|
Name |
Accession |
Description |
Interval |
E-value |
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
101-1115 |
0e+00 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 564.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 101 ETTFSFTVENVVQLKSQRLSPPVYVRMLPWRIMVIP---NDRALGFFL----QCNGENDSPTWSCNAIAELRLKCHKPDA 173
Cdd:COG5077 38 EMSFTWKVKRWSELAKKVESPPFSVGGHTWKIILFPqgnNQCNVSVYLeyepQELEETGGKYYDCCAQFAFDISNPKYPT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 174 QPFTRARiKHLFYSKENDYGYSNFITWQELKDSEK---SYVHNNSITLEVHV-VADAPHGVLW------DSKKHTGYVGL 243
Cdd:COG5077 118 IEYINKS-HHRFSMESTDWGFTNFIDLNKLIEPSPgrpPFLEEGTLVITVYVrVLKDPTGVLWhsflnyNSKKETGYVGL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 244 KNQGATCYMNSLLQTLYFTNSLRLSVYRIPTEADDSSKSVGLSLQRVFHELQFGDRPVGTKKLTKSFGWETLDSFMQHDV 323
Cdd:COG5077 197 RNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWDSDDSFMQHDI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 324 QEFLRVLLDKLESKMKGTILEGTIPGLFEGKMSSYIKCKNVDYNSTRYETFYDIQLNIKDKKNIYESFQDYVAPETLEGD 403
Cdd:COG5077 277 QEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 404 NKYDAGVHGLQEASKGVIFTSFPPVLHLHLMRFQYDPVTDSSIKYNDRFEFYEHINLDRYLAE----SENTLADYVLHAV 479
Cdd:COG5077 357 NRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRdadkSENSDAVYVLYGV 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 480 LVHSGDNHGGHYVVFINPKADGRWFKFDDDVVSSCRKQEAIEQNYGG---MDDEISFHAKC---SNAYMLVYIRQSELDR 553
Cdd:COG5077 437 LVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpYKDKIRDHSGIkrfMSAYMLVYLRKSMLDD 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 554 VLGDITESEISSDLVERLDLEKRIEMARRKERGEANTYVSVHVILEENFEEQHKRRLFDL-----EKVHPRvFRIKQNQT 628
Cdd:COG5077 517 LLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDYPDFsselnDSGLAQ-FVIKRGAK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 629 VDELVDLFVRGFGVSRQR-MRMW------------------------NLCTAQTQKF----SHFDFVAEGSRTIEQISTS 679
Cdd:COG5077 596 ISDLRNNIAEHLNTPQSLyLREWtmikrhnktvrvdrpcnrvnittrELVGMNTRTGeelrSYLERIIEHNQLDSQRKVA 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 680 -QKPWVIwlqlawtdvpgplppfnpktesLLFLKYYDPRNKRLNYIGCTQQPHTRRLIDLVPDVNSKLgfEPDTELTIYD 758
Cdd:COG5077 676 lTKDGVI----------------------NIFVKYFDYTTQPISGFGGLHVNKFLKISSISPWIEDSI--SSNLPLTLYE 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 759 EyADKKLVNLNEPIESalFIPQDHLQGHILIFERENvDAKLDLPTVGDYFLDLV----YRIEIIFSDKCNP-NEPDFTLE 833
Cdd:COG5077 732 E-IKPGMVDTIGDNIT--FIGSEIGTGDIICFEVPG-AVEFDTSSAYDSALKLYdflqGRVLVAFRRFSDEyRENVFEFL 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 834 LSNRYNYDQLANAVAERLNTDPQKLQFFMCiNNYKETAGNAVP----YTFKDLVSYTKQSSTK-RIFYQRLSLSIHELDN 908
Cdd:COG5077 808 LFIGDFYDDLCRNVSCKLHVTPFYLRGTKS-TELEDRIRRVVGsksiFLLKEALSSSSEFRQApVDFYEVLDVPLSELER 886
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 909 KKQFKCVWVSSDLKDEKELVLYPNKNDTVKGLLEEAAKKISFAENSRRKLRLLKISNHKIVAvckdDIPLDTLLKSNESI 988
Cdd:COG5077 887 KRLIRLCFLSNGYQHVYLAEFYVEKDYTAVDHLHIVVTKVGCTDELKKSVLVYEVVNLRPVR----GHSLKTLIIDDNVR 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 989 TTAQGaqktfriEEVPAEDMQLAENEFLIPVAHFSKELYNSFGIPFLTKARQGEPYGALKQRIQRRLNVQDKEWENYKFC 1068
Cdd:COG5077 963 STLYG-------EVFPLEQEQLTTNEMCVVVQHFFKDLIRTHGIPFMFVIVPFETFLDTKVRLVARFGYKYKLFSKIKLF 1035
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....
gi 665390884 1069 VISMGHNADV-------NDNTPVDLEVYRswTSGQLpffgLDHINKSRKRSSLN 1115
Cdd:COG5077 1036 VGKSYTDGELdwpmsyfNDEDILYDLIER--LDYIL----LDHPDRLRSHSSYD 1083
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
239-549 |
1.45e-157 |
|
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: 471.36 E-value: 1.45e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 239 GYVGLKNQGATCYMNSLLQTLYFTNSLRLSVYRI-PTEADDSSKSVGLSLQRVFHELQFGDRPVGTKKL---TKSFGWET 314
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIpPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELtdkTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 315 LDSFMQHDVQEFLRVLLDKLESKMKGTILEGTIPGLFEGKMSSYIKCKNVDYNSTRYETFYDIQLNIKDKKNIYESFQDY 394
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 395 VAPETLEGDNKYDAGVHGLQ-EASKGVIFTSFPPVLHLHLMRFQYDPVTDSSIKYNDRFEFYEHINLDRYLAES------ 467
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKvDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGlakkeg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 468 -----ENTLADYVLHAVLVHSGDNHGGHYVVFINPKADGRWFKFDDDVVSSCRKQEAIEQNYGGMDDEISF------HAK 536
Cdd:cd02659 241 dsekkDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGEETQKTYdsgpraFKR 320
|
330
....*....|...
gi 665390884 537 CSNAYMLVYIRQS 549
Cdd:cd02659 321 TTNAYMLFYERKS 333
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
241-545 |
1.96e-85 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 279.33 E-value: 1.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 241 VGLKNQGATCYMNSLLQTLYFTNSLRLSVYRIPTEADDS----SKSVGLSLQRVFHELQFG--DRPVGTKKLTKSFGW-- 312
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSrynkDINLLCALRDLFKALQKNskSSSVSPKMFKKSLGKln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 313 ETLDSFMQHDVQEFLRVLLDKLESKMKG---TILEGTIPGLFEGKMSSYIKCKNVDYNSTRYETFYDIQLNIKDKKN--- 386
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 387 ---IYESFQDYVAPETLEGDNKYDAGV-HGLQEASKGVIFTSFPPVLHLHLMRFQYDpvTDSSIKYNDRFEFYEHINLDR 462
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYCDKcGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 463 YLA----ESENTLADYVLHAVLVHSGDNHGGHYVVFINPKADGRWFKFDDDVVSSCRKQEAIEQnyggmddeisfhakcS 538
Cdd:pfam00443 239 YLAeelkPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS---------------S 303
|
....*..
gi 665390884 539 NAYMLVY 545
Cdd:pfam00443 304 SAYILFY 310
|
|
| MATH_HAUSP |
cd03772 |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ... |
100-229 |
8.54e-71 |
|
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: 231.96 E-value: 8.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 100 SETTFSFTVENVVQLKSQRLSPPVYVRMLPWRIMVIPND--------RALGFFLQCNGENDSPTWSCNAIAELRLKCHKP 171
Cdd:cd03772 1 SEATFSFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRNypdrnphqKSVGFFLQCNAESDSTSWSCHAQAVLRIINYKD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 665390884 172 DaQPFTRARIKHLFYSKENDYGYSNFITWQELKDSEKSYVHNNSITLEVHVVADAPHG 229
Cdd:cd03772 81 D-EPSFSRRISHLFFSKENDWGFSNFMTWSEVTDPEKGFIEDDTITLEVYVQADAPHG 137
|
|
| USP7_C2 |
pfam14533 |
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ... |
893-1109 |
8.82e-71 |
|
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: 234.69 E-value: 8.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 893 RIFYQRLSLSIHELDNKKQFKCVWVSSDLKDEKELVLYPNKNDTVKGLLEEAAKKISFAENSRRKLRLLKISNHKIVAVC 972
Cdd:pfam14533 1 ALYYEVLDISLSELENKKSIKVTWLSPGLKKEEELELLVPKNGTVADLLEELQKKVKLSEEGSGKIRLYEVSNHKIYKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 973 KDDIPLDTLLKSnesittaqgaqKTFRIEEVPAEDMQLAENEFLIPVAHFSKELYNSFGIPFLTKARQGEPYGALKQRIQ 1052
Cdd:pfam14533 81 SEDEPIDSLNDY-----------LTLYAEEIPEEELNLDEGERLIPVFHFQKEPSRTHGIPFLFVLKPGEPFSDTKKRLQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665390884 1053 RRLNVQDKEWENYKFCVISMGHNADVNDNTPVDLEVYrsWTSGQLPFFGLDHINKSR 1109
Cdd:pfam14533 150 KRLGLPDKEFEKIKFALVQRGKKPEYLEDDDVLFDLL--GQPDDLPWLGLDHPDKTP 204
|
|
| USP7_ICP0_bdg |
pfam12436 |
ICP0-binding domain of Ubiquitin-specific protease 7; This domain is one of two C-terminal ... |
647-879 |
2.16e-69 |
|
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: 232.02 E-value: 2.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 647 MRMWNLCTAQ--TQKFSHFDFVAEGSRTIEQI----STSQKPWVIWLQLAwtdvpGPLPPFNPKTESLLFLKYYDPRNKR 720
Cdd:pfam12436 1 IRLWPMVNRQnkTVRPDQPLPEADPAKTVEEIrdkmATRDNPLRLFLEVA-----EELPPFDKNDDILLFLKYYDPEKQT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 721 LNYIGCTQQPHTRRLIDLVPDVNSKLGFEPDTELTIYDEYA--DKKLVNLNEPIESALFipQDhlqGHILIFERENVD-A 797
Cdd:pfam12436 76 LRGVGHVYVPKSSKVSDLVPIINERMGWPPDTPLLLYEEIKpnMIEIMKPKQTLKKSEL--QD---GDIICFQRELSEkE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 798 KLDLPTVGDYFLDLVYRIEIIFSDKCNPNEPDFTLELSNRYNYDQLANAVAERLNTDPQKLQFFMCiNNYKETAGNAVPY 877
Cdd:pfam12436 151 QDEYPTAKDYYDFLLNRVEVTFRPKDNPNDPGFTLELSKKMTYDQLAEKVAERLGVDPTKLRFTTV-NNYSGQPKTPIKR 229
|
..
gi 665390884 878 TF 879
Cdd:pfam12436 230 NP 231
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
242-546 |
1.19e-63 |
|
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: 216.58 E-value: 1.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYFtnslrlsvyripteaddssksvglslqrvfhelqfgdrpvgtkkltksfgwetldsfMQH 321
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS---------------------------------------------------------EQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 322 DVQEFLRVLLDKLESKMKG--------TILEGTIPGLFEGKMSSYIKCKNVDYNSTRYETFYDIQLNI----KDKKNIYE 389
Cdd:cd02257 24 DAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVSLED 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 390 SFQDYVAPETLEGDNKYDAGVHGLQEASKGVIFTSFPPVLHLHLMRFQYDPvTDSSIKYNDRFEFYEHINLDRYLAESEN 469
Cdd:cd02257 104 CLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLSPYLSEGEK 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 470 TLAD------YVLHAVLVHSGDN-HGGHYVVFINPKADGRWFKFDDDVVSSCRKQEAIEqnyggmddeisFHAKCSNAYM 542
Cdd:cd02257 183 DSDSdngsykYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLE-----------FGSLSSSAYI 251
|
....
gi 665390884 543 LVYI 546
Cdd:cd02257 252 LFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-545 |
1.08e-56 |
|
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: 1.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYFTNSLRLSVYRIPTEADDSSKSVGLS-----------LQRVFHELQFGDR----PVGtkkL 306
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDkphepqtiidqLQLIFAQLQFGNRsvvdPSG---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 307 TKSFGwetLDSFMQHDVQEFLRVLLDKLESKM---KGTILEGTIPGLFEGKMSsYIKCKNVDYNSTRYET-FYDIQLNIK 382
Cdd:cd02668 78 VKALG---LDTGQQQDAQEFSKLFLSLLEAKLsksKNPDLKNIVQDLFRGEYS-YVTQCSKCGRESSLPSkFYELELQLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 383 DKKNIYESFQDYVAPETLEGDNKYDAG-VHGLQEASKGVIFTSFPPVLHLHLMRFQYDPVTDSSIKYNDRFEFYEHINLD 461
Cdd:cd02668 154 GHKTLEECIDEFLKEEQLTGDNQYFCEsCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 462 RYLAESENTLADYVLHAVLVHSGDN-HGGHYVVFINPKADGRWFKFDDDVVS---SCRKQEAIEQNYGGM---DDEISFH 534
Cdd:cd02668 234 EYLAESDEGSYVYELSGVLIHQGVSaYSGHYIAHIKDEQTGEWYKFNDEDVEempGKPLKLGNSEDPAKPrksEIKKGTH 313
|
330
....*....|.
gi 665390884 535 AKcSNAYMLVY 545
Cdd:cd02668 314 SS-RTAYMLVY 323
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-546 |
1.25e-39 |
|
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: 149.35 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYFTNSLrlSVYRIPTEADDSSKSVGL----SLQRVFHELQFGDRPVGTKKLT----KSFgWE 313
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPL--ANYLLSREHSKDCCNEGFcmmcALEAHVERALASSGPGSAPRIFssnlKQI-SK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 314 TLDSFMQHDVQEFLRVLLDKLES--------------KMKGTILEGTIpglFEGKMSSYIKCKNVDYNSTRYETFYDIQL 379
Cdd:cd02661 80 HFRIGRQEDAHEFLRYLLDAMQKacldrfkklkavdpSSQETTLVQQI---FGGYLRSQVKCLNCKHVSNTYDPFLDLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 380 NIKDKKNIYESFQDYVAPETLEGDNKYD-AGVHGLQEASKGVIFTSFPPVLHLHLMRFQYDPvtdsSIKYNDRFEFYEHI 458
Cdd:cd02661 157 DIKGADSLEDALEQFTKPEQLDGENKYKcERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR----GGKINKQISFPETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 459 NLDRYLAESENTLADYVLHAVLVHSG-DNHGGHYVVFINpKADGRWFKFDDDVVSSCRKQEAIEQnyggmddeisfhakc 537
Cdd:cd02661 233 DLSPYMSQPNDGPLKYKLYAVLVHSGfSPHSGHYYCYVK-SSNGKWYNMDDSKVSPVSIETVLSQ--------------- 296
|
....*....
gi 665390884 538 sNAYMLVYI 546
Cdd:cd02661 297 -KAYILFYI 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-546 |
4.17e-36 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 136.65 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLyftnslrlsvyripteaddssksvglslqrvfhelqfgdrpvgtkkltksfgwetldSFMQH 321
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL---------------------------------------------------------SADQQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 322 DVQEFLRVLLDKLESKmkgtilegtIPGLFEGKMSSYIKCKNVDYNSTRYETFYDIQLNIKDKK------NIYESFQDYV 395
Cdd:cd02674 24 DAQEFLLFLLDGLHSI---------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFT 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 396 APETLEGDNK-YDAGVHGLQEASKGVIFTSFPPVLHLHLMRFQYDPVtdSSIKYNDRFEF-YEHINLDRYLAESENT-LA 472
Cdd:cd02674 95 KEETLDGDNAwKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRG--STRKLTTPVTFpLNDLDLTPYVDTRSFTgPF 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665390884 473 DYVLHAVLVHSGDNHGGHYVVFINPKADGRWFKFDDDVVSSCRKQEAIEqnyggmddeisfhakcSNAYMLVYI 546
Cdd:cd02674 173 KYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVS----------------SSAYILFYE 230
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-545 |
5.59e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 138.60 E-value: 5.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYFTNSLRlsvyripteaddssksvglSLQRVFHELQFGDRPVGT-------KKLTKSFgwET 314
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT-------------------CLKDLFESISEQKKRTGVispkkfiTRLKREN--EL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 315 LDSFMQHDVQEFLRVLLDKL------ESKMKGTILEGT-----------IPGLFEGKMSSYIKCKNVDYNSTRYETFYDI 377
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIaeildaERKAEKANRKLNnnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 378 QLNIKDKKNIYESFQDYVAPETLEGDNKYDAGV-HGLQEASKGVIFTSFPPVLHLHLMRFQYDPVTDSSIKYNDRFEFYE 456
Cdd:cd02663 140 SIDVEQNTSITSCLRQFSATETLCGRNKFYCDEcCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 457 HINLDRYLAESENTLADYVLHAVLVH--SGDNHgGHYVVFInpKADGRWFKFDDDVVsscrkqEAIEQNYggMDDEISFH 534
Cdd:cd02663 220 ELRLFNTTDDAENPDRLYELVAVVVHigGGPNH-GHYVSIV--KSHGGWLLFDDETV------EKIDENA--VEEFFGDS 288
|
330
....*....|.
gi 665390884 535 AKCSNAYMLVY 545
Cdd:cd02663 289 PNQATAYVLFY 299
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-546 |
4.90e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 127.87 E-value: 4.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYFTNSLR---LS-VYRIPTEADDSSKSVGLSLQRVFHELQFGDRPVG---TKKLTKSfgW-- 312
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRnyfLSdRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPygpINLLYLS--Wkh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 313 -ETLDSFMQHDVQEFLRVLLDKL-ESKMKGTILEGTIPG-------LFEGKMSSYIKCKNVDYNSTRYETFYDIQLNIKD 383
Cdd:cd02660 80 sRNLAGYSQQDAHEFFQFLLDQLhTHYGGDKNEANDESHcnciihqTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 384 K---------------KNIYESFQDYVAPETLEGDNKYDAGVHGLQEASKGVIFTSFPPVLHLHLMRFQYDpVTDSSIKY 448
Cdd:cd02660 160 KstpswalgesgvsgtPTLSDCLDRFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNKTSRKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 449 NDRFEFYEHINLDRYLAESENTLAD---------YVLHAVLVHSGDNHGGHYVVFINPKaDGRWFKFDDDVVSSCRKQEA 519
Cdd:cd02660 239 DTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEV 317
|
330 340
....*....|....*....|....*..
gi 665390884 520 IEqnyggmddeisfhakcSNAYMLVYI 546
Cdd:cd02660 318 LK----------------SQAYLLFYH 328
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-555 |
5.28e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 126.35 E-value: 5.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYFTNSLRLSVYRIPTEAddssksvgLSLQRVFHElQFGDrpvgtkkltksfgwetldsFMQH 321
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKEL--------FSQVCRKAP-QFKG-------------------YQQQ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 322 DVQEFLRVLLDKLESkmkgtilegTIPGLFEGKMSSYIKCKNVDYNSTRYETFYDIQLNIKDKKNIYESFQD----YVAP 397
Cdd:cd02667 53 DSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSECSIESclkqFTEV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 398 ETLEGDNKYdaGVHGLQEASKGVIFTSFPPVLHLHLMRFQYDPvTDSSIKYNDRFEFYEHINLDRYLAESENTLAD---- 473
Cdd:cd02667 124 EILEGNNKF--ACENCTKAKKQYLISKLPPVLVIHLKRFQQPR-SANLRKVSRHVSFPEILDLAPFCDPKCNSSEDkssv 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 474 -YVLHAVLVHSGDNHGGHYVVFI--NPKADgrwfkfdddvVSSCRKQEAIEQNYGGMDDEISFHAKCSnaymlvYIRQSE 550
Cdd:cd02667 201 lYRLYGVVEHSGTMRSGHYVAYVkvRPPQQ----------RLSDLTKSKPAADEAGPGSGQWYYISDS------DVREVS 264
|
....*
gi 665390884 551 LDRVL 555
Cdd:cd02667 265 LEEVL 269
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-545 |
6.32e-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: 124.91 E-value: 6.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYFTNSLRLSVYRIPTEADDSSKSVGLSLQRVFHELQFGDRPVGTkkltksfgweTLDSFM-- 319
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEA----------PPDYFLea 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 320 ----------QHDVQEFLRVLLDKLESkmkgtilegTIPGLFEGKMSSYIKCKNVDYNSTRYETFYDIQLNikdkkniYE 389
Cdd:cd02664 71 srppwftpgsQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLS-------FP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 390 SFQD----YVAPETLEGDNKYDA-GVHGLQEASKGVIFTSFPPVLHLHLMRFQYDPVTDSSIKYND-------------- 450
Cdd:cd02664 135 SVQDllnyFLSPEKLTGDNQYYCeKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDnvsinevlslpvrv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 451 -----RFEFYEHINLDRYLAESENTLADYVLHAVLVHSG-DNHGGHYVVFI--------------------NPKADGRWF 504
Cdd:cd02664 215 eskssESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGySSESGHYFTYArdqtdadstgqecpepkdaeENDESKNWY 294
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 665390884 505 KFDDDVVSSCRKQEaieqnyggMDDEISFHAKcSNAYMLVY 545
Cdd:cd02664 295 LFNDSRVTFSSFES--------VQNVTSRFPK-DTPYILFY 326
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-545 |
1.41e-27 |
|
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: 114.35 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYFTNSLR--LSVY-RIPTEADDSSKSVGLSLQRVFHELQFGDRPVGTKKLTKSFG-----WE 313
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRdaLKNYnPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRmafpqFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 314 TLDS---FMQHDVQEFLRVLLDKLESKMKGTILEG-TIPGLFEGKMSSYIKCK-NVDYNSTRYETFYDIQLNIKDKKNIY 388
Cdd:cd02657 81 EKQNqggYAQQDAEECWSQLLSVLSQKLPGAGSKGsFIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQCHISITTEVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 389 ESF---------QDYVAPETLEGDNKYdagvhglqeaSKGVIFTSFPPVLHLHLMRFQYDPVTDSSIKYNDRFEFyeHIN 459
Cdd:cd02657 161 YLQdglkkgleeEIEKHSPTLGRDAIY----------TKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKF--PFE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 460 LD--RYLAESENtladYVLHAVLVHSGDN-HGGHYVVFINPKADGRWFKFDDDVVSScRKQEAIEQNYGGMDDEIsfhak 536
Cdd:cd02657 229 LDlyELCTPSGY----YELVAVITHQGRSaDSGHYVAWVRRKNDGKWIKFDDDKVSE-VTEEDILKLSGGGDWHI----- 298
|
....*....
gi 665390884 537 csnAYMLVY 545
Cdd:cd02657 299 ---AYILLY 304
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-545 |
2.70e-23 |
|
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: 100.13 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLyftnslrlsvyripteaddssksvgLSLQRVFhelqfgdrpvgtkkltksfgwETLDSFM-Q 320
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL-------------------------ASLPSLI---------------------EYLEEFLeQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 321 HDVQEFLRVLLDKLESKMKGtilegtipgLFEGKMSSYIKCKNVDYNST-RYETFYDIQLNIKDKKNIYES-----FQDY 394
Cdd:cd02662 35 QDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSGSGTtlehcLDDF 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 395 VAPETLEGDNKYdagvhglqeaSKGVIFTSFPPVLHLHLMRFQYDPvTDSSIKYNDRFEFYEHinLDRYLaesentladY 474
Cdd:cd02662 106 LSTEIIDDYKCD----------RCQTVIVRLPQILCIHLSRSVFDG-RGTSTKNSCKVSFPER--LPKVL---------Y 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 475 VLHAVLVHSGDNHGGHYVVF----INPK----------------ADGRWFKFDDDVVSSCRKQEAIEQnyggmddeisfh 534
Cdd:cd02662 164 RLRAVVVHYGSHSSGHYVCYrrkpLFSKdkepgsfvrmregpssTSHPWWRISDTTVKEVSESEVLEQ------------ 231
|
330
....*....|.
gi 665390884 535 akcSNAYMLVY 545
Cdd:cd02662 232 ---KSAYMLFY 239
|
|
| MATH |
cd00121 |
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ... |
103-222 |
3.72e-21 |
|
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: 90.13 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 103 TFSFTVENVVQLKSQRL-SPPVYVRMLPWRIMVIPNDRA-----LGFFLQC-NGENDSPTWSCNAIAELRLKCHKPDaQP 175
Cdd:cd00121 2 KHTWKIVNFSELEGESIySPPFEVGGYKWRIRIYPNGDGesgdyLSLYLELdKGESDLEKWSVRAEFTLKLVNQNGG-KS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 665390884 176 FTRARIKHLFYSKENDYGYSNFITWQELKDSEksYVHNNSITLEVHV 222
Cdd:cd00121 81 LSKSFTHVFFSEKGSGWGFPKFISWDDLEDSY--YLVDDSLTIEVEV 125
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
222-511 |
8.44e-20 |
|
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: 91.88 E-value: 8.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 222 VVADAPHGVLWDSKKHTG---YVGLKNQGATCYMNSLLQTLYFTNSLRLSVYRIPT--EADDSSKSVGLSLQRVFHELQF 296
Cdd:cd02671 3 VVPAPQPSSATSCEKRENllpFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSliSSVEQLQSSFLLNPEKYNDELA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 297 GDRPVGTKKLTKSFGwETLDSFMQHDVQEFLRVLLDKLESKMKgtilegtipGLFEGKMSSYIKCKNVDYNSTRYETFYD 376
Cdd:cd02671 83 NQAPRRLLNALREVN-PMYEGYLQHDAQEVLQCILGNIQELVE---------KDFQGQLVLRTRCLECETFTERREDFQD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 377 IQLNIK-------------------DKKNIYESFQDYVAPETLEGDNKYDAGV-HGLQEASKGVIFTSFPPVLHLHLMRF 436
Cdd:cd02671 153 ISVPVQeselskseesseispdpktEMKTLKWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKLPEVITIHLKCF 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665390884 437 QYDPVTDSSIKYNDRFEFYEHINLDRYLAE--SENTLADYVLHAVLVHSGDN-HGGHYVVFInpkadgRWFKFDDDVV 511
Cdd:cd02671 233 AANGSEFDCYGGLSKVNTPLLTPLKLSLEEwsTKPKNDVYRLFAVVMHSGATiSSGHYTAYV------RWLLFDDSEV 304
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-523 |
2.36e-18 |
|
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: 87.38 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYFTNS-------LRLSVYRIPTEADDS-----SK----------SVGLSLQRVFHELQFGDR 299
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSfqwryddLENKFPSDVVDPANDlncqlIKladgllsgrySKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 300 PVGTKKLTkSFGWETLDSFMQHDVQEFLRVLLDKLESKMKGTilEGTIPG-LFEGKMSSYIKCKNVDYNSTRYETFYDIQ 378
Cdd:cd02658 81 PSMFKALI-GKGHPEFSTMRQQDALEFLLHLIDKLDRESFKN--LGLNPNdLFKFMIEDRLECLSCKKVKYTSELSEILS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 379 LNIKDKKNIY--------------ESFQDYVAPETLEGdnkYDAGVHGLQEASKGVIFTSFPPVLHLHLMRFQ----YDP 440
Cdd:cd02658 158 LPVPKDEATEkeegelvyepvpleDCLKAYFAPETIED---FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQllenWVP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 441 V-TDSSIKYNDRFefyehinldrylaesenTLADYVLHAVLVHSGDN-HGGHYVVFINPKAD--GRWFKFDDDVVSSCRK 516
Cdd:cd02658 235 KkLDVPIDVPEEL-----------------GPGKYELIAFISHKGTSvHSGHYVAHIKKEIDgeGKWVLFNDEKVVASQD 297
|
....*..
gi 665390884 517 QEAIEQN 523
Cdd:cd02658 298 PPEMKKL 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
242-547 |
1.14e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 84.85 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYFTNSlrlsvyRIPTEADDSSKSVGlSLQRV---------FHELQFGDRPVGTKKLTKsFGW 312
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLP------KLDELLDDLSKELK-VLKNVirkpepdlnQEEALKLFTALWSSKEHK-VGW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 313 ETlDSFMQHDVQEFLRVLLDKLESKMKGTILEGTIPgLFEGKMSSYIKCKNVDYNSTRYETFYDIQLNIKDKKNIYESFQ 392
Cdd:COG5533 73 IP-PMGSQEDAHELLGKLLDELKLDLVNSFTIRIFK-TTKDKKKTSTGDWFDIIIELPDQTWVNNLKTLQEFIDNMEELV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 393 DyVAPETLEGDNKydaGVHGLQEASKGVIFTSFPPVLHLHLMRFQYDpVTDSSIKYNDRFEFYEHINLDRYLAESENTLa 472
Cdd:COG5533 151 D-DETGVKAKENE---ELEVQAKQEYEVSFVKLPKILTIQLKRFANL-GGNQKIDTEVDEKFELPVKHDQILNIVKETY- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665390884 473 dYVLHAVLVHSGDNHGGHYVVFInpKADGRWFKFDDDVVSSCRKQEAIEqnyggMDDEisfhakcsNAYMLVYIR 547
Cdd:COG5533 225 -YDLVGFVLHQGSLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAIN-----EKAK--------NAYLYFYER 283
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-546 |
1.40e-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: 77.21 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 242 GLKNQGATCYMNSLLQTLYftnslrlsvyripteaddssksvglSLQRVFHELqfgdrpvgtkkLTKSFGWETlDSFmqh 321
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLF-------------------------SQQQDVSEF-----------THLLLDWLE-DAF--- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 322 DVQEFLRVLLDKLESKM----KGTILegtIPGLFEGKMSSYIkcknvdynstryETFYDIQLNIKDKKNIYESFQdyvaP 397
Cdd:cd02665 41 QAAAEAISPGEKSKNPMvqlfYGTFL---TEGVLEGKPFCNC------------ETFGQYPLQVNGYGNLHECLE----A 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 398 ETLEGDNKYDAGVHGLQEASKGvIFTSFPPVLHLHLMRFQYDpvTDSSIKYNDRFEFYEHINLdrylaesentlADYVLH 477
Cdd:cd02665 102 AMFEGEVELLPSDHSVKSGQER-WFTELPPVLTFELSRFEFN--QGRPEKIHDKLEFPQIIQQ-----------VPYELH 167
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665390884 478 AVLVHSGDNHGGHYVVFINPKADGRWFKFDDDVVSSCRKQEAIEQNYGGMDDeisfhakcSNAYMLVYI 546
Cdd:cd02665 168 AVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRN--------PSAYCLMYI 228
|
|
| MATH |
pfam00917 |
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ... |
108-222 |
5.59e-15 |
|
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: 71.90 E-value: 5.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 108 VENVVQLK--SQRLSPPVYVRMLPWRIMVIPNDRALGFFLQC-NGENDSPTWSCNaiAELRLKCHKPDAQPFTRaRIKHL 184
Cdd:pfam00917 1 IKNFSKIKegESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCdKEEELERGWSIE--TEFTLKLVSSNGKSVTK-TDTHV 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 665390884 185 FySKENDYGYSNFITWQELkdsEKSYVHNNSITLEVHV 222
Cdd:pfam00917 78 F-EKPKGWGWGKFISWDDL---EKDYLVDDSITVEAHV 111
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-546 |
4.94e-13 |
|
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: 71.75 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 241 VGLKNQGATCYMNSLLQTLYFTNSLR-----------------LSVYRIPTEA-----DDSSKSVGLSLQRVFHELQFGD 298
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRdlvlnfdeskaelasdyPTERRIGGREvsrseLQRSNQFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 299 ----RPvgTKKLTksfgwetLDSFMQHDVQEFLRVLLDKLESKMKGTILEGTIP-------------GLFEGKM-SSYIK 360
Cdd:cd02666 82 trsvTP--SKELA-------YLALRQQDVTECIDNVLFQLEVALEPISNAFAGPdteddkeqsdlikRLFSGKTkQQLVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 361 CKNVDYNSTR--YETFYDIQLNIKDKKNIyesfqdyvAPETLEGDNKYDAgvhgLQEASKGVIFTSFPPVLHLHLmrfQY 438
Cdd:cd02666 153 ESMGNQPSVRtkTERFLSLLVDVGKKGRE--------IVVLLEPKDLYDA----LDRYFDYDSLTKLPQRSQVQA---QL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 439 DPVTDSSIKYNDRFEFYEHIN----LDRYLAESENTLA------------------------DYVLHAVLVHSGDNHGGH 490
Cdd:cd02666 218 AQPLQRELISMDRYELPSSIDdideLIREAIQSESSLVrqaqnelaelkheiekqfddlksyGYRLHAVFIHRGEASSGH 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 665390884 491 YVVFINPKADGRWFKFDDDVVSSCRKQEAIEQNYGGMDdeisfhakcsNAYMLVYI 546
Cdd:cd02666 298 YWVYIKDFEENVWRKYNDETVTVVPASEVFLFTLGNTA----------TPYFLVYV 343
|
|
| MATH |
smart00061 |
meprin and TRAF homology; |
104-198 |
2.35e-12 |
|
meprin and TRAF homology;
Pssm-ID: 214496 [Multi-domain] Cd Length: 95 Bit Score: 63.86 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 104 FSFTVENVVQLK--SQRLSPPVYVRMLPWRIMVIPNDRALGFFLQCN-GENDSPTWSCNAIAELRLKChkPDAQPFTRaR 180
Cdd:smart00061 2 LSHTFKNVSRLEegESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEkEECDSRKWSIEAEFTLKLVS--QNGKSLSK-K 78
|
90
....*....|....*...
gi 665390884 181 IKHLFYsKENDYGYSNFI 198
Cdd:smart00061 79 DKHVFE-KPSGWGFSKFI 95
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
263-549 |
5.91e-11 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 66.83 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 263 NSLRLSVYRIPTEADDSSKSVglslqrvfhelqFGDRPVGTKKLTKSFGWETL-DSFMQHDVQEFLRVLLDKLESKMKGT 341
Cdd:COG5560 538 NGIEVPVVHLRIEKGYKSKRL------------FGDPFLQLNVLIKASIYDKLvKEFEELLVLVEMKKTDVDLVSEQVRL 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 342 ILEGTIPG------------LFEGKMSSYIKCKNV------DYNSTRYETF--YDIQLNIKDKKNIYES------FQDYV 395
Cdd:COG5560 606 LREESSPSswlkleteidtkREEQVEEEGQMNFNDavviscEWEEKRYLSLfsYDPLWTIREIGAAERTitlqdcLNEFS 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 396 APETL-EGDNKYDAGVHGLQEASKGVIFTSFPPVLHLHLMRFQYDpvTDSSIKYNDRFEF-YEHINLDRYLAESENTLAD 473
Cdd:COG5560 686 KPEQLgLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYpIDDLDLSGVEYMVDDPRLI 763
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665390884 474 YVLHAVLVHSGDNHGGHYVVFINPKADGRWFKFDDDVVSSCRKQEAIEqnyggmddeisfhakcSNAYMLVYIRQS 549
Cdd:COG5560 764 YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT----------------SSAYVLFYRRKS 823
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
241-508 |
8.15e-11 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 64.60 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 241 VGLKNQGATCYMNSLLQTLYFTNSLR-LSVYRIPTE-ADDSS-------------KSVGLS-----LQRVF------HEL 294
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRnLALSHLATEcLKEHCllcelgflfdmleKAKGKNcqasnFLRALssipeaSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 295 QFGDRPVGTKKltksfgwETLDSFMqhdVQEFLRVLLDKLES-----KMKGTILEGTIPGLFEGKMSSYIKCKNVDYNST 369
Cdd:pfam13423 81 GLLDEDRETNS-------AISLSSL---IQSFNRFLLDQLSSeenstPPNPSPAESPLEQLFGIDAETTIRCSNCGHESV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 370 RYETFYDIQLN------IKDKKNIYESFQDYVApETLEGDNKYDAGV---HGLQEASKGVIFTSFPPVLHLHLMRFQYDp 440
Cdd:pfam13423 151 RESSTHVLDLIyprkpsSNNKKPPNQTFSSILK-SSLERETTTKAWCekcKRYQPLESRRTVRNLPPVLSLNAALTNEE- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665390884 441 vtDSSIKYNDRF---EFYEHINLDrylAESENTLADYVLHAVLVH-SGDNHGGHYVVFIN-------PKADGRWFKFDD 508
Cdd:pfam13423 229 --WRQLWKTPGWlppEIGLTLSDD---LQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
234-334 |
8.66e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 53.35 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 234 SKKHTGYVGLKNQGATCYMNSLLQTLyfTNSLRLSVYRIPTEADDS-----SKSVGLSLQRVFHEL--QFGDR------P 300
Cdd:COG5560 259 INKEAGTCGLRNLGNTCYMNSALQCL--MHTWELRDYFLSDEYEESineenPLGMHGSVASAYADLikQLYDGnlhaftP 336
|
90 100 110
....*....|....*....|....*....|....
gi 665390884 301 VGTKKLTKSFgWETLDSFMQHDVQEFLRVLLDKL 334
Cdd:COG5560 337 SGFKKTIGSF-NEEFSGYDQQDSQEFIAFLLDGL 369
|
|
| MATH_Ubp21p |
cd03775 |
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ... |
102-222 |
5.71e-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: 43.88 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 102 TTFSFTVENVVQLKSQRLSPPVYVRMLPWRIMVIP----NDRALGFFL-----QCNGENDSPTWSCNAIAELRL-KCHKP 171
Cdd:cd03775 1 QSFTWRIKNWSELEKKVHSPKFKCGGFEWRILLFPqgnsQTGGVSIYLephpeEEEKAPLDEDWSVCAQFALVIsNPGDP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 665390884 172 DAQPFTRARikHLFYSKENDYGYSNFITWQELK----DSEKSYVHNNSITLEVHV 222
Cdd:cd03775 81 SIQLSNVAH--HRFNAEDKDWGFTRFIELRKLAhrtpDKPSPFLENGELNITVYV 133
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
243-521 |
8.01e-04 |
|
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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 42.52 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 243 LKNQGATCYMNSLLQTLYftnslrlSVYRIPTEADDSSksvglslqrvfhelqfgdrpvgtkkltksfgwetldsfmQHD 322
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS-------SIGKINTEFDNDD---------------------------------------QQD 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 323 VQEFLRVLL----DKLESKMKgtiLEGTIPG---------LFEGKMSSYIKCKNVDYNSTRYETFYDIQLNIKDkkNIYE 389
Cdd:cd02673 36 AHEFLLTLLeaidDIMQVNRT---NVPPSNIeikrlnpleAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMID--NKLD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390884 390 SFQDYVAPETLEGDNKYDAGVHGLQEASKGVIFTSFPPVLHLHLMRFQYDPVTDSSIKYNDR-FEFYEHinldrylaese 468
Cdd:cd02673 111 IDELLISNFKTWSPIEKDCSSCKCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEiMKKYCG----------- 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 665390884 469 nTLADYVLHAVLVHSGDN-HGGHYVVFINPKADG-RWFKFDDDVVSSCRKQEAIE 521
Cdd:cd02673 180 -TDAKYSLVAVICHLGESpYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDVST 233
|
|
| |
