|
Name |
Accession |
Description |
Interval |
E-value |
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
2-1042 |
0e+00 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 653.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 2 EDDTSWRSEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMvmprFYPDRPHQKSVGFFL----QCNAESDSTSWSCHAQ 77
Cdd:COG5077 30 DPDVEELLEMSFTWKVKRWSELAKKVESPPFSVGGHTWKII----LFPQGNNQCNVSVYLeyepQELEETGGKYYDCCAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 78 AVLKIINYRDDEKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKG---FIDDDKVTFEVFVQA-DAPHGVAW------ 147
Cdd:COG5077 106 FAFDISNPKYPTIEYINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGrppFLEEGTLVITVYVRVlKDPTGVLWhsflny 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 148 DSKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGW 227
Cdd:COG5077 186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGW 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 228 ETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFV 307
Cdd:COG5077 266 DSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 308 DYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKTDPK-- 385
Cdd:COG5077 346 RYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDADKse 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 386 -DPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGG----HD---DDLSVRHCTNAYM 457
Cdd:COG5077 426 nSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpyKDkirDHSGIKRFMSAYM 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 458 LVYIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQKRKERQEAHLYMQVQIVAEDQFCGHQGNDMYD----EEKVKY 533
Cdd:COG5077 506 LVYLRKSMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDYPDfsseLNDSGL 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 534 TVFKVLKNSSLAEFVQSLSQTMGFPQD-QIRLWPMQARSNGTKRPAMLDNEAdgNKTMIELSDNEN--------PWTIFL 604
Cdd:COG5077 586 AQFVIKRGAKISDLRNNIAEHLNTPQSlYLREWTMIKRHNKTVRVDRPCNRV--NITTRELVGMNTrtgeelrsYLERII 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 605 ETVdpELAAS-GATLpkfDKDHDVMLFLKMYDPKTRSLNYCGHIYTPISCKIRDLLPVMCDRagFIQDTSLILYEEVKPN 683
Cdd:COG5077 664 EHN--QLDSQrKVAL---TKDGVINIFVKYFDYTTQPISGFGGLHVNKFLKISSISPWIEDS--ISSNLPLTLYEEIKPG 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 684 LTERIQDyDVSLDKAldELMDGDIIVFQK-DDPENDNSE-LPTAKEYFRDLYHRVDVIFCDKTIPNDPG-FVVTLSNRMN 760
Cdd:COG5077 737 MVDTIGD-NITFIGS--EIGTGDIICFEVpGAVEFDTSSaYDSALKLYDFLQGRVLVAFRRFSDEYRENvFEFLLFIGDF 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 761 YFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRHNYEGTLRD-LLQFFKPRQPKKLYYQQLKMKITDFENRRSFKCI 839
Cdd:COG5077 814 YDDLCRNVSCKLHVTPFYLRGTKSTELEDRIRRVVGSKSIFLLKEaLSSSSEFRQAPVDFYEVLDVPLSELERKRLIRLC 893
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 840 WL-NSQFREEEITLYPDKHGCVRDLLEECKKAVELGEKASGKLRLLEIVSYKIIGVHQEDELLECLSPATsrTFRIEEIP 918
Cdd:COG5077 894 FLsNGYQHVYLAEFYVEKDYTAVDHLHIVVTKVGCTDELKKSVLVYEVVNLRPVRGHSLKTLIIDDNVRS--TLYGEVFP 971
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 919 LDQVDIdKENEMLVTVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEKEFEKFKFAIV-------MMGRHQ 991
Cdd:COG5077 972 LEQEQL-TTNEMCVVVQHFFKDLIRTHGIPFMFVIVPFETFLDTKVRLVARFGYKYKLFSKIKLFVGksytdgeLDWPMS 1050
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|.
gi 1013061510 992 YINEDEYEVNLkdFEPQPGNMshprpwlgLDHfnkAPKRSRYTYLEKAIKI 1042
Cdd:COG5077 1051 YFNDEDILYDL--IERLDYIL--------LDH---PDRLRSHSSYDRAIIM 1088
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
154-465 |
3.55e-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: 478.29 E-value: 3.55e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 154 GYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMM-PTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKL---TKSFGWET 229
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIpPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELtdkTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 230 LDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDY 309
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 310 VAVEQLDGDNKYDAGEHGLQ-EAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKT------ 382
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKvDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGlakkeg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 383 ----DPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDD-------DLSVRH 451
Cdd:cd02659 241 dsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGEETqktydsgPRAFKR 320
|
330
....*....|....
gi 1013061510 452 CTNAYMLVYIRESK 465
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 ... |
562-807 |
3.33e-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: 3.33e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 562 IRLWPMQARSNGTKRPAMLDNEADGNKTMIELSDN----ENPWTIFLETVDPelaasgatLPKFDKDHDVMLFLKMYDPK 637
Cdd:pfam12436 1 IRLWPMVNRQNKTVRPDQPLPEADPAKTVEEIRDKmatrDNPLRLFLEVAEE--------LPPFDKNDDILLFLKYYDPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 638 TRSLNYCGHIYTPISCKIRDLLPVMCDRAGFIQDTSLILYEEVKPNLTErIQDYDVSLDKAldELMDGDIIVFQKDDPEN 717
Cdd:pfam12436 73 KQTLRGVGHVYVPKSSKVSDLVPIINERMGWPPDTPLLLYEEIKPNMIE-IMKPKQTLKKS--ELQDGDIICFQRELSEK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 718 DNSELPTAKEYFRDLYHRVDVIFCDKTIPNDPGFVVTLSNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRH 797
Cdd:pfam12436 150 EQDEYPTAKDYYDFLLNRVEVTFRPKDNPNDPGFTLELSKKMTYDQLAEKVAERLGVDPTKLRFTTVNNYSGQPKTPIKR 229
|
250
....*....|
gi 1013061510 798 NYEGTLRDLL 807
Cdd:pfam12436 230 NPNQTLKDIL 239
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
156-460 |
3.83e-87 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 282.79 E-value: 3.83e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 156 VGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDS----SKSVPLALQRVFYELQH--SDKPVGTKKLTKSFGW-- 227
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSrynkDINLLCALRDLFKALQKnsKSSSVSPKMFKKSLGKln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 228 ETLDSFMQHDVQELCRVLLDNVENKMKG---TCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKN--- 301
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 302 ---IFESFVDYVAVEQLDGDNKYD-AGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpqTDQNIKINDRFEFPEQLPLDE 377
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYcDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 378 FLQKTDPKDPAN---YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHnygghdddlsvrhcTN 454
Cdd:pfam00443 239 YLAEELKPKTNNlqdYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS--------------SS 304
|
....*.
gi 1013061510 455 AYMLVY 460
Cdd:pfam00443 305 AYILFY 310
|
|
| MATH_HAUSP |
cd03772 |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ... |
9-144 |
1.79e-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: 1.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 9 SEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRFYPDR-PHQKSVGFFLQCNAESDSTSWSCHAQAVLKIINYRD 87
Cdd:cd03772 1 SEATFSFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRNYPDRnPHQKSVGFFLQCNAESDSTSWSCHAQAVLRIINYKD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1013061510 88 DEKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKGFIDDDKVTFEVFVQADAPHG 144
Cdd:cd03772 81 DEPSFSRRISHLFFSKENDWGFSNFMTWSEVTDPEKGFIEDDTITLEVYVQADAPHG 137
|
|
| USP7_C2 |
pfam14533 |
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ... |
817-1028 |
1.47e-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: 1.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 817 KLYYQQLKMKITDFENRRSFKCIWLNSQF-REEEITLYPDKHGCVRDLLEECKKAVELGEKASGKLRLLEIVSYKIIGVH 895
Cdd:pfam14533 1 ALYYEVLDISLSELENKKSIKVTWLSPGLkKEEELELLVPKNGTVADLLEELQKKVKLSEEGSGKIRLYEVSNHKIYKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 896 QEDELLECLSPATsrTFRIEEIPLDQVDIDkENEMLVTVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEK 975
Cdd:pfam14533 81 SEDEPIDSLNDYL--TLYAEEIPEEELNLD-EGERLIPVFHFQKEPSRTHGIPFLFVLKPGEPFSDTKKRLQKRLGLPDK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1013061510 976 EFEKFKFAIVMMGRH-QYINEDEyevNLKDFEPQPGNMshprPWLGLDHFNKAP 1028
Cdd:pfam14533 158 EFEKIKFALVQRGKKpEYLEDDD---VLFDLLGQPDDL----PWLGLDHPDKTP 204
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
157-461 |
4.76e-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: 208.88 E-value: 4.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLFFtnqlrkavymmptegddssksvplalqrvfyelqhsdkpvgtkkltksfgwetldsfMQH 236
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS---------------------------------------------------------EQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 237 DVQELCRVLLDNVENKMKGTCVEG--------TIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSI----KGKKNIFE 304
Cdd:cd02257 24 DAHEFLLFLLDKLHEELKKSSKRTsdssslksLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVSLED 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 305 SFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQtDQNIKINDRFEFPEQLPLDEFLQKTDP 384
Cdd:cd02257 104 CLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELDLSPYLSEGEK 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 385 KDPAN-----YILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHdddlsvrhctNAYML 458
Cdd:cd02257 183 DSDSDngsykYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSS----------SAYIL 252
|
...
gi 1013061510 459 VYI 461
Cdd:cd02257 253 FYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-460 |
6.99e-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: 199.57 E-value: 6.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLA-----------LQRVFYELQHSDK----PVGtkkL 221
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDkphepqtiidqLQLIFAQLQFGNRsvvdPSG---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 222 TKSFGwetLDSFMQHDVQELCRVLLDNVENKM---KGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKG 298
Cdd:cd02668 78 VKALG---LDTGQQQDAQEFSKLFLSLLEAKLsksKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 299 KKNIFESFVDYVAVEQLDGDNKYDAGEHGL-QEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDE 377
Cdd:cd02668 155 HKTLEECIDEFLKEEQLTGDNQYFCESCNSkTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 378 FLQKTDPKDpANYILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRCTK---EEAIEHNYGGHD--DDLSVRH 451
Cdd:cd02668 235 YLAESDEGS-YVYELSGVLIHQGVSaYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGkplKLGNSEDPAKPRksEIKKGTH 313
|
330
....*....|
gi 1013061510 452 CT-NAYMLVY 460
Cdd:cd02668 314 SSrTAYMLVY 323
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-460 |
9.03e-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: 140.91 E-value: 9.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLFFTNQLRkavymmptegddssksvplALQRVFYELQHSDKPVGT-------KKLTKSFgwET 229
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT-------------------CLKDLFESISEQKKRTGVispkkfiTRLKREN--EL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 230 LDSFMQHDVQELCRVLLDNV------ENKMKGTCVEGT-----------IPKLFRGKMVSYIQCKEVDYRSDRREDYYDI 292
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIaeildaERKAEKANRKLNnnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 293 QLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPE 371
Cdd:cd02663 140 SIDVEQNTSITSCLRQFSATETLCGRNKFYCDEcCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 372 QLPLdeFLQKTDPKDPAN-YILHAVLVH--SGDNHgGHYVVYLnpKGDGKWCKFDDDVVSRcTKEEAIEHNYGGHdddls 448
Cdd:cd02663 220 ELRL--FNTTDDAENPDRlYELVAVVVHigGGPNH-GHYVSIV--KSHGGWLLFDDETVEK-IDENAVEEFFGDS----- 288
|
330
....*....|..
gi 1013061510 449 vRHCTNAYMLVY 460
Cdd:cd02663 289 -PNQATAYVLFY 299
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-461 |
1.49e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 137.41 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLFFTNQLrkAVYMmPTEGDDSSKSVPL-----ALQR-VFYELQHSDKPVGTKKLT---KSFgW 227
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPL--ANYL-LSREHSKDCCNEGfcmmcALEAhVERALASSGPGSAPRIFSsnlKQI-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 228 ETLDSFMQHDVQELCRVLLDnvenKMKGTCVEG---------------TIPKLFRGKMVSYIQCKEVDYRSDRREDYYDI 292
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLLD----AMQKACLDRfkklkavdpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 293 QLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFmydpQTDQNIKINDRFEFPE 371
Cdd:cd02661 155 SLDIKGADSLEDALEQFTKPEQLDGENKYKCERcKKKVKASKQLTIHRAPNVLTIHLKRF----SNFRGGKINKQISFPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 372 QLPLDEFL-QKTDPkdPANYILHAVLVHSG-DNHGGHYVVYLnpKG-DGKWCKFDDDVVSRCTKEEAiehnygghdddLS 448
Cdd:cd02661 231 TLDLSPYMsQPNDG--PLKYKLYAVLVHSGfSPHSGHYYCYV--KSsNGKWYNMDDSKVSPVSIETV-----------LS 295
|
330
....*....|...
gi 1013061510 449 vrhcTNAYMLVYI 461
Cdd:cd02661 296 ----QKAYILFYI 304
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-460 |
7.03e-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: 132.45 E-value: 7.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLFFTNQLRKAV-YMMPTEGDDSSKSVPL--ALQRVFYELQHSDKPVGTKKLTKSFG-----WE 228
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALkNYNPARRGANQSSDNLtnALRDLFDTMDKKQEPVPPIEFLQLLRmafpqFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 229 TLDS---FMQHDVQELCRVLLDNVENKMKGTCVEG-TIPKLFRGKMVSYIQCKEVDYRSD-RREDYYDIQLSIKGKKNif 303
Cdd:cd02657 81 EKQNqggYAQQDAEECWSQLLSVLSQKLPGAGSKGsFIDQLFGIELETKMKCTESPDEEEvSTESEYKLQCHISITTE-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 304 esfVDYVaVEQLdgdnkydagEHGLQEAE--------------KGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEF 369
Cdd:cd02657 159 ---VNYL-QDGL---------KKGLEEEIekhsptlgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 370 PEQLPLDEFLQKTdpkdpANYILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRcTKEEAIEHNYGGHDDDLs 448
Cdd:cd02657 226 PFELDLYELCTPS-----GYYELVAVITHQGRSaDSGHYVAWVRRKNDGKWIKFDDDKVSE-VTEEDILKLSGGGDWHI- 298
|
330
....*....|..
gi 1013061510 449 vrhctnAYMLVY 460
Cdd:cd02657 299 ------AYILLY 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-461 |
2.96e-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: 125.48 E-value: 2.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLfftnqlrkavymmptegddssksvplalqrvfyelqhsdkpvgtkkltksfgwetldSFMQH 236
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL---------------------------------------------------------SADQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 237 DVQELCRVLLDNVENKmkgtcvegtIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKK------NIFESFVDYV 310
Cdd:cd02674 24 DAQEFLLFLLDGLHSI---------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFT 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 311 AVEQLDGDNK-YDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFP-EQLPLDEFLQKTDPKDPA 388
Cdd:cd02674 95 KEETLDGDNAwKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTR--KLTTPVTFPlNDLDLTPYVDTRSFTGPF 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013061510 389 NYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEhnygghdddlsvrhcTNAYMLVYI 461
Cdd:cd02674 173 KYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVS---------------SSAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-460 |
2.69e-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: 125.68 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTkkltksfgweTLDSFM-- 234
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEA----------PPDYFLea 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 235 ----------QHDVQELCRVLLDNVENkmkgtcvegTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKgkknIFE 304
Cdd:cd02664 71 srppwftpgsQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP----SVQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 305 SFVDY-VAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPE--QLPLDEFLQ 380
Cdd:cd02664 138 DLLNYfLSPEKLTGDNQYYCEKcASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEvlSLPVRVESK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 381 KTDPKD----------------PANYILHAVLVHSG-DNHGGHYVVYL-NPKG-------------------DGKWCKFD 423
Cdd:cd02664 218 SSESPLekkeeesgddgelvtrQVHYRLYAVVVHSGySSESGHYFTYArDQTDadstgqecpepkdaeendeSKNWYLFN 297
|
330 340 350
....*....|....*....|....*....|....*..
gi 1013061510 424 DDVVSRCTKEEAiehnygghDDDLSVRHCTNAYMLVY 460
Cdd:cd02664 298 DSRVTFSSFESV--------QNVTSRFPKDTPYILFY 326
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-472 |
8.50e-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: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEgddssksvplalqrVFYELQHSDKpvgtkkltksfgweTLDSFMQH 236
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAP--------------QFKGYQQQ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 237 DVQELCRVLLDNVENkmkgtcvegTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQL----SIKGKKNIFESFVDYVAV 312
Cdd:cd02667 53 DSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 313 EQLDGDNKYdaGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQnIKINDRFEFPEQLPLDEFLqktDPKDPAN--- 389
Cdd:cd02667 124 EILEGNNKF--ACENCTKAKKQYLISKLPPVLVIHLKRFQQPRSANL-RKVSRHVSFPEILDLAPFC---DPKCNSSedk 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 390 ----YILHAVLVHSGDNHGGHYV--VYLNPKGDgkwckFDDDVVSRCTKEEAIEHNYGghdddlSVRHCTNAymlvYIRE 463
Cdd:cd02667 198 ssvlYRLYGVVEHSGTMRSGHYVayVKVRPPQQ-----RLSDLTKSKPAADEAGPGSG------QWYYISDS----DVRE 262
|
....*....
gi 1013061510 464 SKLSEVLQA 472
Cdd:cd02667 263 VSLEEVLKS 271
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-461 |
7.46e-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: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLFFTNQLRKavYMM------PTEGDDSSKSVPLALQRVFYELQHSDKPVG---TKKLTKSfgW 227
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRN--YFLsdrhscTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPygpINLLYLS--W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 228 ---ETLDSFMQHDVQELCRVLLD-----------NVENKMKGTCVegtIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQ 293
Cdd:cd02660 78 khsRNLAGYSQQDAHEFFQFLLDqlhthyggdknEANDESHCNCI---IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 294 LSIKGKKNIF----ESFVD-----------YVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpQTD 358
Cdd:cd02660 155 LDIPNKSTPSwalgESGVSgtptlsdcldrFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 359 QNIKINDRFEFPEQLPLDEFL-------QKTDPKDPAN-YILHAVLVHSGDNHGGHYVVYLNpKGDGKWCKFDDDVVSRC 430
Cdd:cd02660 234 TSRKIDTYVQFPLELNMTPYTsssigdtQDSNSLDPDYtYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRV 312
|
330 340 350
....*....|....*....|....*....|.
gi 1013061510 431 TKEEaiehnygghdddlsVRHCtNAYMLVYI 461
Cdd:cd02660 313 SEEE--------------VLKS-QAYLLFYH 328
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
150-460 |
2.35e-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: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 150 KKHTG---YVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGddSSKSvplALQRVF------YELQHSDKPVGTKK 220
Cdd:cd02671 16 EKRENllpFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI--SSVE---QLQSSFllnpekYNDELANQAPRRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 221 LTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKgtcvegtipKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGK- 299
Cdd:cd02671 91 NALREVNPMYEGYLQHDAQEVLQCILGNIQELVE---------KDFQGQLVLRTRCLECETFTERREDFQDISVPVQESe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 300 ------------------KNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQN 360
Cdd:cd02671 162 lskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 361 I----KINDRFEFPEQLPLDEFlqKTDPKDPAnYILHAVLVHSGDN-HGGHYVVYLnpkgdgKWCKFDDDVVSRCTKEEA 435
Cdd:cd02671 242 YgglsKVNTPLLTPLKLSLEEW--STKPKNDV-YRLFAVVMHSGATiSSGHYTAYV------RWLLFDDSEVKVTEEKDF 312
|
330 340
....*....|....*....|....*..
gi 1013061510 436 IEhnygghddDLS--VRHCTNAYMLVY 460
Cdd:cd02671 313 LE--------ALSpnTSSTSTPYLLFY 331
|
|
| MATH |
cd00121 |
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ... |
12-138 |
6.73e-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: 100.92 E-value: 6.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 12 TFQFTVERFSRL-SESVLSPPCFVRNLPWKIMVMPRFypDRPHQKSVGFFLQC-NAESDSTSWSCHAQAVLKIINyRDDE 89
Cdd:cd00121 2 KHTWKIVNFSELeGESIYSPPFEVGGYKWRIRIYPNG--DGESGDYLSLYLELdKGESDLEKWSVRAEFTLKLVN-QNGG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1013061510 90 KSFSRRISHLFF-HKENDWGFSNFMAWSEVTDPekGFIDDDKVTFEVFVQ 138
Cdd:cd00121 79 KSLSKSFTHVFFsEKGSGWGFPKFISWDDLEDS--YYLVDDSLTIEVEVK 126
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
157-462 |
2.35e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 92.56 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLFFTN--------QLRKAVYMMPTEGDDSSKsvPLALQRVFYELqhsdKPVGTKKLTKsFGWE 228
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLpkldelldDLSKELKVLKNVIRKPEP--DLNQEEALKLF----TALWSSKEHK-VGWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 229 TlDSFMQHDVQELCRVLLDNVENKMKGTcveGTIPKLFRGKmvsyiqckevDYRSDRREDYYDI------QLSIKGKKNi 302
Cdd:COG5533 74 P-PMGSQEDAHELLGKLLDELKLDLVNS---FTIRIFKTTK----------DKKKTSTGDWFDIiielpdQTWVNNLKT- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 303 FESFVDyvAVEQLDGD-----NKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpqtDQNIKINDRFEFPEQLPLde 377
Cdd:COG5533 139 LQEFID--NMEELVDDetgvkAKENEELEVQAKQEYEVSFVKLPKILTIQLKRFANL---GGNQKIDTEVDEKFELPV-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 378 flqKTDPKDPAN----YILHAVLVHSGDNHGGHYVVYLnpKGDGKWCKFDDDVVSRCTKEEAIEHNygghdddlsvrhCT 453
Cdd:COG5533 212 ---KHDQILNIVketyYDLVGFVLHQGSLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINEK------------AK 274
|
....*....
gi 1013061510 454 NAYMLVYIR 462
Cdd:COG5533 275 NAYLYFYER 283
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-460 |
2.90e-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: 83.91 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLF--------------------------FTNQLRKAVYMMPTEgdDSSKSVPLALQRVFYelQ 210
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwryddlenkfpsdvvdpandLNCQLIKLADGLLSG--RYSKPASLKSENDPY--Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 211 HSDKPVGTKKLTkSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTcvEGTIP-KLFRGKMVSYIQCKEVDYRSDRREDY 289
Cdd:cd02658 77 VGIKPSMFKALI-GKGHPEFSTMRQQDALEFLLHLIDKLDRESFKN--LGLNPnDLFKFMIEDRLECLSCKKVKYTSELS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 290 YDIQLSI---------KGKK-----NIFESFVDYVAVEQLDgDNKYDAGEHGlqEAEKGVKFLTLPPVLHLQLMRFMYDP 355
Cdd:cd02658 154 EILSLPVpkdeatekeEGELvyepvPLEDCLKAYFAPETIE-DFCSTCKEKT--TATKTTGFKTFPDYLVINMKRFQLLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 356 QTDQnIKINDRFEFPEQLpldeflqktdpkDPANYILHAVLVHSGDN-HGGHYVVYL--NPKGDGKWCKFDDDVVSRCTK 432
Cdd:cd02658 231 NWVP-KKLDVPIDVPEEL------------GPGKYELIAFISHKGTSvHSGHYVAHIkkEIDGEGKWVLFNDEKVVASQD 297
|
330 340
....*....|....*....|....*...
gi 1013061510 433 EEAIEhnygghdddlsvrhcTNAYMLVY 460
Cdd:cd02658 298 PPEMK---------------KLGYIYFY 310
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-461 |
3.05e-15 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLFFTNQlrkavymmptegdDSSKSvplalqrvfyelqhsdkpvgtkkLTKSFGWETlDSFmqh 236
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLFSQQQ-------------DVSEF-----------------------THLLLDWLE-DAF--- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 237 DVQELCRVLLDNVENKMKgtcvegtipKLFRGK--MVSYIQCKevdyRSDRREDYYDIQLSIKGKKNIFEsfvdyvAVE- 313
Cdd:cd02665 41 QAAAEAISPGEKSKNPMV---------QLFYGTflTEGVLEGK----PFCNCETFGQYPLQVNGYGNLHE------CLEa 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 314 -QLDGDNKYDAGEHGLQEAEKGVkFLTLPPVLHLQLMRFMYDpqTDQNIKINDRFEFPEQLpldeflqktdpkDPANYIL 392
Cdd:cd02665 102 aMFEGEVELLPSDHSVKSGQERW-FTELPPVLTFELSRFEFN--QGRPEKIHDKLEFPQII------------QQVPYEL 166
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013061510 393 HAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDdlsvrhcTNAYMLVYI 461
Cdd:cd02665 167 HAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRN-------PSAYCLMYI 228
|
|
| MATH |
smart00061 |
meprin and TRAF homology; |
16-113 |
4.90e-15 |
|
meprin and TRAF homology;
Pssm-ID: 214496 [Multi-domain] Cd Length: 95 Bit Score: 71.56 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 16 TVERFSRLS--ESVLSPPCFVRNLPWKIMVMPRfypdrphQKSVGFFLQCNAE-SDSTSWSCHAQAVLKIINYrdDEKSF 92
Cdd:smart00061 5 TFKNVSRLEegESYFSPSEEHFNIPWRLKIYRK-------NGFLSLYLHCEKEeCDSRKWSIEAEFTLKLVSQ--NGKSL 75
|
90 100
....*....|....*....|.
gi 1013061510 93 SRRISHLfFHKENDWGFSNFM 113
Cdd:smart00061 76 SKKDKHV-FEKPSGWGFSKFI 95
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-460 |
5.41e-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: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 157 GLKNQGATCYMNSLLQTLfftnqlrkavymmptegdDSSKSVPlalqrvfyelqhsdkpvgtkkltksfgwETLDSFM-Q 235
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL------------------ASLPSLI----------------------------EYLEEFLeQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 236 HDVQELCRVLLDNVENKMKGtcvegtipkLFRGKMVSYIQCKEVDYRSDRRED-YYDIQLSIKGKKNIFESFVDyvavEQ 314
Cdd:cd02662 35 QDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSKVRYEsFTMLSLPVPNQSSGSGTTLE----HC 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 315 LDGDNKydagehglQEAEKGVK-------FLTLPPVLHLQLMRFMYDPQtDQNIKINDRFEFPEQLPldeflqktDPKdp 387
Cdd:cd02662 102 LDDFLS--------TEIIDDYKcdrcqtvIVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP--------KVL-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 388 anYILHAVLVHSGDNHGGHYVVY----LNPKG----------------DGKWCKFDDDVVSRCTKEEAIEHNYgghdddl 447
Cdd:cd02662 163 --YRLRAVVVHYGSHSSGHYVCYrrkpLFSKDkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQKS------- 233
|
330
....*....|...
gi 1013061510 448 svrhctnAYMLVY 460
Cdd:cd02662 234 -------AYMLFY 239
|
|
| MATH |
pfam00917 |
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ... |
20-137 |
1.29e-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: 68.05 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 20 FSRL--SESVLSPPCFVRNLPWKIMVmprfypdRPHQKSVGFFLQCNA-ESDSTSWSCHAQAVLKIINyrDDEKSFSRRI 96
Cdd:pfam00917 4 FSKIkeGESYYSPVEERFNIPWRLQI-------YRKGGFLGLYLHCDKeEELERGWSIETEFTLKLVS--SNGKSVTKTD 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1013061510 97 SHLFfHKENDWGFSNFMAWSEVtdpEKGFIDDDKVTFEVFV 137
Cdd:pfam00917 75 THVF-EKPKGWGWGKFISWDDL---EKDYLVDDSITVEAHV 111
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
156-461 |
1.19e-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: 70.60 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 156 VGLKNQGATCYMNSLLQTLFFTNQLRKAV------YMMPTEGDDSSKSVP----------------LALQRVFYELQHSD 213
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVlnfdesKAELASDYPTERRIGgrevsrselqrsnqfvYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 214 KPVGT--KKLtksfgweTLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYI--QCKEVDYRSDRREDY 289
Cdd:cd02666 82 TRSVTpsKEL-------AYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKEQSDLikRLFSGKTKQQLVPES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 290 YDIQLSIKGKKNIFESF-VDYV-----AVEQLDGDNKYDAGEHGLQEAEKGvkflTLPPVLHLQL------------MRF 351
Cdd:cd02666 155 MGNQPSVRTKTERFLSLlVDVGkkgreIVVLLEPKDLYDALDRYFDYDSLT----KLPQRSQVQAqlaqplqrelisMDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 352 MYDPQTDQNIKINDRFEFPEQLPLDEFLQKT-------------DPKDPAnYILHAVLVHSGDNHGGHYVVYLNPKGDGK 418
Cdd:cd02666 231 YELPSSIDDIDELIREAIQSESSLVRQAQNElaelkheiekqfdDLKSYG-YRLHAVFIHRGEASSGHYWVYIKDFEENV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1013061510 419 WCKFDDDVVSRCTKEEAIEHNYGGHDddlsvrhctNAYMLVYI 461
Cdd:cd02666 310 WRKYNDETVTVVPASEVFLFTLGNTA---------TPYFLVYV 343
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
313-464 |
9.15e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 62.98 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 313 EQLD-GDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFPeqlpLDEFL--QKTDPKDPAN 389
Cdd:COG5560 688 EQLGlSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD--KIDDLVEYP----IDDLDlsGVEYMVDDPR 761
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013061510 390 --YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEhnygghdddlsvrhcTNAYMLVYIRES 464
Cdd:COG5560 762 liYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT---------------SSAYVLFYRRKS 823
|
|
| MATH_Ubp21p |
cd03775 |
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ... |
13-137 |
2.33e-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: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 13 FQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRfypdRPHQ-KSVGFFL----QCNAES-DSTSWSCHAQAVLKIINYR 86
Cdd:cd03775 3 FTWRIKNWSELEKKVHSPKFKCGGFEWRILLFPQ----GNSQtGGVSIYLephpEEEEKApLDEDWSVCAQFALVISNPG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1013061510 87 DDEKSFSRRISHLFFHKENDWGFSNFMAWS--EVTDPEK--GFIDDDKVTFEVFV 137
Cdd:cd03775 79 DPSIQLSNVAHHRFNAEDKDWGFTRFIELRklAHRTPDKpsPFLENGELNITVYV 133
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
149-247 |
5.14e-08 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 57.20 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 149 SKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKavYMMPTEGDDS-SKSVPLA----LQRVFYEL--------QHSDKP 215
Cdd:COG5560 259 INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRD--YFLSDEYEESiNEENPLGmhgsVASAYADLikqlydgnLHAFTP 336
|
90 100 110
....*....|....*....|....*....|..
gi 1013061510 216 VGTKKLTKSFgWETLDSFMQHDVQELCRVLLD 247
Cdd:COG5560 337 SGFKKTIGSF-NEEFSGYDQQDSQEFIAFLLD 367
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
156-424 |
3.54e-06 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 49.96 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 156 VGLKNQGATCYMNSLLQTLFFTNQLRKAV----------------------YMMptegDDSSKSVPLA--LQRVF----- 206
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAlshlateclkehcllcelgflfDML----EKAKGKNCQAsnFLRALssipe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 207 ---YEL-QHSDKPVGTKKLTksfgwetldsfmqHDVQELCRVLLDNV---ENKMKGTCVEGT--IPKLFRGKMVSYIQCK 277
Cdd:pfam13423 77 asaLGLlDEDRETNSAISLS-------------SLIQSFNRFLLDQLsseENSTPPNPSPAEspLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 278 EVDYRSDRREDYYDIQL------SIKGKKNIFESFVDYVA--VEQLDGD-------NKYDagehgLQEAEKGVKflTLPP 342
Cdd:pfam13423 144 NCGHESVRESSTHVLDLiyprkpSSNNKKPPNQTFSSILKssLERETTTkawcekcKRYQ-----PLESRRTVR--NLPP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 343 VLHLQLMrfMYDPQTDQNIKINDrfEFPEQLPLDEFLQKTDPKDPANYILHAVLVH-SGDNHGGHYV-------VYLNPK 414
Cdd:pfam13423 217 VLSLNAA--LTNEEWRQLWKTPG--WLPPEIGLTLSDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVsfvkvadSELEDP 292
|
330
....*....|
gi 1013061510 415 GDGKWCKFDD 424
Cdd:pfam13423 293 TESQWYLFND 302
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
337-424 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013061510 337 FLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFPEQLPLDEFLQ-------------------KTDPKDPANY--ILHAV 395
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTEGKAQ--KMFKKILIPDEIDIPDFVAddpracskcqlecrvcyddKDFSPTCGKFklSLCSA 172
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1013061510 396 LVHSGDN-HGGHYVVYL-----------NPKGDGKWCKFDD 424
Cdd:cd02670 173 VCHRGTSlETGHYVAFVrygsysltetdNEAYNAQWVFFDD 213
|
|
| |
