|
Name |
Accession |
Description |
Interval |
E-value |
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
6-1001 |
0e+00 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 638.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 6 FYPDRPHQKSVGFFL----QCNAESDSTSWSCHAQAVLKIINYRDDEKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPE 81
Cdd:COG5077 71 LFPQGNNQCNVSVYLeyepQELEETGGKYYDCCAQFAFDISNPKYPTIEYINKSHHRFSMESTDWGFTNFIDLNKLIEPS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 82 KG---FIDDDKVTFEVFVQA-DAPHGVAW------DSKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGD 151
Cdd:COG5077 151 PGrppFLEEGTLVITVYVRVlKDPTGVLWhsflnyNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 152 DSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVS 231
Cdd:COG5077 231 RGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 232 YIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFM 311
Cdd:COG5077 311 YIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 312 YDPQTDQNIKINDRFEFPEQLPLDEFLQKTDPK---DPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSR 388
Cdd:COG5077 391 YDFERDMMVKINDRYEFPLEIDLLPFLDRDADKsenSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTR 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 389 CTKEEAIEHNYGG----HD---DDLSVRHCTNAYMLVYIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQKRKERQE 461
Cdd:COG5077 471 ATEKEVLEENFGGdhpyKDkirDHSGIKRFMSAYMLVYLRKSMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDE 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 462 AHLYMQVQIVAEDQFCGHQGNDMYD----EEKVKYTVFKVLKNSSLAEFVQSLSQTMGFPQD-QIRLWPMQARSNGTKRP 536
Cdd:COG5077 551 IHLYRGVRLYTIDSFIHYHGFDYPDfsseLNDSGLAQFVIKRGAKISDLRNNIAEHLNTPQSlYLREWTMIKRHNKTVRV 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 537 AMLDNEAdgNKTMIELSDNEN--------PWTIFLETVdpELAAS-GATLpkfDKDHDVMLFLKMYDPKTRSLNYCGHIY 607
Cdd:COG5077 631 DRPCNRV--NITTRELVGMNTrtgeelrsYLERIIEHN--QLDSQrKVAL---TKDGVINIFVKYFDYTTQPISGFGGLH 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 608 TPISCKIRDLLPVMCDRagFIQDTSLILYEEVKPNLTERIQDyDVSLDKAldELMDGDIIVFQK-DDPENDNSE-LPTAK 685
Cdd:COG5077 704 VNKFLKISSISPWIEDS--ISSNLPLTLYEEIKPGMVDTIGD-NITFIGS--EIGTGDIICFEVpGAVEFDTSSaYDSAL 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 686 EYFRDLYHRVDVIFCDKTIPNDPG-FVVTLSNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRHNYEGTLRD 764
Cdd:COG5077 779 KLYDFLQGRVLVAFRRFSDEYRENvFEFLLFIGDFYDDLCRNVSCKLHVTPFYLRGTKSTELEDRIRRVVGSKSIFLLKE 858
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 765 -LLQFFKPRQPKKLYYQQLKMKITDFENRRSFKCIWL-NSQFREEEITLYPDKHGCVRDLLEECKKAVELGEKASGKLRL 842
Cdd:COG5077 859 aLSSSSEFRQAPVDFYEVLDVPLSELERKRLIRLCFLsNGYQHVYLAEFYVEKDYTAVDHLHIVVTKVGCTDELKKSVLV 938
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 843 LEIVSYKIIGVHQEDELLECLSPATsrTFRIEEIPLDQVDIdKENEMLVTVAHFHKEVFGTFGIPFLLRIHQGEHFREVM 922
Cdd:COG5077 939 YEVVNLRPVRGHSLKTLIIDDNVRS--TLYGEVFPLEQEQL-TTNEMCVVVQHFFKDLIRTHGIPFMFVIVPFETFLDTK 1015
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 923 KRIQSLLDIQEKEFEKFKFAIV-------MMGRHQYINEDEYEVNLkdFEPQPGNMshprpwlgLDHfnkAPKRSRYTYL 995
Cdd:COG5077 1016 VRLVARFGYKYKLFSKIKLFVGksytdgeLDWPMSYFNDEDILYDL--IERLDYIL--------LDH---PDRLRSHSSY 1082
|
....*.
gi 557129022 996 EKAIKI 1001
Cdd:COG5077 1083 DRAIIM 1088
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
113-424 |
2.85e-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: 477.52 E-value: 2.85e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 113 GYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMM-PTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKL---TKSFGWET 188
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIpPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELtdkTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 189 LDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDY 268
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 269 VAVEQLDGDNKYDAGEHGLQ-EAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKT------ 341
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKvDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGlakkeg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 342 ----DPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDD-------DLSVRH 410
Cdd:cd02659 241 dsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGEETqktydsgPRAFKR 320
|
330
....*....|....
gi 557129022 411 CTNAYMLVYIRESK 424
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 ... |
521-766 |
1.90e-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: 333.32 E-value: 1.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 521 IRLWPMQARSNGTKRPAMLDNEADGNKTMIELSDN----ENPWTIFLETVDPelaasgatLPKFDKDHDVMLFLKMYDPK 596
Cdd:pfam12436 1 IRLWPMVNRQNKTVRPDQPLPEADPAKTVEEIRDKmatrDNPLRLFLEVAEE--------LPPFDKNDDILLFLKYYDPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 597 TRSLNYCGHIYTPISCKIRDLLPVMCDRAGFIQDTSLILYEEVKPNLTErIQDYDVSLDKAldELMDGDIIVFQKDDPEN 676
Cdd:pfam12436 73 KQTLRGVGHVYVPKSSKVSDLVPIINERMGWPPDTPLLLYEEIKPNMIE-IMKPKQTLKKS--ELQDGDIICFQRELSEK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 677 DNSELPTAKEYFRDLYHRVDVIFCDKTIPNDPGFVVTLSNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRH 756
Cdd:pfam12436 150 EQDEYPTAKDYYDFLLNRVEVTFRPKDNPNDPGFTLELSKKMTYDQLAEKVAERLGVDPTKLRFTTVNNYSGQPKTPIKR 229
|
250
....*....|
gi 557129022 757 NYEGTLRDLL 766
Cdd:pfam12436 230 NPNQTLKDIL 239
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
115-419 |
2.73e-87 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 282.79 E-value: 2.73e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 115 VGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDS----SKSVPLALQRVFYELQH--SDKPVGTKKLTKSFGW-- 186
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSrynkDINLLCALRDLFKALQKnsKSSSVSPKMFKKSLGKln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 187 ETLDSFMQHDVQELCRVLLDNVENKMKG---TCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKN--- 260
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 261 ---IFESFVDYVAVEQLDGDNKYD-AGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpqTDQNIKINDRFEFPEQLPLDE 336
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYcDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 337 FLQKTDPKDPAN---YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHnygghdddlsvrhcTN 413
Cdd:pfam00443 239 YLAEELKPKTNNlqdYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS--------------SS 304
|
....*.
gi 557129022 414 AYMLVY 419
Cdd:pfam00443 305 AYILFY 310
|
|
| USP7_C2 |
pfam14533 |
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ... |
776-987 |
1.49e-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: 221.97 E-value: 1.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 776 KLYYQQLKMKITDFENRRSFKCIWLNSQF-REEEITLYPDKHGCVRDLLEECKKAVELGEKASGKLRLLEIVSYKIIGVH 854
Cdd:pfam14533 1 ALYYEVLDISLSELENKKSIKVTWLSPGLkKEEELELLVPKNGTVADLLEELQKKVKLSEEGSGKIRLYEVSNHKIYKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 855 QEDELLECLSPATsrTFRIEEIPLDQVDIDkENEMLVTVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEK 934
Cdd:pfam14533 81 SEDEPIDSLNDYL--TLYAEEIPEEELNLD-EGERLIPVFHFQKEPSRTHGIPFLFVLKPGEPFSDTKKRLQKRLGLPDK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 557129022 935 EFEKFKFAIVMMGRH-QYINEDEyevNLKDFEPQPGNMshprPWLGLDHFNKAP 987
Cdd:pfam14533 158 EFEKIKFALVQRGKKpEYLEDDD---VLFDLLGQPDDL----PWLGLDHPDKTP 204
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
116-420 |
5.93e-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: 208.49 E-value: 5.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLFFtnqlrkavymmptegddssksvplalqrvfyelqhsdkpvgtkkltksfgwetldsfMQH 195
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS---------------------------------------------------------EQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 196 DVQELCRVLLDNVENKMKGTCVEG--------TIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSI----KGKKNIFE 263
Cdd:cd02257 24 DAHEFLLFLLDKLHEELKKSSKRTsdssslksLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVSLED 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 264 SFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQtDQNIKINDRFEFPEQLPLDEFLQKTDP 343
Cdd:cd02257 104 CLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELDLSPYLSEGEK 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 344 KDPAN-----YILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHdddlsvrhctNAYML 417
Cdd:cd02257 183 DSDSDngsykYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSS----------SAYIL 252
|
...
gi 557129022 418 VYI 420
Cdd:cd02257 253 FYE 255
|
|
| MATH_HAUSP |
cd03772 |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ... |
1-103 |
9.47e-61 |
|
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: 203.07 E-value: 9.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 1 MVMPRFYPDR-PHQKSVGFFLQCNAESDSTSWSCHAQAVLKIINYRDDEKSFSRRISHLFFHKENDWGFSNFMAWSEVTD 79
Cdd:cd03772 34 MVMPRNYPDRnPHQKSVGFFLQCNAESDSTSWSCHAQAVLRIINYKDDEPSFSRRISHLFFSKENDWGFSNFMTWSEVTD 113
|
90 100
....*....|....*....|....
gi 557129022 80 PEKGFIDDDKVTFEVFVQADAPHG 103
Cdd:cd03772 114 PEKGFIEDDTITLEVYVQADAPHG 137
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-419 |
8.01e-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: 199.18 E-value: 8.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLA-----------LQRVFYELQHSDK----PVGtkkL 180
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDkphepqtiidqLQLIFAQLQFGNRsvvdPSG---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 181 TKSFGwetLDSFMQHDVQELCRVLLDNVENKM---KGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKG 257
Cdd:cd02668 78 VKALG---LDTGQQQDAQEFSKLFLSLLEAKLsksKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 258 KKNIFESFVDYVAVEQLDGDNKYDAGEHGL-QEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDE 336
Cdd:cd02668 155 HKTLEECIDEFLKEEQLTGDNQYFCESCNSkTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 337 FLQKTDPKDpANYILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRCTK---EEAIEHNYGGHD--DDLSVRH 410
Cdd:cd02668 235 YLAESDEGS-YVYELSGVLIHQGVSaYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGkplKLGNSEDPAKPRksEIKKGTH 313
|
330
....*....|
gi 557129022 411 CT-NAYMLVY 419
Cdd:cd02668 314 SSrTAYMLVY 323
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-419 |
9.43e-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: 9.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLFFTNQLRkavymmptegddssksvplALQRVFYELQHSDKPVGT-------KKLTKSFgwET 188
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT-------------------CLKDLFESISEQKKRTGVispkkfiTRLKREN--EL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 189 LDSFMQHDVQELCRVLLDNV------ENKMKGTCVEGT-----------IPKLFRGKMVSYIQCKEVDYRSDRREDYYDI 251
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIaeildaERKAEKANRKLNnnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 252 QLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPE 330
Cdd:cd02663 140 SIDVEQNTSITSCLRQFSATETLCGRNKFYCDEcCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 331 QLPLdeFLQKTDPKDPAN-YILHAVLVH--SGDNHgGHYVVYLnpKGDGKWCKFDDDVVSRcTKEEAIEHNYGGHdddls 407
Cdd:cd02663 220 ELRL--FNTTDDAENPDRlYELVAVVVHigGGPNH-GHYVSIV--KSHGGWLLFDDETVEK-IDENAVEEFFGDS----- 288
|
330
....*....|..
gi 557129022 408 vRHCTNAYMLVY 419
Cdd:cd02663 289 -PNQATAYVLFY 299
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-420 |
1.57e-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: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLFFTNQLrkAVYMmPTEGDDSSKSVPL-----ALQR-VFYELQHSDKPVGTKKLT---KSFgW 186
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPL--ANYL-LSREHSKDCCNEGfcmmcALEAhVERALASSGPGSAPRIFSsnlKQI-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 187 ETLDSFMQHDVQELCRVLLDnvenKMKGTCVEG---------------TIPKLFRGKMVSYIQCKEVDYRSDRREDYYDI 251
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLLD----AMQKACLDRfkklkavdpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 252 QLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFmydpQTDQNIKINDRFEFPE 330
Cdd:cd02661 155 SLDIKGADSLEDALEQFTKPEQLDGENKYKCERcKKKVKASKQLTIHRAPNVLTIHLKRF----SNFRGGKINKQISFPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 331 QLPLDEFL-QKTDPkdPANYILHAVLVHSG-DNHGGHYVVYLnpKG-DGKWCKFDDDVVSRCTKEEAiehnygghdddLS 407
Cdd:cd02661 231 TLDLSPYMsQPNDG--PLKYKLYAVLVHSGfSPHSGHYYCYV--KSsNGKWYNMDDSKVSPVSIETV-----------LS 295
|
330
....*....|...
gi 557129022 408 vrhcTNAYMLVYI 420
Cdd:cd02661 296 ----QKAYILFYI 304
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-419 |
7.14e-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: 7.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLFFTNQLRKAV-YMMPTEGDDSSKSVPL--ALQRVFYELQHSDKPVGTKKLTKSFG-----WE 187
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALkNYNPARRGANQSSDNLtnALRDLFDTMDKKQEPVPPIEFLQLLRmafpqFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 188 TLDS---FMQHDVQELCRVLLDNVENKMKGTCVEG-TIPKLFRGKMVSYIQCKEVDYRSD-RREDYYDIQLSIKGKKNif 262
Cdd:cd02657 81 EKQNqggYAQQDAEECWSQLLSVLSQKLPGAGSKGsFIDQLFGIELETKMKCTESPDEEEvSTESEYKLQCHISITTE-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 263 esfVDYVaVEQLdgdnkydagEHGLQEAE--------------KGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEF 328
Cdd:cd02657 159 ---VNYL-QDGL---------KKGLEEEIekhsptlgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 329 PEQLPLDEFLQKTdpkdpANYILHAVLVHSGDN-HGGHYVVYLNPKGDGKWCKFDDDVVSRcTKEEAIEHNYGGHDDDLs 407
Cdd:cd02657 226 PFELDLYELCTPS-----GYYELVAVITHQGRSaDSGHYVAWVRRKNDGKWIKFDDDKVSE-VTEEDILKLSGGGDWHI- 298
|
330
....*....|..
gi 557129022 408 vrhctnAYMLVY 419
Cdd:cd02657 299 ------AYILLY 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-420 |
3.07e-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: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLfftnqlrkavymmptegddssksvplalqrvfyelqhsdkpvgtkkltksfgwetldSFMQH 195
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL---------------------------------------------------------SADQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 196 DVQELCRVLLDNVENKmkgtcvegtIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKK------NIFESFVDYV 269
Cdd:cd02674 24 DAQEFLLFLLDGLHSI---------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFT 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 270 AVEQLDGDNK-YDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFP-EQLPLDEFLQKTDPKDPA 347
Cdd:cd02674 95 KEETLDGDNAwKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTR--KLTTPVTFPlNDLDLTPYVDTRSFTGPF 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557129022 348 NYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEhnygghdddlsvrhcTNAYMLVYI 420
Cdd:cd02674 173 KYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVS---------------SSAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-419 |
2.07e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 126.07 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTkkltksfgweTLDSFM-- 193
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEA----------PPDYFLea 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 194 ----------QHDVQELCRVLLDNVENkmkgtcvegTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKgkknIFE 263
Cdd:cd02664 71 srppwftpgsQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP----SVQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 264 SFVDY-VAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPE--QLPLDEFLQ 339
Cdd:cd02664 138 DLLNYfLSPEKLTGDNQYYCEKcASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEvlSLPVRVESK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 340 KTDPKD----------------PANYILHAVLVHSG-DNHGGHYVVYL-NPKG-------------------DGKWCKFD 382
Cdd:cd02664 218 SSESPLekkeeesgddgelvtrQVHYRLYAVVVHSGySSESGHYFTYArDQTDadstgqecpepkdaeendeSKNWYLFN 297
|
330 340 350
....*....|....*....|....*....|....*..
gi 557129022 383 DDVVSRCTKEEAiehnygghDDDLSVRHCTNAYMLVY 419
Cdd:cd02664 298 DSRVTFSSFESV--------QNVTSRFPKDTPYILFY 326
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-431 |
7.01e-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: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEgddssksvplalqrVFYELQHSDKpvgtkkltksfgweTLDSFMQH 195
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAP--------------QFKGYQQQ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 196 DVQELCRVLLDNVENkmkgtcvegTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQL----SIKGKKNIFESFVDYVAV 271
Cdd:cd02667 53 DSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 272 EQLDGDNKYdaGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQnIKINDRFEFPEQLPLDEFLqktDPKDPAN--- 348
Cdd:cd02667 124 EILEGNNKF--ACENCTKAKKQYLISKLPPVLVIHLKRFQQPRSANL-RKVSRHVSFPEILDLAPFC---DPKCNSSedk 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 349 ----YILHAVLVHSGDNHGGHYV--VYLNPKGDgkwckFDDDVVSRCTKEEAIEHNYGghdddlSVRHCTNAymlvYIRE 422
Cdd:cd02667 198 ssvlYRLYGVVEHSGTMRSGHYVayVKVRPPQQ-----RLSDLTKSKPAADEAGPGSG------QWYYISDS----DVRE 262
|
....*....
gi 557129022 423 SKLSEVLQA 431
Cdd:cd02667 263 VSLEEVLKS 271
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-420 |
8.08e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 115.55 E-value: 8.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLFFTNQLRKavYMM------PTEGDDSSKSVPLALQRVFYELQHSDKPVG---TKKLTKSfgW 186
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRN--YFLsdrhscTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPygpINLLYLS--W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 187 ---ETLDSFMQHDVQELCRVLLD-----------NVENKMKGTCVegtIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQ 252
Cdd:cd02660 78 khsRNLAGYSQQDAHEFFQFLLDqlhthyggdknEANDESHCNCI---IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 253 LSIKGKKNIF----ESFVD-----------YVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpQTD 317
Cdd:cd02660 155 LDIPNKSTPSwalgESGVSgtptlsdcldrFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 318 QNIKINDRFEFPEQLPLDEFL-------QKTDPKDPAN-YILHAVLVHSGDNHGGHYVVYLNpKGDGKWCKFDDDVVSRC 389
Cdd:cd02660 234 TSRKIDTYVQFPLELNMTPYTsssigdtQDSNSLDPDYtYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRV 312
|
330 340 350
....*....|....*....|....*....|.
gi 557129022 390 TKEEaiehnygghdddlsVRHCtNAYMLVYI 420
Cdd:cd02660 313 SEEE--------------VLKS-QAYLLFYH 328
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
109-419 |
1.99e-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: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 109 KKHTG---YVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGddSSKSvplALQRVF------YELQHSDKPVGTKK 179
Cdd:cd02671 16 EKRENllpFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI--SSVE---QLQSSFllnpekYNDELANQAPRRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 180 LTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKgtcvegtipKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGK- 258
Cdd:cd02671 91 NALREVNPMYEGYLQHDAQEVLQCILGNIQELVE---------KDFQGQLVLRTRCLECETFTERREDFQDISVPVQESe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 259 ------------------KNIFESFVDYVAVEQLDGDNKYDAGE-HGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQN 319
Cdd:cd02671 162 lskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 320 I----KINDRFEFPEQLPLDEFlqKTDPKDPAnYILHAVLVHSGDN-HGGHYVVYLnpkgdgKWCKFDDDVVSRCTKEEA 394
Cdd:cd02671 242 YgglsKVNTPLLTPLKLSLEEW--STKPKNDV-YRLFAVVMHSGATiSSGHYTAYV------RWLLFDDSEVKVTEEKDF 312
|
330 340
....*....|....*....|....*..
gi 557129022 395 IEhnygghddDLS--VRHCTNAYMLVY 419
Cdd:cd02671 313 LE--------ALSpnTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
116-421 |
3.13e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 92.17 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLFFTN--------QLRKAVYMMPTEGDDSSKsvPLALQRVFYELqhsdKPVGTKKLTKsFGWE 187
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLpkldelldDLSKELKVLKNVIRKPEP--DLNQEEALKLF----TALWSSKEHK-VGWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 188 TlDSFMQHDVQELCRVLLDNVENKMKGTcveGTIPKLFRGKmvsyiqckevDYRSDRREDYYDI------QLSIKGKKNi 261
Cdd:COG5533 74 P-PMGSQEDAHELLGKLLDELKLDLVNS---FTIRIFKTTK----------DKKKTSTGDWFDIiielpdQTWVNNLKT- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 262 FESFVDyvAVEQLDGD-----NKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDpqtDQNIKINDRFEFPEQLPLde 336
Cdd:COG5533 139 LQEFID--NMEELVDDetgvkAKENEELEVQAKQEYEVSFVKLPKILTIQLKRFANL---GGNQKIDTEVDEKFELPV-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 337 flqKTDPKDPAN----YILHAVLVHSGDNHGGHYVVYLnpKGDGKWCKFDDDVVSRCTKEEAIEHNygghdddlsvrhCT 412
Cdd:COG5533 212 ---KHDQILNIVketyYDLVGFVLHQGSLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINEK------------AK 274
|
....*....
gi 557129022 413 NAYMLVYIR 421
Cdd:COG5533 275 NAYLYFYER 283
|
|
| MATH |
cd00121 |
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ... |
5-97 |
1.96e-17 |
|
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: 79.35 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 5 RFYP--DRPHQKSVGFFLQC-NAESDSTSWSCHAQAVLKIINyRDDEKSFSRRISHLFF-HKENDWGFSNFMAWSEVTDP 80
Cdd:cd00121 33 RIYPngDGESGDYLSLYLELdKGESDLEKWSVRAEFTLKLVN-QNGGKSLSKSFTHVFFsEKGSGWGFPKFISWDDLEDS 111
|
90
....*....|....*..
gi 557129022 81 ekGFIDDDKVTFEVFVQ 97
Cdd:cd00121 112 --YYLVDDSLTIEVEVK 126
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-419 |
3.55e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 83.53 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLF--------------------------FTNQLRKAVYMMPTEgdDSSKSVPLALQRVFYelQ 169
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwryddlenkfpsdvvdpandLNCQLIKLADGLLSG--RYSKPASLKSENDPY--Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 170 HSDKPVGTKKLTkSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTcvEGTIP-KLFRGKMVSYIQCKEVDYRSDRREDY 248
Cdd:cd02658 77 VGIKPSMFKALI-GKGHPEFSTMRQQDALEFLLHLIDKLDRESFKN--LGLNPnDLFKFMIEDRLECLSCKKVKYTSELS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 249 YDIQLSI---------KGKK-----NIFESFVDYVAVEQLDgDNKYDAGEHGlqEAEKGVKFLTLPPVLHLQLMRFMYDP 314
Cdd:cd02658 154 EILSLPVpkdeatekeEGELvyepvPLEDCLKAYFAPETIE-DFCSTCKEKT--TATKTTGFKTFPDYLVINMKRFQLLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 315 QTDQnIKINDRFEFPEQLpldeflqktdpkDPANYILHAVLVHSGDN-HGGHYVVYL--NPKGDGKWCKFDDDVVSRCTK 391
Cdd:cd02658 231 NWVP-KKLDVPIDVPEEL------------GPGKYELIAFISHKGTSvHSGHYVAHIkkEIDGEGKWVLFNDEKVVASQD 297
|
330 340
....*....|....*....|....*...
gi 557129022 392 EEAIEhnygghdddlsvrhcTNAYMLVY 419
Cdd:cd02658 298 PPEMK---------------KLGYIYFY 310
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-420 |
2.60e-15 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 76.44 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLFFTNQlrkavymmptegdDSSKSvplalqrvfyelqhsdkpvgtkkLTKSFGWETlDSFmqh 195
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLFSQQQ-------------DVSEF-----------------------THLLLDWLE-DAF--- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 196 DVQELCRVLLDNVENKMKgtcvegtipKLFRGK--MVSYIQCKevdyRSDRREDYYDIQLSIKGKKNIFEsfvdyvAVE- 272
Cdd:cd02665 41 QAAAEAISPGEKSKNPMV---------QLFYGTflTEGVLEGK----PFCNCETFGQYPLQVNGYGNLHE------CLEa 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 273 -QLDGDNKYDAGEHGLQEAEKGVkFLTLPPVLHLQLMRFMYDpqTDQNIKINDRFEFPEQLpldeflqktdpkDPANYIL 351
Cdd:cd02665 102 aMFEGEVELLPSDHSVKSGQERW-FTELPPVLTFELSRFEFN--QGRPEKIHDKLEFPQII------------QQVPYEL 166
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557129022 352 HAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDdlsvrhcTNAYMLVYI 420
Cdd:cd02665 167 HAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRN-------PSAYCLMYI 228
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-419 |
4.56e-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: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 116 GLKNQGATCYMNSLLQTLfftnqlrkavymmptegdDSSKSVPlalqrvfyelqhsdkpvgtkkltksfgwETLDSFM-Q 194
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL------------------ASLPSLI----------------------------EYLEEFLeQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 195 HDVQELCRVLLDNVENKMKGtcvegtipkLFRGKMVSYIQCKEVDYRSDRRED-YYDIQLSIKGKKNIFESFVDyvavEQ 273
Cdd:cd02662 35 QDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSKVRYEsFTMLSLPVPNQSSGSGTTLE----HC 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 274 LDGDNKydagehglQEAEKGVK-------FLTLPPVLHLQLMRFMYDPQtDQNIKINDRFEFPEQLPldeflqktDPKdp 346
Cdd:cd02662 102 LDDFLS--------TEIIDDYKcdrcqtvIVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP--------KVL-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 347 anYILHAVLVHSGDNHGGHYVVY----LNPKG----------------DGKWCKFDDDVVSRCTKEEAIEHNYgghdddl 406
Cdd:cd02662 163 --YRLRAVVVHYGSHSSGHYVCYrrkpLFSKDkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQKS------- 233
|
330
....*....|...
gi 557129022 407 svrhctnAYMLVY 419
Cdd:cd02662 234 -------AYMLFY 239
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
115-420 |
1.27e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 70.21 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 115 VGLKNQGATCYMNSLLQTLFFTNQLRKAV------YMMPTEGDDSSKSVP----------------LALQRVFYELQHSD 172
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVlnfdesKAELASDYPTERRIGgrevsrselqrsnqfvYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 173 KPVGT--KKLtksfgweTLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYI--QCKEVDYRSDRREDY 248
Cdd:cd02666 82 TRSVTpsKEL-------AYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKEQSDLikRLFSGKTKQQLVPES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 249 YDIQLSIKGKKNIFESF-VDYV-----AVEQLDGDNKYDAGEHGLQEAEKGvkflTLPPVLHLQL------------MRF 310
Cdd:cd02666 155 MGNQPSVRTKTERFLSLlVDVGkkgreIVVLLEPKDLYDALDRYFDYDSLT----KLPQRSQVQAqlaqplqrelisMDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 311 MYDPQTDQNIKINDRFEFPEQLPLDEFLQKT-------------DPKDPAnYILHAVLVHSGDNHGGHYVVYLNPKGDGK 377
Cdd:cd02666 231 YELPSSIDDIDELIREAIQSESSLVRQAQNElaelkheiekqfdDLKSYG-YRLHAVFIHRGEASSGHYWVYIKDFEENV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 557129022 378 WCKFDDDVVSRCTKEEAIEHNYGGHDddlsvrhctNAYMLVYI 420
Cdd:cd02666 310 WRKYNDETVTVVPASEVFLFTLGNTA---------TPYFLVYV 343
|
|
| MATH |
pfam00917 |
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ... |
17-96 |
1.06e-11 |
|
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: 62.66 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 17 GFFLQCNA-ESDSTSWSCHAQAVLKIINyrDDEKSFSRRISHLFfHKENDWGFSNFMAWSEVtdpEKGFIDDDKVTFEVF 95
Cdd:pfam00917 37 GLYLHCDKeEELERGWSIETEFTLKLVS--SNGKSVTKTDTHVF-EKPKGWGWGKFISWDDL---EKDYLVDDSITVEAH 110
|
.
gi 557129022 96 V 96
Cdd:pfam00917 111 V 111
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
272-423 |
8.31e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 62.98 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 272 EQLD-GDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFPeqlpLDEFL--QKTDPKDPAN 348
Cdd:COG5560 688 EQLGlSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD--KIDDLVEYP----IDDLDlsGVEYMVDDPR 761
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557129022 349 --YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEhnygghdddlsvrhcTNAYMLVYIRES 423
Cdd:COG5560 762 liYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT---------------SSAYVLFYRRKS 823
|
|
| MATH |
smart00061 |
meprin and TRAF homology; |
14-72 |
2.23e-08 |
|
meprin and TRAF homology;
Pssm-ID: 214496 [Multi-domain] Cd Length: 95 Bit Score: 52.69 E-value: 2.23e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 14 KSVGFFLQCNAE-SDSTSWSCHAQAVLKIINYrdDEKSFSRRISHLfFHKENDWGFSNFM 72
Cdd:smart00061 39 GFLSLYLHCEKEeCDSRKWSIEAEFTLKLVSQ--NGKSLSKKDKHV-FEKPSGWGFSKFI 95
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
110-206 |
4.56e-08 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 57.20 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 110 KHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKavYMMPTEGDDS-SKSVPLA----LQRVFYEL--------QHSDKPVG 176
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRD--YFLSDEYEESiNEENPLGmhgsVASAYADLikqlydgnLHAFTPSG 338
|
90 100 110
....*....|....*....|....*....|
gi 557129022 177 TKKLTKSFgWETLDSFMQHDVQELCRVLLD 206
Cdd:COG5560 339 FKKTIGSF-NEEFSGYDQQDSQEFIAFLLD 367
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
115-383 |
3.29e-06 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 49.96 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 115 VGLKNQGATCYMNSLLQTLFFTNQLRKAV----------------------YMMptegDDSSKSVPLA--LQRVF----- 165
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAlshlateclkehcllcelgflfDML----EKAKGKNCQAsnFLRALssipe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 166 ---YEL-QHSDKPVGTKKLTksfgwetldsfmqHDVQELCRVLLDNV---ENKMKGTCVEGT--IPKLFRGKMVSYIQCK 236
Cdd:pfam13423 77 asaLGLlDEDRETNSAISLS-------------SLIQSFNRFLLDQLsseENSTPPNPSPAEspLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 237 EVDYRSDRREDYYDIQL------SIKGKKNIFESFVDYVA--VEQLDGD-------NKYDagehgLQEAEKGVKflTLPP 301
Cdd:pfam13423 144 NCGHESVRESSTHVLDLiyprkpSSNNKKPPNQTFSSILKssLERETTTkawcekcKRYQ-----PLESRRTVR--NLPP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 302 VLHLQLMrfMYDPQTDQNIKINDrfEFPEQLPLDEFLQKTDPKDPANYILHAVLVH-SGDNHGGHYV-------VYLNPK 373
Cdd:pfam13423 217 VLSLNAA--LTNEEWRQLWKTPG--WLPPEIGLTLSDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVsfvkvadSELEDP 292
|
330
....*....|
gi 557129022 374 GDGKWCKFDD 383
Cdd:pfam13423 293 TESQWYLFND 302
|
|
| MATH_Ubp21p |
cd03775 |
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ... |
6-96 |
4.76e-05 |
|
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: 44.27 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 6 FYPDRPHQ-KSVGFFL----QCNAES-DSTSWSCHAQAVLKIINYRDDEKSFSRRISHLFFHKENDWGFSNFMAWS--EV 77
Cdd:cd03775 33 LFPQGNSQtGGVSIYLephpEEEEKApLDEDWSVCAQFALVISNPGDPSIQLSNVAHHRFNAEDKDWGFTRFIELRklAH 112
|
90 100
....*....|....*....|.
gi 557129022 78 TDPEK--GFIDDDKVTFEVFV 96
Cdd:cd03775 113 RTPDKpsPFLENGELNITVYV 133
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
296-383 |
2.31e-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: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557129022 296 FLTLPPVLHLQLMRFMYDPQTDQniKINDRFEFPEQLPLDEFLQ-------------------KTDPKDPANY--ILHAV 354
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTEGKAQ--KMFKKILIPDEIDIPDFVAddpracskcqlecrvcyddKDFSPTCGKFklSLCSA 172
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 557129022 355 LVHSGDN-HGGHYVVYL-----------NPKGDGKWCKFDD 383
Cdd:cd02670 173 VCHRGTSlETGHYVAFVrygsysltetdNEAYNAQWVFFDD 213
|
|
| |
