|
Name |
Accession |
Description |
Interval |
E-value |
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
55-1100 |
0e+00 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 655.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 55 AEEDMEDdtswRSEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMvmprFYPDRPHQKSVGFFL----QCNAESDSTSW 130
Cdd:COG5077 29 FDPDVEE----LLEMSFTWKVKRWSELAKKVESPPFSVGGHTWKII----LFPQGNNQCNVSVYLeyepQELEETGGKYY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 131 SCHAQAVLKIINYRDDEKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKG---FIDDDKVTFEVFVQA-DAPHGVAW- 205
Cdd:COG5077 101 DCCAQFAFDISNPKYPTIEYINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGrppFLEEGTLVITVYVRVlKDPTGVLWh 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 206 -----DSKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKLT 280
Cdd:COG5077 181 sflnyNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 281 KSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNI 360
Cdd:COG5077 261 RSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 361 FESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKT 440
Cdd:COG5077 341 QESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 441 DPK---DPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGG----HD---DDLSVRHC 510
Cdd:COG5077 421 ADKsenSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpyKDkirDHSGIKRF 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 511 TNAYMLVYIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQKRKERQEAHLYMQVQIVAEDQFCGHQGNDMYD----E 586
Cdd:COG5077 501 MSAYMLVYLRKSMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDYPDfsseL 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 587 EKVKYTVFKVLKNSSLAEFVQSLSQTMGFPQD-QIRLWPMQARSNGTKRPAMLDNEAdgNKTMIELSDNEN--------P 657
Cdd:COG5077 581 NDSGLAQFVIKRGAKISDLRNNIAEHLNTPQSlYLREWTMIKRHNKTVRVDRPCNRV--NITTRELVGMNTrtgeelrsY 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 658 WTIFLETVdpELAAS-GATLpkfDKDHDVMLFLKMYDPKTRSLNYCGHIYTPISCKIRDLLPVMCDRagFIQDTSLILYE 736
Cdd:COG5077 659 LERIIEHN--QLDSQrKVAL---TKDGVINIFVKYFDYTTQPISGFGGLHVNKFLKISSISPWIEDS--ISSNLPLTLYE 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 737 EVKPNLTERIQDyDVSLDKAldELMDGDIIVFQK-DDPENDNSE-LPTAKEYFRDLYHRVDVIFCDKTIPNDPG-FVVTL 813
Cdd:COG5077 732 EIKPGMVDTIGD-NITFIGS--EIGTGDIICFEVpGAVEFDTSSaYDSALKLYDFLQGRVLVAFRRFSDEYRENvFEFLL 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 814 SNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRHNYEGTLRD-LLQFFKPRQPKKLYYQQLKMKITDFENRR 892
Cdd:COG5077 809 FIGDFYDDLCRNVSCKLHVTPFYLRGTKSTELEDRIRRVVGSKSIFLLKEaLSSSSEFRQAPVDFYEVLDVPLSELERKR 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 893 SFKCIWL-NSQFREEEITLYPDKHGCVRDLLEECKKAVELGEKASGKLRLLEIVSYKIIGVHQEDELLECLSPATsrTFR 971
Cdd:COG5077 889 LIRLCFLsNGYQHVYLAEFYVEKDYTAVDHLHIVVTKVGCTDELKKSVLVYEVVNLRPVRGHSLKTLIIDDNVRS--TLY 966
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 972 IEEIPLDQVDIdKENEMLVTVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEKEFEKFKFAIV-------M 1044
Cdd:COG5077 967 GEVFPLEQEQL-TTNEMCVVVQHFFKDLIRTHGIPFMFVIVPFETFLDTKVRLVARFGYKYKLFSKIKLFVGksytdgeL 1045
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*.
gi 150378533 1045 MGRHQYINEDEYEVNLkdFEPQPGNMshprpwlgLDHfnkAPKRSRYTYLEKAIKI 1100
Cdd:COG5077 1046 DWPMSYFNDEDILYDL--IERLDYIL--------LDH---PDRLRSHSSYDRAIIM 1088
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
212-523 |
6.23e-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: 6.23e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 212 GYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMM-PTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKL---TKSFGWET 287
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIpPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELtdkTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 288 LDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDY 367
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 368 VAVEQLDGDNKYDAGEHGLQ-EAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKT------ 440
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKvDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGlakkeg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 441 ----DPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDD-------DLSVRH 509
Cdd:cd02659 241 dsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGEETqktydsgPRAFKR 320
|
330
....*....|....
gi 150378533 510 CTNAYMLVYIRESK 523
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 ... |
620-865 |
6.47e-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: 334.09 E-value: 6.47e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 620 IRLWPMQARSNGTKRPAMLDNEADGNKTMIELSDN----ENPWTIFLETVDPelaasgatLPKFDKDHDVMLFLKMYDPK 695
Cdd:pfam12436 1 IRLWPMVNRQNKTVRPDQPLPEADPAKTVEEIRDKmatrDNPLRLFLEVAEE--------LPPFDKNDDILLFLKYYDPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 696 TRSLNYCGHIYTPISCKIRDLLPVMCDRAGFIQDTSLILYEEVKPNLTErIQDYDVSLDKAldELMDGDIIVFQKDDPEN 775
Cdd:pfam12436 73 KQTLRGVGHVYVPKSSKVSDLVPIINERMGWPPDTPLLLYEEIKPNMIE-IMKPKQTLKKS--ELQDGDIICFQRELSEK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 776 DNSELPTAKEYFRDLYHRVDVIFCDKTIPNDPGFVVTLSNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRH 855
Cdd:pfam12436 150 EQDEYPTAKDYYDFLLNRVEVTFRPKDNPNDPGFTLELSKKMTYDQLAEKVAERLGVDPTKLRFTTVNNYSGQPKTPIKR 229
|
250
....*....|
gi 150378533 856 NYEGTLRDLL 865
Cdd:pfam12436 230 NPNQTLKDIL 239
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
214-518 |
2.23e-87 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 284.33 E-value: 2.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 214 VGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDS----SKSVPLALQRVFYELQH--SDKPVGTKKLTKSFGW-- 285
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSrynkDINLLCALRDLFKALQKnsKSSSVSPKMFKKSLGKln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 286 ETLDSFMQHDVQELCRVLLDNVENKMKG---TCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKN--- 359
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 360 ---IFESFVDYVAVEQLDGDNKYD-AGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpqTDQNIKINDRFEFPEQLPLDE 435
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYcDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 436 FLQKTDPKDPAN---YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHnygghdddlsvrhcTN 512
Cdd:pfam00443 239 YLAEELKPKTNNlqdYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS--------------SS 304
|
....*.
gi 150378533 513 AYMLVY 518
Cdd:pfam00443 305 AYILFY 310
|
|
| MATH_HAUSP |
cd03772 |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ... |
67-202 |
2.57e-84 |
|
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: 268.94 E-value: 2.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 67 SEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRFYPDR-PHQKSVGFFLQCNAESDSTSWSCHAQAVLKIINYRD 145
Cdd:cd03772 1 SEATFSFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRNYPDRnPHQKSVGFFLQCNAESDSTSWSCHAQAVLRIINYKD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 150378533 146 DEKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKGFIDDDKVTFEVFVQADAPHG 202
Cdd:cd03772 81 DEPSFSRRISHLFFSKENDWGFSNFMTWSEVTDPEKGFIEDDTITLEVYVQADAPHG 137
|
|
| USP7_C2 |
pfam14533 |
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ... |
875-1086 |
1.18e-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: 222.74 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 875 KLYYQQLKMKITDFENRRSFKCIWLNSQF-REEEITLYPDKHGCVRDLLEECKKAVELGEKASGKLRLLEIVSYKIIGVH 953
Cdd:pfam14533 1 ALYYEVLDISLSELENKKSIKVTWLSPGLkKEEELELLVPKNGTVADLLEELQKKVKLSEEGSGKIRLYEVSNHKIYKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 954 QEDELLECLSPATsrTFRIEEIPLDQVDIDkENEMLVTVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEK 1033
Cdd:pfam14533 81 SEDEPIDSLNDYL--TLYAEEIPEEELNLD-EGERLIPVFHFQKEPSRTHGIPFLFVLKPGEPFSDTKKRLQKRLGLPDK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 150378533 1034 EFEKFKFAIVMMGRH-QYINEDEyevNLKDFEPQPGNMshprPWLGLDHFNKAP 1086
Cdd:pfam14533 158 EFEKIKFALVQRGKKpEYLEDDD---VLFDLLGQPDDL----PWLGLDHPDKTP 204
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
215-519 |
2.37e-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: 210.03 E-value: 2.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLFFtnqlrkavymmptegddssksvplalqrvfyelqhsdkpvgtkkltksfgwetldsfMQH 294
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS---------------------------------------------------------EQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 295 DVQELCRVLLDNVENKMKGTCVEG--------TIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSI----KGKKNIFE 362
Cdd:cd02257 24 DAHEFLLFLLDKLHEELKKSSKRTsdssslksLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVSLED 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 363 SFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQtDQNIKINDRFEFPEQLPLDEFLQKTDP 442
Cdd:cd02257 104 CLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELDLSPYLSEGEK 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 443 KDPAN-----YILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHdddlsvrhctNAYML 516
Cdd:cd02257 183 DSDSDngsykYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSS----------SAYIL 252
|
...
gi 150378533 517 VYI 519
Cdd:cd02257 253 FYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-518 |
4.45e-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: 200.34 E-value: 4.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLA-----------LQRVFYELQHSDK----PVGtkkL 279
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDkphepqtiidqLQLIFAQLQFGNRsvvdPSG---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 280 TKSFGwetLDSFMQHDVQELCRVLLDNVENKM---KGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKG 356
Cdd:cd02668 78 VKALG---LDTGQQQDAQEFSKLFLSLLEAKLsksKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 357 KKNIFESFVDYVAVEQLDGDNKYDAGEHG-LQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDE 435
Cdd:cd02668 155 HKTLEECIDEFLKEEQLTGDNQYFCESCNsKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 436 FLQKTDPKDpANYILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRCTK---EEAIEHNYGGHD--DDLSVRH 509
Cdd:cd02668 235 YLAESDEGS-YVYELSGVLIHQGVSaYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGkplKLGNSEDPAKPRksEIKKGTH 313
|
330
....*....|
gi 150378533 510 CT-NAYMLVY 518
Cdd:cd02668 314 SSrTAYMLVY 323
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-518 |
6.86e-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: 141.29 E-value: 6.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLFFTNQLRkavymmptegddssksvplALQRVFYELQHSDKPVGT-------KKLTKSFgwET 287
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT-------------------CLKDLFESISEQKKRTGVispkkfiTRLKREN--EL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 288 LDSFMQHDVQELCRVLLDNV------ENKMKGTCVEGT-----------IPKLFRGKMVSYIQCKEVDYRSDRREDYYDI 350
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIaeildaERKAEKANRKLNnnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 351 QLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPE 429
Cdd:cd02663 140 SIDVEQNTSITSCLRQFSATETLCGRNKFYCDEcCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 430 QLPLdeFLQKTDPKDPAN-YILHAVLVH--SGDNHgGHYVVYLnpKGDGKWCKFDDDVVSRcTKEEAIEHNYGGHdddls 506
Cdd:cd02663 220 ELRL--FNTTDDAENPDRlYELVAVVVHigGGPNH-GHYVSIV--KSHGGWLLFDDETVEK-IDENAVEEFFGDS----- 288
|
330
....*....|..
gi 150378533 507 vRHCTNAYMLVY 518
Cdd:cd02663 289 -PNQATAYVLFY 299
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-519 |
8.50e-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: 8.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLFFTNQLrkAVYMmPTEGDDSSKSVPL-----ALQR-VFYELQHSDKPVGTKKLT---KSFgW 285
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPL--ANYL-LSREHSKDCCNEGfcmmcALEAhVERALASSGPGSAPRIFSsnlKQI-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 286 ETLDSFMQHDVQELCRVLLDnvenKMKGTCVEG---------------TIPKLFRGKMVSYIQCKEVDYRSDRREDYYDI 350
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLLD----AMQKACLDRfkklkavdpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 351 QLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFmydpQTDQNIKINDRFEFPE 429
Cdd:cd02661 155 SLDIKGADSLEDALEQFTKPEQLDGENKYKCERcKKKVKASKQLTIHRAPNVLTIHLKRF----SNFRGGKINKQISFPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 430 QLPLDEFL-QKTDPkdPANYILHAVLVHSG-DNHGGHYVVYLnpKG-DGKWCKFDDDVVSRCTKEEAiehnygghdddLS 506
Cdd:cd02661 231 TLDLSPYMsQPNDG--PLKYKLYAVLVHSGfSPHSGHYYCYV--KSsNGKWYNMDDSKVSPVSIETV-----------LS 295
|
330
....*....|...
gi 150378533 507 vrhcTNAYMLVYI 519
Cdd:cd02661 296 ----QKAYILFYI 304
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-518 |
6.05e-34 |
|
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: 132.84 E-value: 6.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLFFTNQLRKAV-YMMPTEGDDSSKSVPL--ALQRVFYELQHSDKPVGTKKLTKSFG-----WE 286
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALkNYNPARRGANQSSDNLtnALRDLFDTMDKKQEPVPPIEFLQLLRmafpqFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 287 TLDS---FMQHDVQELCRVLLDNVENKMKGTCVEG-TIPKLFRGKMVSYIQCKEVDYRSD-RREDYYDIQLSIKGKKNif 361
Cdd:cd02657 81 EKQNqggYAQQDAEECWSQLLSVLSQKLPGAGSKGsFIDQLFGIELETKMKCTESPDEEEvSTESEYKLQCHISITTE-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 362 esfVDYVaVEQLdgdnkydagEHGLQEAE--------------KGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEF 427
Cdd:cd02657 159 ---VNYL-QDGL---------KKGLEEEIekhsptlgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 428 PEQLPLDEFLQKTdpkdpANYILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRcTKEEAIEHNYGGHDDDLs 506
Cdd:cd02657 226 PFELDLYELCTPS-----GYYELVAVITHQGRSaDSGHYVAWVRRKNDGKWIKFDDDKVSE-VTEEDILKLSGGGDWHI- 298
|
330
....*....|..
gi 150378533 507 vrhctnAYMLVY 518
Cdd:cd02657 299 ------AYILLY 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-519 |
1.72e-32 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 126.25 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLfftnqlrkavymmptegddssksvplalqrvfyelqhsdkpvgtkkltksfgwetldSFMQH 294
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL---------------------------------------------------------SADQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 295 DVQELCRVLLDNVENKmkgtcvegtIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKK------NIFESFVDYV 368
Cdd:cd02674 24 DAQEFLLFLLDGLHSI---------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFT 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 369 AVEQLDGDNK-YDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFP-EQLPLDEFLQKTDPKDPA 446
Cdd:cd02674 95 KEETLDGDNAwKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTR--KLTTPVTFPlNDLDLTPYVDTRSFTGPF 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150378533 447 NYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEhnygghdddlsvrhcTNAYMLVYI 519
Cdd:cd02674 173 KYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVS---------------SSAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-518 |
1.99e-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: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTkkltksfgweTLDSFM-- 292
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEA----------PPDYFLea 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 293 ----------QHDVQELCRVLLDNVENkmkgtcvegTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKgkknIFE 362
Cdd:cd02664 71 srppwftpgsQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP----SVQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 363 SFVDY-VAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPE--QLPLDEFLQ 438
Cdd:cd02664 138 DLLNYfLSPEKLTGDNQYYCEKcASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEvlSLPVRVESK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 439 KTDPKD----------------PANYILHAVLVHSG-DNHGGHYVVYL-NPKG-------------------DGKWCKFD 481
Cdd:cd02664 218 SSESPLekkeeesgddgelvtrQVHYRLYAVVVHSGySSESGHYFTYArDQTDadstgqecpepkdaeendeSKNWYLFN 297
|
330 340 350
....*....|....*....|....*....|....*..
gi 150378533 482 DDVVSRCTKEEAiehnygghDDDLSVRHCTNAYMLVY 518
Cdd:cd02664 298 DSRVTFSSFESV--------QNVTSRFPKDTPYILFY 326
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-530 |
4.85e-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: 117.87 E-value: 4.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEgddssksvplalqrVFYELQHSDKpvgtkkltksfgweTLDSFMQH 294
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAP--------------QFKGYQQQ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 295 DVQELCRVLLDNVENkmkgtcvegTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQL----SIKGKKNIFESFVDYVAV 370
Cdd:cd02667 53 DSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 371 EQLDGDNKYdaGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQnIKINDRFEFPEQLPLDEFLqktDPKDPAN--- 447
Cdd:cd02667 124 EILEGNNKF--ACENCTKAKKQYLISKLPPVLVIHLKRFQQPRSANL-RKVSRHVSFPEILDLAPFC---DPKCNSSedk 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 448 ----YILHAVLVHSGDNHGGHYV--VYLNPKGDgkwckFDDDVVSRCTKEEAIEHNYGghdddlSVRHCTNAymlvYIRE 521
Cdd:cd02667 198 ssvlYRLYGVVEHSGTMRSGHYVayVKVRPPQQ-----RLSDLTKSKPAADEAGPGSG------QWYYISDS----DVRE 262
|
....*....
gi 150378533 522 SKLSEVLQA 530
Cdd:cd02667 263 VSLEEVLKS 271
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-519 |
6.27e-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: 115.93 E-value: 6.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLFFTNQLRKavYMM------PTEGDDSSKSVPLALQRVFYELQHSDKPVG---TKKLTKSfgW 285
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRN--YFLsdrhscTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPygpINLLYLS--W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 286 ---ETLDSFMQHDVQELCRVLLD-----------NVENKMKGTCVegtIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQ 351
Cdd:cd02660 78 khsRNLAGYSQQDAHEFFQFLLDqlhthyggdknEANDESHCNCI---IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 352 LSIKGKKNIF----ESFVD-----------YVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpQTD 416
Cdd:cd02660 155 LDIPNKSTPSwalgESGVSgtptlsdcldrFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 417 QNIKINDRFEFPEQLPLDEFL-------QKTDPKDPAN-YILHAVLVHSGDNHGGHYVVYLNpKGDGKWCKFDDDVVSRC 488
Cdd:cd02660 234 TSRKIDTYVQFPLELNMTPYTsssigdtQDSNSLDPDYtYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRV 312
|
330 340 350
....*....|....*....|....*....|.
gi 150378533 489 TKEEaiehnygghdddlsVRHCtNAYMLVYI 519
Cdd:cd02660 313 SEEE--------------VLKS-QAYLLFYH 328
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
208-518 |
2.39e-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: 108.44 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 208 KKHTG---YVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGddSSKSvplALQRVF------YELQHSDKPVGTKK 278
Cdd:cd02671 16 EKRENllpFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI--SSVE---QLQSSFllnpekYNDELANQAPRRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 279 LTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKgtcvegtipKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGK- 357
Cdd:cd02671 91 NALREVNPMYEGYLQHDAQEVLQCILGNIQELVE---------KDFQGQLVLRTRCLECETFTERREDFQDISVPVQESe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 358 ------------------KNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQN 418
Cdd:cd02671 162 lskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 419 I----KINDRFEFPEQLPLDEFlqKTDPKDPAnYILHAVLVHSGDN-HGGHYVVYLnpkgdgKWCKFDDDVVSRCTKEEA 493
Cdd:cd02671 242 YgglsKVNTPLLTPLKLSLEEW--STKPKNDV-YRLFAVVMHSGATiSSGHYTAYV------RWLLFDDSEVKVTEEKDF 312
|
330 340
....*....|....*....|....*..
gi 150378533 494 IEhnygghddDLS--VRHCTNAYMLVY 518
Cdd:cd02671 313 LE--------ALSpnTSSTSTPYLLFY 331
|
|
| MATH |
cd00121 |
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ... |
70-196 |
3.41e-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: 101.69 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 70 TFQFTVERFSRL-SESVLSPPCFVRNLPWKIMVMPRFypDRPHQKSVGFFLQC-NAESDSTSWSCHAQAVLKIINyRDDE 147
Cdd:cd00121 2 KHTWKIVNFSELeGESIYSPPFEVGGYKWRIRIYPNG--DGESGDYLSLYLELdKGESDLEKWSVRAEFTLKLVN-QNGG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 150378533 148 KSFSRRISHLFF-HKENDWGFSNFMAWSEVTDPekGFIDDDKVTFEVFVQ 196
Cdd:cd00121 79 KSLSKSFTHVFFsEKGSGWGFPKFISWDDLEDS--YYLVDDSLTIEVEVK 126
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
215-520 |
3.30e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 92.17 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLFFTN--------QLRKAVYMMPTEGDDSSKsvPLALQRVFYELqhsdKPVGTKKLTKsFGWE 286
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLpkldelldDLSKELKVLKNVIRKPEP--DLNQEEALKLF----TALWSSKEHK-VGWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 287 TlDSFMQHDVQELCRVLLDNVENKMKGTcveGTIPKLFRGKmvsyiqckevDYRSDRREDYYDI------QLSIKGKKNi 360
Cdd:COG5533 74 P-PMGSQEDAHELLGKLLDELKLDLVNS---FTIRIFKTTK----------DKKKTSTGDWFDIiielpdQTWVNNLKT- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 361 FESFVDyvAVEQLDGD-----NKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpqtDQNIKINDRFEFPEQLPLde 435
Cdd:COG5533 139 LQEFID--NMEELVDDetgvkAKENEELEVQAKQEYEVSFVKLPKILTIQLKRFANL---GGNQKIDTEVDEKFELPV-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 436 flqKTDPKDPAN----YILHAVLVHSGDNHGGHYVVYLnpKGDGKWCKFDDDVVSRCTKEEAIEHNygghdddlsvrhCT 511
Cdd:COG5533 212 ---KHDQILNIVketyYDLVGFVLHQGSLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINEK------------AK 274
|
....*....
gi 150378533 512 NAYMLVYIR 520
Cdd:COG5533 275 NAYLYFYER 283
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-518 |
2.44e-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: 84.30 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLF--------------------------FTNQLRKAVYMMPTEgdDSSKSVPLALQRVFYelQ 268
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwryddlenkfpsdvvdpandLNCQLIKLADGLLSG--RYSKPASLKSENDPY--Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 269 HSDKPVGTKKLTkSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTcvEGTIP-KLFRGKMVSYIQCKEVDYRSDRREDY 347
Cdd:cd02658 77 VGIKPSMFKALI-GKGHPEFSTMRQQDALEFLLHLIDKLDRESFKN--LGLNPnDLFKFMIEDRLECLSCKKVKYTSELS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 348 YDIQLSI---------KGKK-----NIFESFVDYVAVEQLDgDNKYDAGEHGlqEAEKGVKFLTLPPVLHLQLMRFMYDP 413
Cdd:cd02658 154 EILSLPVpkdeatekeEGELvyepvPLEDCLKAYFAPETIE-DFCSTCKEKT--TATKTTGFKTFPDYLVINMKRFQLLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 414 QTDQnIKINDRFEFPEQLpldeflqktdpkDPANYILHAVLVHSGDN-HGGHYVVYL--NPKGDGKWCKFDDDVVSRCTK 490
Cdd:cd02658 231 NWVP-KKLDVPIDVPEEL------------GPGKYELIAFISHKGTSvHSGHYVAHIkkEIDGEGKWVLFNDEKVVASQD 297
|
330 340
....*....|....*....|....*...
gi 150378533 491 EEAIEhnygghdddlsvrhcTNAYMLVY 518
Cdd:cd02658 298 PPEMK---------------KLGYIYFY 310
|
|
| MATH |
smart00061 |
meprin and TRAF homology; |
74-171 |
3.03e-15 |
|
meprin and TRAF homology;
Pssm-ID: 214496 [Multi-domain] Cd Length: 95 Bit Score: 72.33 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 74 TVERFSRLS--ESVLSPPCFVRNLPWKIMVMPRfypdrphQKSVGFFLQCNAE-SDSTSWSCHAQAVLKIINYrdDEKSF 150
Cdd:smart00061 5 TFKNVSRLEegESYFSPSEEHFNIPWRLKIYRK-------NGFLSLYLHCEKEeCDSRKWSIEAEFTLKLVSQ--NGKSL 75
|
90 100
....*....|....*....|.
gi 150378533 151 SRRISHLfFHKENDWGFSNFM 171
Cdd:smart00061 76 SKKDKHV-FEKPSGWGFSKFI 95
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-519 |
3.31e-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: 76.06 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLFFTNQlrkavymmptegdDSSKSvplalqrvfyelqhsdkpvgtkkLTKSFGWETlDSFmqh 294
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLFSQQQ-------------DVSEF-----------------------THLLLDWLE-DAF--- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 295 DVQELCRVLLDNVENKMKgtcvegtipKLFRGK--MVSYIQCKevdyRSDRREDYYDIQLSIKGKKNIFEsfvdyvAVE- 371
Cdd:cd02665 41 QAAAEAISPGEKSKNPMV---------QLFYGTflTEGVLEGK----PFCNCETFGQYPLQVNGYGNLHE------CLEa 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 372 -QLDGDNKYDAGEHGLQEAEKGVkFLTLPPVLHLQLMRFMYDpqTDQNIKINDRFEFPEQLpldeflqktdpkDPANYIL 450
Cdd:cd02665 102 aMFEGEVELLPSDHSVKSGQERW-FTELPPVLTFELSRFEFN--QGRPEKIHDKLEFPQII------------QQVPYEL 166
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150378533 451 HAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDdlsvrhcTNAYMLVYI 519
Cdd:cd02665 167 HAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRN-------PSAYCLMYI 228
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
215-518 |
3.50e-15 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 76.25 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 215 GLKNQGATCYMNSLLQTLfftnqlrkavymmptegdDSSKSVPlalqrvfyelqhsdkpvgtkkltksfgwETLDSFM-Q 293
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL------------------ASLPSLI----------------------------EYLEEFLeQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 294 HDVQELCRVLLDNVENKMKGtcvegtipkLFRGKMVSYIQCKEVDYRSDRRED-YYDIQLSIKGKKNIFESFVDyvavEQ 372
Cdd:cd02662 35 QDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSKVRYEsFTMLSLPVPNQSSGSGTTLE----HC 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 373 LDGDNKydagehglQEAEKGVK-------FLTLPPVLHLQLMRFMYDPQtDQNIKINDRFEFPEQLPldeflqktDPKdp 445
Cdd:cd02662 102 LDDFLS--------TEIIDDYKcdrcqtvIVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP--------KVL-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 446 anYILHAVLVHSGDNHGGHYVVY----LNPKG----------------DGKWCKFDDDVVSRCTKEEAIEHNYgghdddl 505
Cdd:cd02662 163 --YRLRAVVVHYGSHSSGHYVCYrrkpLFSKDkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQKS------- 233
|
330
....*....|...
gi 150378533 506 svrhctnAYMLVY 518
Cdd:cd02662 234 -------AYMLFY 239
|
|
| MATH |
pfam00917 |
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ... |
78-195 |
1.04e-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: 68.44 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 78 FSRL--SESVLSPPCFVRNLPWKIMVmprfypdRPHQKSVGFFLQCNA-ESDSTSWSCHAQAVLKIINyrDDEKSFSRRI 154
Cdd:pfam00917 4 FSKIkeGESYYSPVEERFNIPWRLQI-------YRKGGFLGLYLHCDKeEELERGWSIETEFTLKLVS--SNGKSVTKTD 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 150378533 155 SHLFfHKENDWGFSNFMAWSEVtdpEKGFIDDDKVTFEVFV 195
Cdd:pfam00917 75 THVF-EKPKGWGWGKFISWDDL---EKDYLVDDSITVEAHV 111
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
214-519 |
1.34e-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: 70.21 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 214 VGLKNQGATCYMNSLLQTLFFTNQLRKAV------YMMPTEGDDSSKSVP----------------LALQRVFYELQHSD 271
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVlnfdesKAELASDYPTERRIGgrevsrselqrsnqfvYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 272 KPVGT--KKLtksfgweTLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYI--QCKEVDYRSDRREDY 347
Cdd:cd02666 82 TRSVTpsKEL-------AYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKEQSDLikRLFSGKTKQQLVPES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 348 YDIQLSIKGKKNIFESF-VDYV-----AVEQLDGDNKYDAGEHGLQEAEKGvkflTLPPVLHLQL------------MRF 409
Cdd:cd02666 155 MGNQPSVRTKTERFLSLlVDVGkkgreIVVLLEPKDLYDALDRYFDYDSLT----KLPQRSQVQAqlaqplqrelisMDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 410 MYDPQTDQNIKINDRFEFPEQLPLDEFLQKT-------------DPKDPAnYILHAVLVHSGDNHGGHYVVYLNPKGDGK 476
Cdd:cd02666 231 YELPSSIDDIDELIREAIQSESSLVRQAQNElaelkheiekqfdDLKSYG-YRLHAVFIHRGEASSGHYWVYIKDFEENV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 150378533 477 WCKFDDDVVSRCTKEEAIEHNYGGHDddlsvrhctNAYMLVYI 519
Cdd:cd02666 310 WRKYNDETVTVVPASEVFLFTLGNTA---------TPYFLVYV 343
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
371-522 |
9.49e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 62.98 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 371 EQLD-GDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFPeqlpLDEFL--QKTDPKDPAN 447
Cdd:COG5560 688 EQLGlSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD--KIDDLVEYP----IDDLDlsGVEYMVDDPR 761
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150378533 448 --YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEhnygghdddlsvrhcTNAYMLVYIRES 522
Cdd:COG5560 762 liYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT---------------SSAYVLFYRRKS 823
|
|
| MATH_Ubp21p |
cd03775 |
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ... |
71-195 |
2.29e-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: 56.60 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 71 FQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRfypdRPHQ-KSVGFFL----QCNAES-DSTSWSCHAQAVLKIINYR 144
Cdd:cd03775 3 FTWRIKNWSELEKKVHSPKFKCGGFEWRILLFPQ----GNSQtGGVSIYLephpEEEEKApLDEDWSVCAQFALVISNPG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 150378533 145 DDEKSFSRRISHLFFHKENDWGFSNFMAWS--EVTDPEK--GFIDDDKVTFEVFV 195
Cdd:cd03775 79 DPSIQLSNVAHHRFNAEDKDWGFTRFIELRklAHRTPDKpsPFLENGELNITVYV 133
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
207-305 |
5.23e-08 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 57.20 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 207 SKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKavYMMPTEGDDS-SKSVPLA----LQRVFYEL--------QHSDKP 273
Cdd:COG5560 259 INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRD--YFLSDEYEESiNEENPLGmhgsVASAYADLikqlydgnLHAFTP 336
|
90 100 110
....*....|....*....|....*....|..
gi 150378533 274 VGTKKLTKSFgWETLDSFMQHDVQELCRVLLD 305
Cdd:COG5560 337 SGFKKTIGSF-NEEFSGYDQQDSQEFIAFLLD 367
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
214-482 |
3.45e-06 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 50.35 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 214 VGLKNQGATCYMNSLLQTLFFTNQLRKAV----------------------YMMptegDDSSKSVPLA--LQRVF----- 264
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAlshlateclkehcllcelgflfDML----EKAKGKNCQAsnFLRALssipe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 265 ---YEL-QHSDKPVGTKKLTksfgwetldsfmqHDVQELCRVLLDNV---ENKMKGTCVEGT--IPKLFRGKMVSYIQCK 335
Cdd:pfam13423 77 asaLGLlDEDRETNSAISLS-------------SLIQSFNRFLLDQLsseENSTPPNPSPAEspLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 336 EVDYRSDRREDYYDIQL------SIKGKKNIFESFVDYVA--VEQLDGD-------NKYDagehgLQEAEKGVKflTLPP 400
Cdd:pfam13423 144 NCGHESVRESSTHVLDLiyprkpSSNNKKPPNQTFSSILKssLERETTTkawcekcKRYQ-----PLESRRTVR--NLPP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 401 VLHLQLMrfMYDPQTDQNIKINDrfEFPEQLPLDEFLQKTDPKDPANYILHAVLVH-SGDNHGGHYV-------VYLNPK 472
Cdd:pfam13423 217 VLSLNAA--LTNEEWRQLWKTPG--WLPPEIGLTLSDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVsfvkvadSELEDP 292
|
330
....*....|
gi 150378533 473 GDGKWCKFDD 482
Cdd:pfam13423 293 TESQWYLFND 302
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
395-482 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 395 FLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFPEQLPLDEFLQ-------------------KTDPKDPANY--ILHAV 453
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTEGKAQ--KMFKKILIPDEIDIPDFVAddpracskcqlecrvcyddKDFSPTCGKFklSLCSA 172
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 150378533 454 LVHSGDN-HGGHYVVYL-----------NPKGDGKWCKFDD 482
Cdd:cd02670 173 VCHRGTSlETGHYVAFVrygsysltetdNEAYNAQWVFFDD 213
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
377-491 |
9.62e-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: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378533 377 NKYDaGEHGLQEAEKGVKFL--TLPPVLHLQLMRFMY-DPQTDQNIKIndrFEFP-EQLPLDEFLQKTDPKD--PANYIL 450
Cdd:cd02669 310 KKYD-GKTETELKDSLKRYLisRLPKYLIFHIKRFSKnNFFKEKNPTI---VNFPiKNLDLSDYVHFDKPSLnlSTKYNL 385
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 150378533 451 HAVLVHSGDNHG-GHYVVYLNPKGDGKWCKFDDDVVSRCTKE 491
Cdd:cd02669 386 VANIVHEGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQ 427
|
|
| |
