|
Name |
Accession |
Description |
Interval |
E-value |
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
56-1101 |
0e+00 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 657.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 56 AEEDMEDdtswRSEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMvmprFYPDRPHQKSVGFFL----QCNAESDSTSW 131
Cdd:COG5077 29 FDPDVEE----LLEMSFTWKVKRWSELAKKVESPPFSVGGHTWKII----LFPQGNNQCNVSVYLeyepQELEETGGKYY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 132 SCHAQAVLKIINYRDDDKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKG---FIDDDKVTFEVFVQA-DAPHGVAW- 206
Cdd:COG5077 101 DCCAQFAFDISNPKYPTIEYINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGrppFLEEGTLVITVYVRVlKDPTGVLWh 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 207 -----DSKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKLT 281
Cdd:COG5077 181 sflnyNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 282 KSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKGKKNI 361
Cdd:COG5077 261 RSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 362 FESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKT 441
Cdd:COG5077 341 QESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 442 DPK---DPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGG----HD---DDLSVRHC 511
Cdd:COG5077 421 ADKsenSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpyKDkirDHSGIKRF 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 512 TNAYMLVYIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQKRKERQEAHLYMQVQIVAEDQFCGHQGNDMYD----E 587
Cdd:COG5077 501 MSAYMLVYLRKSMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDYPDfsseL 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 588 EKVRYTVFKVLKNSSLAEFVQSLSQTMGFPQD-QIRLWPMQARSNGTKRPAMLDNEAdgNKTMIELSDNEN--------P 658
Cdd:COG5077 581 NDSGLAQFVIKRGAKISDLRNNIAEHLNTPQSlYLREWTMIKRHNKTVRVDRPCNRV--NITTRELVGMNTrtgeelrsY 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 659 WTIFLETVdpELAAS-GATLpkfDKDHDVMLFLKMYDPKTRSLNYCGHIYTPISCKIRDLLPVMCDRagFIQDTSLILYE 737
Cdd:COG5077 659 LERIIEHN--QLDSQrKVAL---TKDGVINIFVKYFDYTTQPISGFGGLHVNKFLKISSISPWIEDS--ISSNLPLTLYE 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 738 EVKPNLTERIQDyDVSLDKAldELMDGDIIVFQK-DDPENDNSE-LPTAKEYFRDLYHRVDVIFCDKTIPNDPG-FVVTL 814
Cdd:COG5077 732 EIKPGMVDTIGD-NITFIGS--EIGTGDIICFEVpGAVEFDTSSaYDSALKLYDFLQGRVLVAFRRFSDEYRENvFEFLL 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 815 SNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRHNYEGTLRD-LLQFFKPRQPKKLYYQQLKMKITDFENRR 893
Cdd:COG5077 809 FIGDFYDDLCRNVSCKLHVTPFYLRGTKSTELEDRIRRVVGSKSIFLLKEaLSSSSEFRQAPVDFYEVLDVPLSELERKR 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 894 SFKCIWL-NSQFREEEITLYPDKHGCVRDLLEECKKAVELGDKASGRLRLLEIVSYKIIGVHQEDELLECLSPATsrTFR 972
Cdd:COG5077 889 LIRLCFLsNGYQHVYLAEFYVEKDYTAVDHLHIVVTKVGCTDELKKSVLVYEVVNLRPVRGHSLKTLIIDDNVRS--TLY 966
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 973 IEEIPLDQVDIdKENEMLITVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEKEFEKFKFAIV-------M 1045
Cdd:COG5077 967 GEVFPLEQEQL-TTNEMCVVVQHFFKDLIRTHGIPFMFVIVPFETFLDTKVRLVARFGYKYKLFSKIKLFVGksytdgeL 1045
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*.
gi 154146209 1046 MGRHQYINEDEYEVNLkdFEPQPGNMshprpwlgLDHfnkAPKRSRYTYLEKAIKI 1101
Cdd:COG5077 1046 DWPMSYFNDEDILYDL--IERLDYIL--------LDH---PDRLRSHSSYDRAIIM 1088
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-524 |
6.74e-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: 479.45 E-value: 6.74e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 213 GYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMM-PTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKL---TKSFGWET 288
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIpPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELtdkTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 289 LDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKGKKNIFESFVDY 368
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 369 VAVEQLDGDNKYDAGEHGLQ-EAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKT------ 441
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKvDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGlakkeg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 442 ----DPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDD-------DLSVRH 510
Cdd:cd02659 241 dsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGEETqktydsgPRAFKR 320
|
330
....*....|....
gi 154146209 511 CTNAYMLVYIRESK 524
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 ... |
621-866 |
7.15e-107 |
|
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: 7.15e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 621 IRLWPMQARSNGTKRPAMLDNEADGNKTMIELSDN----ENPWTIFLETVDPelaasgatLPKFDKDHDVMLFLKMYDPK 696
Cdd:pfam12436 1 IRLWPMVNRQNKTVRPDQPLPEADPAKTVEEIRDKmatrDNPLRLFLEVAEE--------LPPFDKNDDILLFLKYYDPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 697 TRSLNYCGHIYTPISCKIRDLLPVMCDRAGFIQDTSLILYEEVKPNLTErIQDYDVSLDKAldELMDGDIIVFQKDDPEN 776
Cdd:pfam12436 73 KQTLRGVGHVYVPKSSKVSDLVPIINERMGWPPDTPLLLYEEIKPNMIE-IMKPKQTLKKS--ELQDGDIICFQRELSEK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 777 DNSELPTAKEYFRDLYHRVDVIFCDKTIPNDPGFVVTLSNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRH 856
Cdd:pfam12436 150 EQDEYPTAKDYYDFLLNRVEVTFRPKDNPNDPGFTLELSKKMTYDQLAEKVAERLGVDPTKLRFTTVNNYSGQPKTPIKR 229
|
250
....*....|
gi 154146209 857 NYEGTLRDLL 866
Cdd:pfam12436 230 NPNQTLKDIL 239
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
215-519 |
4.21e-87 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 283.56 E-value: 4.21e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 215 VGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDS----SKSVPLALQRVFYELQH--SDKPVGTKKLTKSFGW-- 286
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSrynkDINLLCALRDLFKALQKnsKSSSVSPKMFKKSLGKln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 287 ETLDSFMQHDVQELCRVLLDNVENKMKG---TCVEGTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKGKKN--- 360
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 361 ---IFESFVDYVAVEQLDGDNKYD-AGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpqTDQNIKINDRFEFPEQLPLDE 436
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYcDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 437 FLQKTDPKDPAN---YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHnygghdddlsvrhcTN 513
Cdd:pfam00443 239 YLAEELKPKTNNlqdYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS--------------SS 304
|
....*.
gi 154146209 514 AYMLVY 519
Cdd:pfam00443 305 AYILFY 310
|
|
| MATH_HAUSP |
cd03772 |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ... |
68-203 |
1.15e-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: 267.40 E-value: 1.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 68 SEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRFYPDR-PHQKSVGFFLQCNAESDSTSWSCHAQAVLKIINYRD 146
Cdd:cd03772 1 SEATFSFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRNYPDRnPHQKSVGFFLQCNAESDSTSWSCHAQAVLRIINYKD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 154146209 147 DDKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKGFIDDDKVTFEVFVQADAPHG 203
Cdd:cd03772 81 DEPSFSRRISHLFFSKENDWGFSNFMTWSEVTDPEKGFIEDDTITLEVYVQADAPHG 137
|
|
| USP7_C2 |
pfam14533 |
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ... |
876-1087 |
1.89e-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: 222.36 E-value: 1.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 876 KLYYQQLKMKITDFENRRSFKCIWLNSQF-REEEITLYPDKHGCVRDLLEECKKAVELGDKASGRLRLLEIVSYKIIGVH 954
Cdd:pfam14533 1 ALYYEVLDISLSELENKKSIKVTWLSPGLkKEEELELLVPKNGTVADLLEELQKKVKLSEEGSGKIRLYEVSNHKIYKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 955 QEDELLECLSPATsrTFRIEEIPLDQVDIDkENEMLITVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEK 1034
Cdd:pfam14533 81 SEDEPIDSLNDYL--TLYAEEIPEEELNLD-EGERLIPVFHFQKEPSRTHGIPFLFVLKPGEPFSDTKKRLQKRLGLPDK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 154146209 1035 EFEKFKFAIVMMGRH-QYINEDEyevNLKDFEPQPGNMshprPWLGLDHFNKAP 1087
Cdd:pfam14533 158 EFEKIKFALVQRGKKpEYLEDDD---VLFDLLGQPDDL----PWLGLDHPDKTP 204
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
216-520 |
4.36e-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: 209.26 E-value: 4.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLFFtnqlrkavymmptegddssksvplalqrvfyelqhsdkpvgtkkltksfgwetldsfMQH 295
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS---------------------------------------------------------EQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 296 DVQELCRVLLDNVENKMKGTCVEG--------TIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSI----KGKKNIFE 363
Cdd:cd02257 24 DAHEFLLFLLDKLHEELKKSSKRTsdssslksLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVSLED 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 364 SFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQtDQNIKINDRFEFPEQLPLDEFLQKTDP 443
Cdd:cd02257 104 CLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELDLSPYLSEGEK 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 444 KDPAN-----YILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHdddlsvrhctNAYML 517
Cdd:cd02257 183 DSDSDngsykYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSS----------SAYIL 252
|
...
gi 154146209 518 VYI 520
Cdd:cd02257 253 FYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-519 |
2.07e-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: 201.50 E-value: 2.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLA-----------LQRVFYELQHSDK----PVGtkkL 280
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDkphepqtiidqLQLIFAQLQFGNRsvvdPSG---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 281 TKSFGwetLDSFMQHDVQELCRVLLDNVENKM---KGTCVEGTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKG 357
Cdd:cd02668 78 VKALG---LDTGQQQDAQEFSKLFLSLLEAKLsksKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 358 KKNIFESFVDYVAVEQLDGDNKYDAGEHG-LQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDE 436
Cdd:cd02668 155 HKTLEECIDEFLKEEQLTGDNQYFCESCNsKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 437 FLQKTDPKDpANYILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRCTK---EEAIEHNYGGHD--DDLSVRH 510
Cdd:cd02668 235 YLAESDEGS-YVYELSGVLIHQGVSaYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGkplKLGNSEDPAKPRksEIKKGTH 313
|
330
....*....|
gi 154146209 511 CT-NAYMLVY 519
Cdd:cd02668 314 SSrTAYMLVY 323
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-519 |
5.36e-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: 5.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLFFTNQLRkavymmptegddssksvplALQRVFYELQHSDKPVGT-------KKLTKSFgwET 288
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT-------------------CLKDLFESISEQKKRTGVispkkfiTRLKREN--EL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 289 LDSFMQHDVQELCRVLLDNV------ENKMKGTCVEGT-----------IPKLFRGKMVSYIQCKDVDYRSDRREDYYDI 351
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIaeildaERKAEKANRKLNnnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 352 QLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPE 430
Cdd:cd02663 140 SIDVEQNTSITSCLRQFSATETLCGRNKFYCDEcCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 431 QLPLdeFLQKTDPKDPAN-YILHAVLVH--SGDNHgGHYVVYLnpKGDGKWCKFDDDVVSRcTKEEAIEHNYGGHdddls 507
Cdd:cd02663 220 ELRL--FNTTDDAENPDRlYELVAVVVHigGGPNH-GHYVSIV--KSHGGWLLFDDETVEK-IDENAVEEFFGDS----- 288
|
330
....*....|..
gi 154146209 508 vRHCTNAYMLVY 519
Cdd:cd02663 289 -PNQATAYVLFY 299
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-520 |
9.73e-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: 138.18 E-value: 9.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLFFTNQLrkAVYMmPTEGDDSSKSVPL-----ALQR-VFYELQHSDKPVGTKKLT---KSFgW 286
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPL--ANYL-LSREHSKDCCNEGfcmmcALEAhVERALASSGPGSAPRIFSsnlKQI-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 287 ETLDSFMQHDVQELCRVLLDnvenKMKGTCVEG---------------TIPKLFRGKMVSYIQCKDVDYRSDRREDYYDI 351
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLLD----AMQKACLDRfkklkavdpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 352 QLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFmydpQTDQNIKINDRFEFPE 430
Cdd:cd02661 155 SLDIKGADSLEDALEQFTKPEQLDGENKYKCERcKKKVKASKQLTIHRAPNVLTIHLKRF----SNFRGGKINKQISFPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 431 QLPLDEFL-QKTDPkdPANYILHAVLVHSG-DNHGGHYVVYLnpKG-DGKWCKFDDDVVSRCTKEEAiehnygghdddLS 507
Cdd:cd02661 231 TLDLSPYMsQPNDG--PLKYKLYAVLVHSGfSPHSGHYYCYV--KSsNGKWYNMDDSKVSPVSIETV-----------LS 295
|
330
....*....|...
gi 154146209 508 vrhcTNAYMLVYI 520
Cdd:cd02661 296 ----QKAYILFYI 304
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-519 |
1.43e-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: 131.68 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLFFTNQLRKAV-YMMPTEGDDSSKSVPL--ALQRVFYELQHSDKPVGTKKLTKSFG-----WE 287
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALkNYNPARRGANQSSDNLtnALRDLFDTMDKKQEPVPPIEFLQLLRmafpqFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 288 TLDS---FMQHDVQELCRVLLDNVENKMKGTCVEG-TIPKLFRGKMVSYIQCKDVDYRSD-RREDYYDIQLSIKGKknif 362
Cdd:cd02657 81 EKQNqggYAQQDAEECWSQLLSVLSQKLPGAGSKGsFIDQLFGIELETKMKCTESPDEEEvSTESEYKLQCHISIT---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 363 eSFVDYVaVEQLdgdnkydagEHGLQEAE--------------KGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEF 428
Cdd:cd02657 157 -TEVNYL-QDGL---------KKGLEEEIekhsptlgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 429 PEQLPLDEFLQKTdpkdpANYILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRcTKEEAIEHNYGGHDDDLs 507
Cdd:cd02657 226 PFELDLYELCTPS-----GYYELVAVITHQGRSaDSGHYVAWVRRKNDGKWIKFDDDKVSE-VTEEDILKLSGGGDWHI- 298
|
330
....*....|..
gi 154146209 508 vrhctnAYMLVY 519
Cdd:cd02657 299 ------AYILLY 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-520 |
6.01e-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: 124.71 E-value: 6.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLfftnqlrkavymmptegddssksvplalqrvfyelqhsdkpvgtkkltksfgwetldSFMQH 295
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL---------------------------------------------------------SADQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 296 DVQELCRVLLDNVENKmkgtcvegtIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKGKK------NIFESFVDYV 369
Cdd:cd02674 24 DAQEFLLFLLDGLHSI---------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFT 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 370 AVEQLDGDNK-YDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFP-EQLPLDEFLQKTDPKDPA 447
Cdd:cd02674 95 KEETLDGDNAwKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTR--KLTTPVTFPlNDLDLTPYVDTRSFTGPF 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154146209 448 NYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEhnygghdddlsvrhcTNAYMLVYI 520
Cdd:cd02674 173 KYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVS---------------SSAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-519 |
2.46e-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: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTkkltksfgweTLDSFM-- 293
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEA----------PPDYFLea 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 294 ----------QHDVQELCRVLLDNVENkmkgtcvegTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKgkknIFE 363
Cdd:cd02664 71 srppwftpgsQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP----SVQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 364 SFVDY-VAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPE--QLPLDEFLQ 439
Cdd:cd02664 138 DLLNYfLSPEKLTGDNQYYCEKcASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEvlSLPVRVESK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 440 KTDPKD----------------PANYILHAVLVHSG-DNHGGHYVVYL-NPKG-------------------DGKWCKFD 482
Cdd:cd02664 218 SSESPLekkeeesgddgelvtrQVHYRLYAVVVHSGySSESGHYFTYArDQTDadstgqecpepkdaeendeSKNWYLFN 297
|
330 340 350
....*....|....*....|....*....|....*..
gi 154146209 483 DDVVSRCTKEEAiehnygghDDDLSVRHCTNAYMLVY 519
Cdd:cd02664 298 DSRVTFSSFESV--------QNVTSRFPKDTPYILFY 326
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-531 |
9.54e-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: 9.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEgddssksvplalqrVFYELQHSDKpvgtkkltksfgweTLDSFMQH 295
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAP--------------QFKGYQQQ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 296 DVQELCRVLLDNVENkmkgtcvegTIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQL----SIKGKKNIFESFVDYVAV 371
Cdd:cd02667 53 DSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 372 EQLDGDNKYdaGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQnIKINDRFEFPEQLPLDEFLqktDPKDPAN--- 448
Cdd:cd02667 124 EILEGNNKF--ACENCTKAKKQYLISKLPPVLVIHLKRFQQPRSANL-RKVSRHVSFPEILDLAPFC---DPKCNSSedk 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 449 ----YILHAVLVHSGDNHGGHYV--VYLNPKGDgkwckFDDDVVSRCTKEEAIEHNYGghdddlSVRHCTNAymlvYIRE 522
Cdd:cd02667 198 ssvlYRLYGVVEHSGTMRSGHYVayVKVRPPQQ-----RLSDLTKSKPAADEAGPGSG------QWYYISDS----DVRE 262
|
....*....
gi 154146209 523 SKLSEVLQA 531
Cdd:cd02667 263 VSLEEVLKS 271
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-520 |
8.48e-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: 8.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLFFTNQLRKavYMM------PTEGDDSSKSVPLALQRVFYELQHSDKPVG---TKKLTKSfgW 286
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRN--YFLsdrhscTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPygpINLLYLS--W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 287 ---ETLDSFMQHDVQELCRVLLD-----------NVENKMKGTCVegtIPKLFRGKMVSYIQCKDVDYRSDRREDYYDIQ 352
Cdd:cd02660 78 khsRNLAGYSQQDAHEFFQFLLDqlhthyggdknEANDESHCNCI---IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 353 LSIKGKKNIF----ESFVD-----------YVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpQTD 417
Cdd:cd02660 155 LDIPNKSTPSwalgESGVSgtptlsdcldrFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 418 QNIKINDRFEFPEQLPLDEFL-------QKTDPKDPAN-YILHAVLVHSGDNHGGHYVVYLNpKGDGKWCKFDDDVVSRC 489
Cdd:cd02660 234 TSRKIDTYVQFPLELNMTPYTsssigdtQDSNSLDPDYtYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRV 312
|
330 340 350
....*....|....*....|....*....|.
gi 154146209 490 TKEEaiehnygghdddlsVRHCtNAYMLVYI 520
Cdd:cd02660 313 SEEE--------------VLKS-QAYLLFYH 328
|
|
| MATH |
cd00121 |
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ... |
71-197 |
4.11e-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: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 71 TFQFTVERFSRL-SESVLSPPCFVRNLPWKIMVMPRFypDRPHQKSVGFFLQC-NAESDSTSWSCHAQAVLKIINyRDDD 148
Cdd:cd00121 2 KHTWKIVNFSELeGESIYSPPFEVGGYKWRIRIYPNG--DGESGDYLSLYLELdKGESDLEKWSVRAEFTLKLVN-QNGG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 154146209 149 KSFSRRISHLFF-HKENDWGFSNFMAWSEVTDPekGFIDDDKVTFEVFVQ 197
Cdd:cd00121 79 KSLSKSFTHVFFsEKGSGWGFPKFISWDDLEDS--YYLVDDSLTIEVEVK 126
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
209-519 |
8.24e-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: 8.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 209 KKHTG---YVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGddSSKSvplALQRVF------YELQHSDKPVGTKK 279
Cdd:cd02671 16 EKRENllpFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI--SSVE---QLQSSFllnpekYNDELANQAPRRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 280 LTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKgtcvegtipKLFRGKMVSYIQCKDVDYRSDRREDYYDIQLSIKGK- 358
Cdd:cd02671 91 NALREVNPMYEGYLQHDAQEVLQCILGNIQELVE---------KDFQGQLVLRTRCLECETFTERREDFQDISVPVQESe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 359 ------------------KNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQN 419
Cdd:cd02671 162 lskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 420 I----KINDRFEFPEQLPLDEFlqKTDPKDPAnYILHAVLVHSGDN-HGGHYVVYLnpkgdgKWCKFDDDVVSRCTKEEA 494
Cdd:cd02671 242 YgglsKVNTPLLTPLKLSLEEW--STKPKNDV-YRLFAVVMHSGATiSSGHYTAYV------RWLLFDDSEVKVTEEKDF 312
|
330 340
....*....|....*....|....*..
gi 154146209 495 IEhnygghddDLS--VRHCTNAYMLVY 519
Cdd:cd02671 313 LE--------ALSpnTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
216-521 |
2.97e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 92.17 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLFFTN--------QLRKAVYMMPTEGDDSSKsvPLALQRVFYELqhsdKPVGTKKLTKsFGWE 287
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLpkldelldDLSKELKVLKNVIRKPEP--DLNQEEALKLF----TALWSSKEHK-VGWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 288 TlDSFMQHDVQELCRVLLDNVENKMKGTcveGTIPKLFRGKmvsyiqckdvDYRSDRREDYYDI------QLSIKGKKNi 361
Cdd:COG5533 74 P-PMGSQEDAHELLGKLLDELKLDLVNS---FTIRIFKTTK----------DKKKTSTGDWFDIiielpdQTWVNNLKT- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 362 FESFVDyvAVEQLDGD-----NKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpqtDQNIKINDRFEFPEQLPLde 436
Cdd:COG5533 139 LQEFID--NMEELVDDetgvkAKENEELEVQAKQEYEVSFVKLPKILTIQLKRFANL---GGNQKIDTEVDEKFELPV-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 437 flqKTDPKDPAN----YILHAVLVHSGDNHGGHYVVYLnpKGDGKWCKFDDDVVSRCTKEEAIEHNygghdddlsvrhCT 512
Cdd:COG5533 212 ---KHDQILNIVketyYDLVGFVLHQGSLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINEK------------AK 274
|
....*....
gi 154146209 513 NAYMLVYIR 521
Cdd:COG5533 275 NAYLYFYER 283
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-519 |
4.34e-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: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLF--------------------------FTNQLRKAVYMMPTEgdDSSKSVPLALQRVFYelQ 269
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwryddlenkfpsdvvdpandLNCQLIKLADGLLSG--RYSKPASLKSENDPY--Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 270 HSDKPVGTKKLTkSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTcvEGTIP-KLFRGKMVSYIQCKDVDYRSDRREDY 348
Cdd:cd02658 77 VGIKPSMFKALI-GKGHPEFSTMRQQDALEFLLHLIDKLDRESFKN--LGLNPnDLFKFMIEDRLECLSCKKVKYTSELS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 349 YDIQLSI---------KGKK-----NIFESFVDYVAVEQLDgDNKYDAGEHGlqEAEKGVKFLTLPPVLHLQLMRFMYDP 414
Cdd:cd02658 154 EILSLPVpkdeatekeEGELvyepvPLEDCLKAYFAPETIE-DFCSTCKEKT--TATKTTGFKTFPDYLVINMKRFQLLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 415 QTDQnIKINDRFEFPEQLpldeflqktdpkDPANYILHAVLVHSGDN-HGGHYVVYL--NPKGDGKWCKFDDDVVSRCTK 491
Cdd:cd02658 231 NWVP-KKLDVPIDVPEEL------------GPGKYELIAFISHKGTSvHSGHYVAHIkkEIDGEGKWVLFNDEKVVASQD 297
|
330 340
....*....|....*....|....*...
gi 154146209 492 EEAIEhnygghdddlsvrhcTNAYMLVY 519
Cdd:cd02658 298 PPEMK---------------KLGYIYFY 310
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-520 |
2.85e-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: 76.44 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLFFTNQlrkavymmptegdDSSKSvplalqrvfyelqhsdkpvgtkkLTKSFGWETlDSFmqh 295
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLFSQQQ-------------DVSEF-----------------------THLLLDWLE-DAF--- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 296 DVQELCRVLLDNVENKMKgtcvegtipKLFRGK--MVSYIQCKdvdyRSDRREDYYDIQLSIKGKKNIFEsfvdyvAVE- 372
Cdd:cd02665 41 QAAAEAISPGEKSKNPMV---------QLFYGTflTEGVLEGK----PFCNCETFGQYPLQVNGYGNLHE------CLEa 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 373 -QLDGDNKYDAGEHGLQEAEKGVkFLTLPPVLHLQLMRFMYDpqTDQNIKINDRFEFPEQLpldeflqktdpkDPANYIL 451
Cdd:cd02665 102 aMFEGEVELLPSDHSVKSGQERW-FTELPPVLTFELSRFEFN--QGRPEKIHDKLEFPQII------------QQVPYEL 166
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154146209 452 HAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDdlsvrhcTNAYMLVYI 520
Cdd:cd02665 167 HAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRN-------PSAYCLMYI 228
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
216-519 |
5.25e-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: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 216 GLKNQGATCYMNSLLQTLfftnqlrkavymmptegdDSSKSVPlalqrvfyelqhsdkpvgtkkltksfgwETLDSFM-Q 294
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL------------------ASLPSLI----------------------------EYLEEFLeQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 295 HDVQELCRVLLDNVENKMKGtcvegtipkLFRGKMVSYIQCKDVDYRSDRRED-YYDIQLSIKGKKNIFESFVDyvavEQ 373
Cdd:cd02662 35 QDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSKVRYEsFTMLSLPVPNQSSGSGTTLE----HC 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 374 LDGDNKydagehglQEAEKGVK-------FLTLPPVLHLQLMRFMYDPQtDQNIKINDRFEFPEQLPldeflqktDPKdp 446
Cdd:cd02662 102 LDDFLS--------TEIIDDYKcdrcqtvIVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP--------KVL-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 447 anYILHAVLVHSGDNHGGHYVVY----LNPKG----------------DGKWCKFDDDVVSRCTKEEAIEHNYgghdddl 506
Cdd:cd02662 163 --YRLRAVVVHYGSHSSGHYVCYrrkpLFSKDkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQKS------- 233
|
330
....*....|...
gi 154146209 507 svrhctnAYMLVY 519
Cdd:cd02662 234 -------AYMLFY 239
|
|
| MATH |
smart00061 |
meprin and TRAF homology; |
75-172 |
5.44e-15 |
|
meprin and TRAF homology;
Pssm-ID: 214496 [Multi-domain] Cd Length: 95 Bit Score: 71.56 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 75 TVERFSRLS--ESVLSPPCFVRNLPWKIMVMPRfypdrphQKSVGFFLQCNAE-SDSTSWSCHAQAVLKIINYrdDDKSF 151
Cdd:smart00061 5 TFKNVSRLEegESYFSPSEEHFNIPWRLKIYRK-------NGFLSLYLHCEKEeCDSRKWSIEAEFTLKLVSQ--NGKSL 75
|
90 100
....*....|....*....|.
gi 154146209 152 SRRISHLfFHKENDWGFSNFM 172
Cdd:smart00061 76 SKKDKHV-FEKPSGWGFSKFI 95
|
|
| MATH |
pfam00917 |
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ... |
79-196 |
2.69e-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: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 79 FSRL--SESVLSPPCFVRNLPWKIMVmprfypdRPHQKSVGFFLQCNA-ESDSTSWSCHAQAVLKIINyrDDDKSFSRRI 155
Cdd:pfam00917 4 FSKIkeGESYYSPVEERFNIPWRLQI-------YRKGGFLGLYLHCDKeEELERGWSIETEFTLKLVS--SNGKSVTKTD 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 154146209 156 SHLFfHKENDWGFSNFMAWSEVtdpEKGFIDDDKVTFEVFV 196
Cdd:pfam00917 75 THVF-EKPKGWGWGKFISWDDL---EKDYLVDDSITVEAHV 111
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-520 |
3.65e-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: 69.06 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 215 VGLKNQGATCYMNSLLQTLFFTNQLRKAV------YMMPTEGDDSSKSVP----------------LALQRVFYELQHSD 272
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVlnfdesKAELASDYPTERRIGgrevsrselqrsnqfvYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 273 KPVGT--KKLTksfgwetLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYI--QCKDVDYRSDRREDY 348
Cdd:cd02666 82 TRSVTpsKELA-------YLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKEQSDLikRLFSGKTKQQLVPES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 349 YDIQLSIKGKKNIFESF-VDYV-----AVEQLDGDNKYDAGEHGLQEAEKGvkflTLPPVLHLQL------------MRF 410
Cdd:cd02666 155 MGNQPSVRTKTERFLSLlVDVGkkgreIVVLLEPKDLYDALDRYFDYDSLT----KLPQRSQVQAqlaqplqrelisMDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 411 MYDPQTDQNIKINDRFEFPEQLPLDEFLQKT-------------DPKDPAnYILHAVLVHSGDNHGGHYVVYLNPKGDGK 477
Cdd:cd02666 231 YELPSSIDDIDELIREAIQSESSLVRQAQNElaelkheiekqfdDLKSYG-YRLHAVFIHRGEASSGHYWVYIKDFEENV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 154146209 478 WCKFDDDVVSRCTKEEAIEHNYGGHDddlsvrhctNAYMLVYI 520
Cdd:cd02666 310 WRKYNDETVTVVPASEVFLFTLGNTA---------TPYFLVYV 343
|
|
| MATH_Ubp21p |
cd03775 |
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ... |
72-196 |
8.31e-10 |
|
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: 58.14 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 72 FQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRfypdRPHQ-KSVGFFL----QCNAES-DSTSWSCHAQAVLKIINYR 145
Cdd:cd03775 3 FTWRIKNWSELEKKVHSPKFKCGGFEWRILLFPQ----GNSQtGGVSIYLephpEEEEKApLDEDWSVCAQFALVISNPG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 154146209 146 DDDKSFSRRISHLFFHKENDWGFSNFMAWS--EVTDPEK--GFIDDDKVTFEVFV 196
Cdd:cd03775 79 DPSIQLSNVAHHRFNAEDKDWGFTRFIELRklAHRTPDKpsPFLENGELNITVYV 133
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
372-523 |
9.42e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 62.98 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 372 EQLD-GDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFPeqlpLDEFL--QKTDPKDPAN 448
Cdd:COG5560 688 EQLGlSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD--KIDDLVEYP----IDDLDlsGVEYMVDDPR 761
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154146209 449 --YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEhnygghdddlsvrhcTNAYMLVYIRES 523
Cdd:COG5560 762 liYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT---------------SSAYVLFYRRKS 823
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
208-306 |
5.42e-08 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 57.20 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 208 SKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKavYMMPTEGDDS-SKSVPLA----LQRVFYEL--------QHSDKP 274
Cdd:COG5560 259 INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRD--YFLSDEYEESiNEENPLGmhgsVASAYADLikqlydgnLHAFTP 336
|
90 100 110
....*....|....*....|....*....|..
gi 154146209 275 VGTKKLTKSFgWETLDSFMQHDVQELCRVLLD 306
Cdd:COG5560 337 SGFKKTIGSF-NEEFSGYDQQDSQEFIAFLLD 367
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
215-483 |
2.65e-06 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 50.73 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 215 VGLKNQGATCYMNSLLQTLFFTNQLRKAV----------------------YMMptegDDSSKSVPLA--LQRVF----- 265
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAlshlateclkehcllcelgflfDML----EKAKGKNCQAsnFLRALssipe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 266 ---YEL-QHSDKPVGTKKLTksfgwetldsfmqHDVQELCRVLLDNV---ENKMKGTCVEGT--IPKLFRGKMVSYIQCK 336
Cdd:pfam13423 77 asaLGLlDEDRETNSAISLS-------------SLIQSFNRFLLDQLsseENSTPPNPSPAEspLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 337 DVDYRSDRREDYYDIQL------SIKGKKNIFESFVDYVA--VEQLDGD-------NKYDagehgLQEAEKGVKflTLPP 401
Cdd:pfam13423 144 NCGHESVRESSTHVLDLiyprkpSSNNKKPPNQTFSSILKssLERETTTkawcekcKRYQ-----PLESRRTVR--NLPP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 402 VLHLQLMrfMYDPQTDQNIKINDrfEFPEQLPLDEFLQKTDPKDPANYILHAVLVH-SGDNHGGHYV-------VYLNPK 473
Cdd:pfam13423 217 VLSLNAA--LTNEEWRQLWKTPG--WLPPEIGLTLSDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVsfvkvadSELEDP 292
|
330
....*....|
gi 154146209 474 GDGKWCKFDD 483
Cdd:pfam13423 293 TESQWYLFND 302
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
396-483 |
2.44e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 40.97 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 396 FLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFPEQLPLDEFLQ-------------------KTDPKDPANY--ILHAV 454
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTEGKAQ--KMFKKILIPDEIDIPDFVAddpracskcqlecrvcyddKDFSPTCGKFklSLCSA 172
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 154146209 455 LVHSGDN-HGGHYVVYL-----------NPKGDGKWCKFDD 483
Cdd:cd02670 173 VCHRGTSlETGHYVAFVrygsysltetdNEAYNAQWVFFDD 213
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
378-492 |
9.63e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 39.61 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146209 378 NKYDaGEHGLQEAEKGVKFL--TLPPVLHLQLMRFMY-DPQTDQNIKIndrFEFP-EQLPLDEFLQKTDPKD--PANYIL 451
Cdd:cd02669 310 KKYD-GKTETELKDSLKRYLisRLPKYLIFHIKRFSKnNFFKEKNPTI---VNFPiKNLDLSDYVHFDKPSLnlSTKYNL 385
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 154146209 452 HAVLVHSGDNHG-GHYVVYLNPKGDGKWCKFDDDVVSRCTKE 492
Cdd:cd02669 386 VANIVHEGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQ 427
|
|
| |
