 SEATFSFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRNYPDRnPHQKSVGFFLQCNAESDSTSWSCHAQAVLRIINYKD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568995352 187 DDKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKGFIDDDKVTFEVFVQADAPHG 243
Cdd:cd03772 81 DEPSFSRRISHLFFSKENDWGFSNFMTWSEVTDPEKGFIEDDTITLEVYVQADAPHG 137
|
|
| USP7_C2 |
pfam14533 |
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ... |
916-1127 |
1.19e-66 |
|
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: 223.13 E-value: 1.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 916 KLYYQQLKMKITDFENRRSFKCIWLNSQF-REEEITLYPDKHGCVRDLLEECKKAVELGDKASGRLRLLEIVSYKIIGVH 994
Cdd:pfam14533 1 ALYYEVLDISLSELENKKSIKVTWLSPGLkKEEELELLVPKNGTVADLLEELQKKVKLSEEGSGKIRLYEVSNHKIYKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 995 QEDELLECLSPATsrTFRIEEIPLDQVDIDkENEMLITVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEK 1074
Cdd:pfam14533 81 SEDEPIDSLNDYL--TLYAEEIPEEELNLD-EGERLIPVFHFQKEPSRTHGIPFLFVLKPGEPFSDTKKRLQKRLGLPDK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568995352 1075 EFEKFKFAIVMMGRH-QYINEDEyevNLKDFEPQPGNMshprPWLGLDHFNKAP 1127
Cdd:pfam14533 158 EFEKIKFALVQRGKKpEYLEDDD---VLFDLLGQPDDL----PWLGLDHPDKTP 204
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
256-560 |
4.01e-61 |
|
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: 209.65 E-value: 4.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLFFtnqlrkavymmptegddssksvplalqrvfyelqhsdkpvgtkkltksfgwetldsfMQH 335
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS---------------------------------------------------------EQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 336 DVQELCRVLLDNVENKMKGTCVEG--------TIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSI----KGKKNIFE 403
Cdd:cd02257 24 DAHEFLLFLLDKLHEELKKSSKRTsdssslksLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVSLED 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 404 SFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQtDQNIKINDRFEFPEQLPLDEFLQKTDP 483
Cdd:cd02257 104 CLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELDLSPYLSEGEK 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 484 KDPAN-----YILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHdddlsvrhctNAYML 557
Cdd:cd02257 183 DSDSDngsykYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSS----------SAYIL 252
|
...
gi 568995352 558 VYI 560
Cdd:cd02257 253 FYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-559 |
1.62e-57 |
|
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: 201.88 E-value: 1.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLA-----------LQRVFYELQHSDK----PVGtkkL 320
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDkphepqtiidqLQLIFAQLQFGNRsvvdPSG---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 321 TKSFGwetLDSFMQHDVQELCRVLLDNVENKM---KGTCVEGTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKG 397
Cdd:cd02668 78 VKALG---LDTGQQQDAQEFSKLFLSLLEAKLsksKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 398 KKNIFESFVDYVAVEQLDGDNKYDAGEHG-LQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDE 476
Cdd:cd02668 155 HKTLEECIDEFLKEEQLTGDNQYFCESCNsKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 477 FLQKTDPKDpANYILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRCTK---EEAIEHNYGGHD--DDLSVRH 550
Cdd:cd02668 235 YLAESDEGS-YVYELSGVLIHQGVSaYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGkplKLGNSEDPAKPRksEIKKGTH 313
|
330
....*....|
gi 568995352 551 CT-NAYMLVY 559
Cdd:cd02668 314 SSrTAYMLVY 323
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-559 |
4.63e-37 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 141.68 E-value: 4.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLFFTNQLRkavymmptegddssksvplALQRVFYELQHSDKPVGT-------KKLTKSFgwET 328
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT-------------------CLKDLFESISEQKKRTGVispkkfiTRLKREN--EL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 329 LDSFMQHDVQELCRVLLDNV------ENKMKGTCVEGT-----------IPKLFRGKMVSYIQCKDVDYRSDRREDYYDI 391
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIaeildaERKAEKANRKLNnnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 392 QLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPE 470
Cdd:cd02663 140 SIDVEQNTSITSCLRQFSATETLCGRNKFYCDEcCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 471 QLPLdeFLQKTDPKDPAN-YILHAVLVH--SGDNHgGHYVVYLnpKGDGKWCKFDDDVVSRcTKEEAIEHNYGGHdddls 547
Cdd:cd02663 220 ELRL--FNTTDDAENPDRlYELVAVVVHigGGPNH-GHYVSIV--KSHGGWLLFDDETVEK-IDENAVEEFFGDS----- 288
|
330
....*....|..
gi 568995352 548 vRHCTNAYMLVY 559
Cdd:cd02663 289 -PNQATAYVLFY 299
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-560 |
7.64e-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: 138.56 E-value: 7.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLFFTNQLrkAVYMmPTEGDDSSKSVPL-----ALQR-VFYELQHSDKPVGTKKLT---KSFgW 326
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPL--ANYL-LSREHSKDCCNEGfcmmcALEAhVERALASSGPGSAPRIFSsnlKQI-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 327 ETLDSFMQHDVQELCRVLLDnvenKMKGTCVEG---------------TIPKLFRGKMVSYIQCKDVDYRSDRREDYYDI 391
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLLD----AMQKACLDRfkklkavdpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 392 QLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFmydpQTDQNIKINDRFEFPE 470
Cdd:cd02661 155 SLDIKGADSLEDALEQFTKPEQLDGENKYKCERcKKKVKASKQLTIHRAPNVLTIHLKRF----SNFRGGKINKQISFPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 471 QLPLDEFL-QKTDPkdPANYILHAVLVHSG-DNHGGHYVVYLnpKG-DGKWCKFDDDVVSRCTKEEAiehnygghdddLS 547
Cdd:cd02661 231 TLDLSPYMsQPNDG--PLKYKLYAVLVHSGfSPHSGHYYCYV--KSsNGKWYNMDDSKVSPVSIETV-----------LS 295
|
330
....*....|...
gi 568995352 548 vrhcTNAYMLVYI 560
Cdd:cd02661 296 ----QKAYILFYI 304
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-559 |
1.18e-33 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 132.07 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLFFTNQLRKAV-YMMPTEGDDSSKSVPL--ALQRVFYELQHSDKPVGTKKLTKSFG-----WE 327
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALkNYNPARRGANQSSDNLtnALRDLFDTMDKKQEPVPPIEFLQLLRmafpqFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 328 TLDS---FMQHDVQELCRVLLDNVENKMKGTCVEG-TIPKLFRGKMVSYIQCKDVDYRSD-RREDYYDIQLSIKGKknif 402
Cdd:cd02657 81 EKQNqggYAQQDAEECWSQLLSVLSQKLPGAGSKGsFIDQLFGIELETKMKCTESPDEEEvSTESEYKLQCHISIT---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 403 eSFVDYVaVEQLdgdnkydagEHGLQEAE--------------KGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEF 468
Cdd:cd02657 157 -TEVNYL-QDGL---------KKGLEEEIekhsptlgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 469 PEQLPLDEFLQKTdpkdpANYILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRcTKEEAIEHNYGGHDDDLs 547
Cdd:cd02657 226 PFELDLYELCTPS-----GYYELVAVITHQGRSaDSGHYVAWVRRKNDGKWIKFDDDKVSE-VTEEDILKLSGGGDWHI- 298
|
330
....*....|..
gi 568995352 548 vrhctnAYMLVY 559
Cdd:cd02657 299 ------AYILLY 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-560 |
8.35e-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: 124.32 E-value: 8.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLfftnqlrkavymmptegddssksvplalqrvfyelqhsdkpvgtkkltksfgwetldSFMQH 335
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL---------------------------------------------------------SADQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 336 DVQELCRVLLDNVENKmkgtcvegtIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKGKK------NIFESFVDYV 409
Cdd:cd02674 24 DAQEFLLFLLDGLHSI---------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFT 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 410 AVEQLDGDNK-YDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFP-EQLPLDEFLQKTDPKDPA 487
Cdd:cd02674 95 KEETLDGDNAwKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTR--KLTTPVTFPlNDLDLTPYVDTRSFTGPF 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568995352 488 NYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEhnygghdddlsvrhcTNAYMLVYI 560
Cdd:cd02674 173 KYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVS---------------SSAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-559 |
2.39e-31 |
|
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: 126.07 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTkkltksfgweTLDSFM-- 333
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEA----------PPDYFLea 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 334 ----------QHDVQELCRVLLDNVENkmkgtcvegTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKgkknIFE 403
Cdd:cd02664 71 srppwftpgsQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP----SVQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 404 SFVDY-VAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPE--QLPLDEFLQ 479
Cdd:cd02664 138 DLLNYfLSPEKLTGDNQYYCEKcASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEvlSLPVRVESK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 480 KTDPKD----------------PANYILHAVLVHSG-DNHGGHYVVYL-NPKG-------------------DGKWCKFD 522
Cdd:cd02664 218 SSESPLekkeeesgddgelvtrQVHYRLYAVVVHSGySSESGHYFTYArDQTDadstgqecpepkdaeendeSKNWYLFN 297
|
330 340 350
....*....|....*....|....*....|....*..
gi 568995352 523 DDVVSRCTKEEAiehnygghDDDLSVRHCTNAYMLVY 559
Cdd:cd02664 298 DSRVTFSSFESV--------QNVTSRFPKDTPYILFY 326
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-571 |
9.41e-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: 117.10 E-value: 9.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEgddssksvplalqrVFYELQHSDKpvgtkkltksfgweTLDSFMQH 335
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAP--------------QFKGYQQQ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 336 DVQELCRVLLDNVENkmkgtcvegTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQL----SIKGKKNIFESFVDYVAV 411
Cdd:cd02667 53 DSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 412 EQLDGDNKYdaGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQnIKINDRFEFPEQLPLDEFLqktDPKDPAN--- 488
Cdd:cd02667 124 EILEGNNKF--ACENCTKAKKQYLISKLPPVLVIHLKRFQQPRSANL-RKVSRHVSFPEILDLAPFC---DPKCNSSedk 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 489 ----YILHAVLVHSGDNHGGHYV--VYLNPKGDgkwckFDDDVVSRCTKEEAIEHNYGghdddlSVRHCTNAymlvYIRE 562
Cdd:cd02667 198 ssvlYRLYGVVEHSGTMRSGHYVayVKVRPPQQ-----RLSDLTKSKPAADEAGPGSG------QWYYISDS----DVRE 262
|
....*....
gi 568995352 563 SKLSEVLQA 571
Cdd:cd02667 263 VSLEEVLKS 271
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-560 |
8.00e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 115.55 E-value: 8.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLFFTNQLRKavYMM------PTEGDDSSKSVPLALQRVFYELQHSDKPVG---TKKLTKSfgW 326
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRN--YFLsdrhscTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPygpINLLYLS--W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 327 ---ETLDSFMQHDVQELCRVLLD-----------NVENKMKGTCVegtIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQ 392
Cdd:cd02660 78 khsRNLAGYSQQDAHEFFQFLLDqlhthyggdknEANDESHCNCI---IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 393 LSIKGKKNIF----ESFVD-----------YVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpQTD 457
Cdd:cd02660 155 LDIPNKSTPSwalgESGVSgtptlsdcldrFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 458 QNIKINDRFEFPEQLPLDEFL-------QKTDPKDPAN-YILHAVLVHSGDNHGGHYVVYLNpKGDGKWCKFDDDVVSRC 529
Cdd:cd02660 234 TSRKIDTYVQFPLELNMTPYTsssigdtQDSNSLDPDYtYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRV 312
|
330 340 350
....*....|....*....|....*....|.
gi 568995352 530 TKEEaiehnygghdddlsVRHCtNAYMLVYI 560
Cdd:cd02660 313 SEEE--------------VLKS-QAYLLFYH 328
|
|
| MATH |
cd00121 |
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ... |
111-237 |
5.33e-25 |
|
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: 101.30 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 111 TFQFTVERFSRL-SESVLSPPCFVRNLPWKIMVMPRFypDRPHQKSVGFFLQC-NAESDSTSWSCHAQAVLKIINyRDDD 188
Cdd:cd00121 2 KHTWKIVNFSELeGESIYSPPFEVGGYKWRIRIYPNG--DGESGDYLSLYLELdKGESDLEKWSVRAEFTLKLVN-QNGG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568995352 189 KSFSRRISHLFF-HKENDWGFSNFMAWSEVTDPekGFIDDDKVTFEVFVQ 237
Cdd:cd00121 79 KSLSKSFTHVFFsEKGSGWGFPKFISWDDLEDS--YYLVDDSLTIEVEVK 126
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
249-559 |
9.75e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 106.90 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 249 KKHTG---YVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGddSSKSvplALQRVF------YELQHSDKPVGTKK 319
Cdd:cd02671 16 EKRENllpFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI--SSVE---QLQSSFllnpekYNDELANQAPRRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 320 LTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKgtcvegtipKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKGK- 398
Cdd:cd02671 91 NALREVNPMYEGYLQHDAQEVLQCILGNIQELVE---------KDFQGQLVLRTRCLECETFTERREDFQDISVPVQESe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 399 ------------------KNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQN 459
Cdd:cd02671 162 lskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 460 I----KINDRFEFPEQLPLDEFlqKTDPKDPAnYILHAVLVHSGDN-HGGHYVVYLnpkgdgKWCKFDDDVVSRCTKEEA 534
Cdd:cd02671 242 YgglsKVNTPLLTPLKLSLEEW--STKPKNDV-YRLFAVVMHSGATiSSGHYTAYV------RWLLFDDSEVKVTEEKDF 312
|
330 340
....*....|....*....|....*..
gi 568995352 535 IEhnygghddDLS--VRHCTNAYMLVY 559
Cdd:cd02671 313 LE--------ALSpnTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
256-561 |
2.43e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 92.56 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLFFTN--------QLRKAVYMMPTEGDDSSKsvPLALQRVFYELqhsdKPVGTKKLTKsFGWE 327
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLpkldelldDLSKELKVLKNVIRKPEP--DLNQEEALKLF----TALWSSKEHK-VGWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 328 TlDSFMQHDVQELCRVLLDNVENKMKGTcveGTIPKLFRGKmvsyiqckdvDYRSDRREDYYDI------QLSIKGKKNi 401
Cdd:COG5533 74 P-PMGSQEDAHELLGKLLDELKLDLVNS---FTIRIFKTTK----------DKKKTSTGDWFDIiielpdQTWVNNLKT- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 402 FESFVDyvAVEQLDGD-----NKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpqtDQNIKINDRFEFPEQLPLde 476
Cdd:COG5533 139 LQEFID--NMEELVDDetgvkAKENEELEVQAKQEYEVSFVKLPKILTIQLKRFANL---GGNQKIDTEVDEKFELPV-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 477 flqKTDPKDPAN----YILHAVLVHSGDNHGGHYVVYLnpKGDGKWCKFDDDVVSRCTKEEAIEHNygghdddlsvrhCT 552
Cdd:COG5533 212 ---KHDQILNIVketyYDLVGFVLHQGSLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINEK------------AK 274
|
....*....
gi 568995352 553 NAYMLVYIR 561
Cdd:COG5533 275 NAYLYFYER 283
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-559 |
3.88e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 83.53 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLF--------------------------FTNQLRKAVYMMPTEgdDSSKSVPLALQRVFYelQ 309
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwryddlenkfpsdvvdpandLNCQLIKLADGLLSG--RYSKPASLKSENDPY--Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 310 HSDKPVGTKKLTkSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTcvEGTIP-KLFRGKMVSYIQCKDVDYRSDRREDY 388
Cdd:cd02658 77 VGIKPSMFKALI-GKGHPEFSTMRQQDALEFLLHLIDKLDRESFKN--LGLNPnDLFKFMIEDRLECLSCKKVKYTSELS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 389 YDIQLSI---------KGKK-----NIFESFVDYVAVEQLDgDNKYDAGEHGlqEAEKGVKFLTLPPVLHLQLMRFMYDP 454
Cdd:cd02658 154 EILSLPVpkdeatekeEGELvyepvPLEDCLKAYFAPETIE-DFCSTCKEKT--TATKTTGFKTFPDYLVINMKRFQLLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 455 QTDQnIKINDRFEFPEQLpldeflqktdpkDPANYILHAVLVHSGDN-HGGHYVVYL--NPKGDGKWCKFDDDVVSRCTK 531
Cdd:cd02658 231 NWVP-KKLDVPIDVPEEL------------GPGKYELIAFISHKGTSvHSGHYVAHIkkEIDGEGKWVLFNDEKVVASQD 297
|
330 340
....*....|....*....|....*...
gi 568995352 532 EEAIEhnygghdddlsvrhcTNAYMLVY 559
Cdd:cd02658 298 PPEMK---------------KLGYIYFY 310
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-560 |
2.23e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 76.83 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLFFTNQlrkavymmptegdDSSKSvplalqrvfyelqhsdkpvgtkkLTKSFGWETlDSFmqh 335
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLFSQQQ-------------DVSEF-----------------------THLLLDWLE-DAF--- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 336 DVQELCRVLLDNVENKMKgtcvegtipKLFRGK--MVSYIQCKdvdyRSDRREDYYDIQLSIKGKKNIFEsfvdyvAVE- 412
Cdd:cd02665 41 QAAAEAISPGEKSKNPMV---------QLFYGTflTEGVLEGK----PFCNCETFGQYPLQVNGYGNLHE------CLEa 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 413 -QLDGDNKYDAGEHGLQEAEKGVkFLTLPPVLHLQLMRFMYDpqTDQNIKINDRFEFPEQLpldeflqktdpkDPANYIL 491
Cdd:cd02665 102 aMFEGEVELLPSDHSVKSGQERW-FTELPPVLTFELSRFEFN--QGRPEKIHDKLEFPQII------------QQVPYEL 166
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568995352 492 HAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDdlsvrhcTNAYMLVYI 560
Cdd:cd02665 167 HAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRN-------PSAYCLMYI 228
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-559 |
5.32e-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: 75.87 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 256 GLKNQGATCYMNSLLQTLfftnqlrkavymmptegdDSSKSVPlalqrvfyelqhsdkpvgtkkltksfgwETLDSFM-Q 334
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL------------------ASLPSLI----------------------------EYLEEFLeQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 335 HDVQELCRVLLDNVENKMKGtcvegtipkLFRGKMVSYIQCKDVDYRSDRRED-YYDIQLSIKGKKNIFESFVDyvavEQ 413
Cdd:cd02662 35 QDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSKVRYEsFTMLSLPVPNQSSGSGTTLE----HC 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 414 LDGDNKydagehglQEAEKGVK-------FLTLPPVLHLQLMRFMYDPQtDQNIKINDRFEFPEQLPldeflqktDPKdp 486
Cdd:cd02662 102 LDDFLS--------TEIIDDYKcdrcqtvIVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP--------KVL-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 487 anYILHAVLVHSGDNHGGHYVVY----LNPKG----------------DGKWCKFDDDVVSRCTKEEAIEHNYgghdddl 546
Cdd:cd02662 163 --YRLRAVVVHYGSHSSGHYVCYrrkpLFSKDkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQKS------- 233
|
330
....*....|...
gi 568995352 547 svrhctnAYMLVY 559
Cdd:cd02662 234 -------AYMLFY 239
|
|
| MATH |
smart00061 |
meprin and TRAF homology; |
115-212 |
6.86e-15 |
|
meprin and TRAF homology;
Pssm-ID: 214496 [Multi-domain] Cd Length: 95 Bit Score: 71.18 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 115 TVERFSRLS--ESVLSPPCFVRNLPWKIMVMPRfypdrphQKSVGFFLQCNAE-SDSTSWSCHAQAVLKIINYrdDDKSF 191
Cdd:smart00061 5 TFKNVSRLEegESYFSPSEEHFNIPWRLKIYRK-------NGFLSLYLHCEKEeCDSRKWSIEAEFTLKLVSQ--NGKSL 75
|
90 100
....*....|....*....|.
gi 568995352 192 SRRISHLfFHKENDWGFSNFM 212
Cdd:smart00061 76 SKKDKHV-FEKPSGWGFSKFI 95
|
|
| MATH |
pfam00917 |
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ... |
119-236 |
2.96e-13 |
|
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: 67.28 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 119 FSRL--SESVLSPPCFVRNLPWKIMVmprfypdRPHQKSVGFFLQCNA-ESDSTSWSCHAQAVLKIINyrDDDKSFSRRI 195
Cdd:pfam00917 4 FSKIkeGESYYSPVEERFNIPWRLQI-------YRKGGFLGLYLHCDKeEELERGWSIETEFTLKLVS--SNGKSVTKTD 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568995352 196 SHLFfHKENDWGFSNFMAWSEVtdpEKGFIDDDKVTFEVFV 236
Cdd:pfam00917 75 THVF-EKPKGWGWGKFISWDDL---EKDYLVDDSITVEAHV 111
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
255-560 |
3.27e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 69.44 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 255 VGLKNQGATCYMNSLLQTLFFTNQLRKAV------YMMPTEGDDSSKSVP----------------LALQRVFYELQHSD 312
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVlnfdesKAELASDYPTERRIGgrevsrselqrsnqfvYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 313 KPVGT--KKLTksfgwetLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKmVSYIQCKDVDYRSDRREDYYD 390
Cdd:cd02666 82 TRSVTpsKELA-------YLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDK-EQSDLIKRLFSGKTKQQLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 391 IQLSIKGKKNIFESF----VDYV-----AVEQLDGDNKYDAGEHGLQEAEKGvkflTLPPVLHLQL------------MR 449
Cdd:cd02666 154 SMGNQPSVRTKTERFlsllVDVGkkgreIVVLLEPKDLYDALDRYFDYDSLT----KLPQRSQVQAqlaqplqrelisMD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 450 FMYDPQTDQNIKINDRFEFPEQLPLDEFLQKT-------------DPKDPAnYILHAVLVHSGDNHGGHYVVYLNPKGDG 516
Cdd:cd02666 230 RYELPSSIDDIDELIREAIQSESSLVRQAQNElaelkheiekqfdDLKSYG-YRLHAVFIHRGEASSGHYWVYIKDFEEN 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568995352 517 KWCKFDDDVVSRCTKEEAIEHNYGGHDddlsvrhctNAYMLVYI 560
Cdd:cd02666 309 VWRKYNDETVTVVPASEVFLFTLGNTA---------TPYFLVYV 343
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
412-563 |
9.95e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 62.98 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 412 EQLD-GDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFPeqlpLDEFL--QKTDPKDPAN 488
Cdd:COG5560 688 EQLGlSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD--KIDDLVEYP----IDDLDlsGVEYMVDDPR 761
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995352 489 --YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEhnygghdddlsvrhcTNAYMLVYIRES 563
Cdd:COG5560 762 liYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT---------------SSAYVLFYRRKS 823
|
|
| MATH_Ubp21p |
cd03775 |
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ... |
112-236 |
1.03e-09 |
|
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: 57.75 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 112 FQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRfypdRPHQ-KSVGFFL----QCNAES-DSTSWSCHAQAVLKIINYR 185
Cdd:cd03775 3 FTWRIKNWSELEKKVHSPKFKCGGFEWRILLFPQ----GNSQtGGVSIYLephpEEEEKApLDEDWSVCAQFALVISNPG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568995352 186 DDDKSFSRRISHLFFHKENDWGFSNFMAWS--EVTDPEK--GFIDDDKVTFEVFV 236
Cdd:cd03775 79 DPSIQLSNVAHHRFNAEDKDWGFTRFIELRklAHRTPDKpsPFLENGELNITVYV 133
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
250-346 |
5.43e-08 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 57.20 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 250 KHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKavYMMPTEGDDS-SKSVPLA----LQRVFYEL--------QHSDKPVG 316
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRD--YFLSDEYEESiNEENPLGmhgsVASAYADLikqlydgnLHAFTPSG 338
|
90 100 110
....*....|....*....|....*....|
gi 568995352 317 TKKLTKSFgWETLDSFMQHDVQELCRVLLD 346
Cdd:COG5560 339 FKKTIGSF-NEEFSGYDQQDSQEFIAFLLD 367
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
255-523 |
2.94e-06 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 50.35 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 255 VGLKNQGATCYMNSLLQTLFFTNQLRKAV----------------------YMMptegDDSSKSVPLA--LQRVF----- 305
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAlshlateclkehcllcelgflfDML----EKAKGKNCQAsnFLRALssipe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 306 ---YEL-QHSDKPVGTKKLTksfgwetldsfmqHDVQELCRVLLDNV---ENKMKGTCVEGT--IPKLFRGKMVSYIQCK 376
Cdd:pfam13423 77 asaLGLlDEDRETNSAISLS-------------SLIQSFNRFLLDQLsseENSTPPNPSPAEspLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 377 DVDYRSDRREDYYDIQL------SIKGKKNIFESFVDYVA--VEQLDGD-------NKYDagehgLQEAEKGVKflTLPP 441
Cdd:pfam13423 144 NCGHESVRESSTHVLDLiyprkpSSNNKKPPNQTFSSILKssLERETTTkawcekcKRYQ-----PLESRRTVR--NLPP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 442 VLHLQLMrfMYDPQTDQNIKINDrfEFPEQLPLDEFLQKTDPKDPANYILHAVLVH-SGDNHGGHYV-------VYLNPK 513
Cdd:pfam13423 217 VLSLNAA--LTNEEWRQLWKTPG--WLPPEIGLTLSDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVsfvkvadSELEDP 292
|
330
....*....|
gi 568995352 514 GDGKWCKFDD 523
Cdd:pfam13423 293 TESQWYLFND 302
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
436-523 |
2.03e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 41.36 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995352 436 FLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFPEQLPLDEFLQ-------------------KTDPKDPANY--ILHAV 494
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTEGKAQ--KMFKKILIPDEIDIPDFVAddpracskcqlecrvcyddKDFSPTCGKFklSLCSA 172
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568995352 495 LVHSGDN-HGGHYVVYL-----------NPKGDGKWCKFDD 523
Cdd:cd02670 173 VCHRGTSlETGHYVAFVrygsysltetdNEAYNAQWVFFDD 213
|
|
| |
