|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-414 |
0e+00 |
|
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: 586.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQMWFLNLELRQALYLCPSAC---GDGIPKDTDYEPQTICEHLQYLFALLQNSKRRYIDPSGFVKA 166
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEdaeLKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 167 LGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQLTD 246
Cdd:cd02668 81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 247 CITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDMEPF-MEQK 325
Cdd:cd02668 161 CIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAESD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 326 NGVYMYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTHCS 405
Cdd:cd02668 241 EGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTHSS 315
|
....*....
gi 1707491019 406 RNAYMLVYR 414
Cdd:cd02668 316 RTAYMLVYK 324
|
|
| Rap_GAP |
pfam02145 |
Rap/ran-GAP; |
1216-1395 |
2.06e-83 |
|
Rap/ran-GAP;
Pssm-ID: 460463 Cd Length: 179 Bit Score: 270.92 E-value: 2.06e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 1216 FGTTEESPAFTEFLDVLGQRVQLRDFKGFRGGLDVTHGQTGSESVYCHFRDKEIMFHVSTKLPYTEGDAQQLQRKRHIGN 1295
Cdd:pfam02145 1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 1296 DIVAVVFQDENTPFVPDMIASNFLHAFVVVQLEQGGAQGTLYKVSVTARDDVPFFGPPLPDPAVFRKG--PEFQEFLltk 1373
Cdd:pfam02145 81 DIVNIVFNESGGPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDnlPEFVRFL--- 157
|
170 180
....*....|....*....|..
gi 1707491019 1374 LINAEYACYRAEKFAKLEERTR 1395
Cdd:pfam02145 158 AINAERAALKSSSFAERLRRIR 179
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-413 |
3.60e-63 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 218.08 E-value: 3.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 89 VGLTNLGATCYVNTFLQMWFLNLELRQALYLCPSACGDGIPKDTDYepqtICEHLQYLF-ALLQNSKRRYIDPSGFVKAL 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN----LLCALRDLFkALQKNSKSSSVSPKMFKKSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 168 G-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNI 238
Cdd:pfam00443 77 GklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 239 QGHK------QLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNTYIGF 312
Cdd:pfam00443 153 PGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 313 SELLDMEPFM-----EQKNGVYMYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEkmegkklqlgiEEDLAE 387
Cdd:pfam00443 231 PLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------EVDEET 298
|
330 340
....*....|....*....|....*.
gi 1707491019 388 PSKSQtrkpkcgkgthcsrNAYMLVY 413
Cdd:pfam00443 299 AVLSS--------------SAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-452 |
6.07e-47 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 184.69 E-value: 6.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 72 FHNIDDPNceRRKKNAFVGLTNLGATCYVNTFLQMWFLNLELRQALYlcpsacgdGIPKDTDYEPQTICEHLQYLFALLQ 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY--------GIPTDHPRGRDSVALALQRLFYNLQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 152 NSkRRYIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQKQFCGEYAYVTVCNQCGRESKLV 228
Cdd:COG5077 249 TG-EEPVDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNYESARV 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 229 SKFYELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNT 308
Cdd:COG5077 325 EDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKIND 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 309 YIGFSELLDMEPFMEQ-----KNGVYMYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDI---EKMEGKKLQLG 380
Cdd:COG5077 404 RYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVLEENFG 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707491019 381 IEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQAREKSL-----TVQVPAFLQELVERDNCKFEEWCNEMAEMR 452
Cdd:COG5077 483 GDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLDDLlnpvaAVDIPPHVEEVLSEEIDKTEVRCKEIDEIH 552
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
935-1012 |
5.30e-31 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.
Pssm-ID: 340493 [Multi-domain] Cd Length: 99 Bit Score: 117.77 E-value: 5.30e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707491019 935 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSLDGKILSDDTATLGSLGVIPESVILLKADEPIADYAAMDD 1012
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADE 79
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
478-549 |
1.31e-13 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 67.39 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 478 GSPYDFISLEWLQKWL----DESTPPKPIDNT--ACLCSHGKLHPDKISLMK--RISEYVADYFYRRYGGGPRLNVKALC 549
Cdd:pfam06337 1 GDKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
474-551 |
2.06e-09 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 55.83 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 474 PAEAGSPYDFISLEWLQKWLD-----ESTPPKPIDNTACLCSHG--KLHPDKI--SLMKRISEYVADYFYRRYGGGPR-L 543
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpI 80
|
....*...
gi 1707491019 544 NVKALCKD 551
Cdd:smart00695 81 PRKVVCQG 88
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
940-998 |
1.15e-05 |
|
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression
Pssm-ID: 214563 [Multi-domain] Cd Length: 72 Bit Score: 44.56 E-value: 1.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1707491019 940 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSLDGKILSDDTaTLGSLGVIPESVILL 998
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
945-998 |
6.22e-05 |
|
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.
Pssm-ID: 459726 [Multi-domain] Cd Length: 72 Bit Score: 42.54 E-value: 6.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1707491019 945 VSANQTLKELKIQIMHAFSVAPFDQNLSLDGKILSDDTaTLGSLGVIPESVILL 998
Cdd:pfam00240 15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQ-TLGEYGIEDGSTIHL 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-414 |
0e+00 |
|
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: 586.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQMWFLNLELRQALYLCPSAC---GDGIPKDTDYEPQTICEHLQYLFALLQNSKRRYIDPSGFVKA 166
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEdaeLKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 167 LGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQLTD 246
Cdd:cd02668 81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 247 CITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDMEPF-MEQK 325
Cdd:cd02668 161 CIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAESD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 326 NGVYMYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTHCS 405
Cdd:cd02668 241 EGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTHSS 315
|
....*....
gi 1707491019 406 RNAYMLVYR 414
Cdd:cd02668 316 RTAYMLVYK 324
|
|
| Rap_GAP |
pfam02145 |
Rap/ran-GAP; |
1216-1395 |
2.06e-83 |
|
Rap/ran-GAP;
Pssm-ID: 460463 Cd Length: 179 Bit Score: 270.92 E-value: 2.06e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 1216 FGTTEESPAFTEFLDVLGQRVQLRDFKGFRGGLDVTHGQTGSESVYCHFRDKEIMFHVSTKLPYTEGDAQQLQRKRHIGN 1295
Cdd:pfam02145 1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 1296 DIVAVVFQDENTPFVPDMIASNFLHAFVVVQLEQGGAQGTLYKVSVTARDDVPFFGPPLPDPAVFRKG--PEFQEFLltk 1373
Cdd:pfam02145 81 DIVNIVFNESGGPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDnlPEFVRFL--- 157
|
170 180
....*....|....*....|..
gi 1707491019 1374 LINAEYACYRAEKFAKLEERTR 1395
Cdd:pfam02145 158 AINAERAALKSSSFAERLRRIR 179
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
88-414 |
1.14e-80 |
|
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: 269.51 E-value: 1.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 88 FVGLTNLGATCYVNTFLQMWFLNLELRQALYLCPSAcgdgipKDTDYEPQTICeHLQYLFALLQNSKRRYIDPSGFVKAL 167
Cdd:cd02659 2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT------EDDDDNKSVPL-ALQRLFLFLQLSESPVKTTELTDKTR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 168 G-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHK 242
Cdd:cd02659 75 SfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 243 QLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDMEPFM 322
Cdd:cd02659 152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 323 EQ------------KNGVYMYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEKM---EGKKLQLGIEEDLAE 387
Cdd:cd02659 232 EKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGEETQKT 310
|
330 340
....*....|....*....|....*..
gi 1707491019 388 PSKSQTRKPKCGkgthcsrNAYMLVYR 414
Cdd:cd02659 311 YDSGPRAFKRTT-------NAYMLFYE 330
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-413 |
3.60e-63 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 218.08 E-value: 3.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 89 VGLTNLGATCYVNTFLQMWFLNLELRQALYLCPSACGDGIPKDTDYepqtICEHLQYLF-ALLQNSKRRYIDPSGFVKAL 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN----LLCALRDLFkALQKNSKSSSVSPKMFKKSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 168 G-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNI 238
Cdd:pfam00443 77 GklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 239 QGHK------QLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNTYIGF 312
Cdd:pfam00443 153 PGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 313 SELLDMEPFM-----EQKNGVYMYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEkmegkklqlgiEEDLAE 387
Cdd:pfam00443 231 PLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------EVDEET 298
|
330 340
....*....|....*....|....*.
gi 1707491019 388 PSKSQtrkpkcgkgthcsrNAYMLVY 413
Cdd:pfam00443 299 AVLSS--------------SAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
90-414 |
1.59e-60 |
|
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: 1.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQmwflnlelrqalylcpsacgdgipkdtdyepqticehlqYLFAllqnskrryidpsgfvkalgl 169
Cdd:cd02257 1 GLNNLGNTCYLNSVLQ---------------------------------------ALFS--------------------- 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 170 dtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQ- 243
Cdd:cd02257 21 ---EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGLp 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 244 ---LTDCITEFLKEEKLEGDNRYFCEtCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSELLDMEP 320
Cdd:cd02257 98 qvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELDLSP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 321 FMEQK-------NGVYMYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEgkklqlgiEEDLAEPSKSqt 393
Cdd:cd02257 176 YLSEGekdsdsdNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVLEFGSL-- 245
|
330 340
....*....|....*....|.
gi 1707491019 394 rkpkcgkgthcSRNAYMLVYR 414
Cdd:cd02257 246 -----------SSSAYILFYE 255
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-452 |
6.07e-47 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 184.69 E-value: 6.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 72 FHNIDDPNceRRKKNAFVGLTNLGATCYVNTFLQMWFLNLELRQALYlcpsacgdGIPKDTDYEPQTICEHLQYLFALLQ 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY--------GIPTDHPRGRDSVALALQRLFYNLQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 152 NSkRRYIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQKQFCGEYAYVTVCNQCGRESKLV 228
Cdd:COG5077 249 TG-EEPVDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNYESARV 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 229 SKFYELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNT 308
Cdd:COG5077 325 EDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKIND 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 309 YIGFSELLDMEPFMEQ-----KNGVYMYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDI---EKMEGKKLQLG 380
Cdd:COG5077 404 RYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVLEENFG 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707491019 381 IEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQAREKSL-----TVQVPAFLQELVERDNCKFEEWCNEMAEMR 452
Cdd:COG5077 483 GDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLDDLlnpvaAVDIPPHVEEVLSEEIDKTEVRCKEIDEIH 552
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
173-414 |
4.27e-44 |
|
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: 160.15 E-value: 4.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 173 QQQDAQEFsklfMSLLEDTLskqknpdvRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNI-----QGHKQ-LTD 246
Cdd:cd02674 21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 247 CITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGhkKKLNTYIGFS-ELLDMEPFM--E 323
Cdd:cd02674 89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGST--RKLTTPVTFPlNDLDLTPYVdtR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 324 QKNGVYMYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEgkklqlgieedlaepsksqtrkpkcgKGTH 403
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS--------------------------ESSV 219
|
250
....*....|.
gi 1707491019 404 CSRNAYMLVYR 414
Cdd:cd02674 220 VSSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-413 |
3.94e-42 |
|
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: 157.05 E-value: 3.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQMwflnleLRQALYLCPSACGDGIPKDTDYE-PQTICEHLQYLFALLQNSkRRYIDPSGFVKAL- 167
Cdd:cd02661 3 GLQNLGNTCFLNSVLQC------LTHTPPLANYLLSREHSKDCCNEgFCMMCALEAHVERALASS-GPGSAPRIFSSNLk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 168 ----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELE 235
Cdd:cd02661 76 qiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 236 LNIQGHKQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHkkKLNTYIGFSEL 315
Cdd:cd02661 156 LDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQISFPET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 316 LDMEPFMEQKNGV-YMYELSAVLIHRGVSAYSGHYIAHVKDPqTGEWYKFNDEDIEKMEgkklqlgiEEDLaepsksqtr 394
Cdd:cd02661 232 LDLSPYMSQPNDGpLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDDSKVSPVS--------IETV--------- 293
|
330
....*....|....*....
gi 1707491019 395 kpkcgkgthCSRNAYMLVY 413
Cdd:cd02661 294 ---------LSQKAYILFY 303
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-413 |
2.75e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 149.00 E-value: 2.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQmwflnlelrqALYlcpsacgdgipkdtdYEpqTICEHLQYLFALLQNSKRRY--IDPSGFVKAL 167
Cdd:cd02663 1 GLENFGNTCYCNSVLQ----------ALY---------------FE--NLLTCLKDLFESISEQKKRTgvISPKKFITRL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 168 G-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNIVQKQFCGEYAYVTVCNQCGRESKLV 228
Cdd:cd02663 54 KrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCETVSSRD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 229 SKFYELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNT 308
Cdd:cd02663 134 ETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 309 YIGFSelLDMEPFMEQKNGVY---MYELSAVLIHRGVSAYSGHYIAHVKdpQTGEWYKFNDEDIEKMEGKKLqlgieEDL 385
Cdd:cd02663 214 RVVFP--LELRLFNTTDDAENpdrLYELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAV-----EEF 284
|
330 340
....*....|....*....|....*...
gi 1707491019 386 AEPSKSQTrkpkcgkgthcsrNAYMLVY 413
Cdd:cd02663 285 FGDSPNQA-------------TAYVLFY 299
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-366 |
2.79e-38 |
|
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: 146.87 E-value: 2.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQMWFLNLELR-QALYLCPSACGDGipkdtdyepQTICEHLQYLFALLQNSKRRYIDP-SGFVKAL 167
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRrQVLSLNLPRLGDS---------QSVMKKLQLLQAHLMHTQRRAEAPpDYFLEAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 168 ---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrniVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIqghKQL 244
Cdd:cd02664 72 rppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF---PSV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 245 TDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDMEPFMEQ 324
Cdd:cd02664 137 QDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVES 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 325 KNGVYM--------------------YELSAVLIHRGVSAYSGHYIAHVKDPQTGE--------------------WYKF 364
Cdd:cd02664 217 KSSESPlekkeeesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQTDADstgqecpepkdaeendesknWYLF 296
|
..
gi 1707491019 365 ND 366
Cdd:cd02664 297 ND 298
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-366 |
1.36e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 141.74 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQMwFLNLELRQALYL----CPSACGDGIPKdtdyepqTICEHLQYLFA-LLQNSKRRyidPSGFV 164
Cdd:cd02660 2 GLINLGATCFMNVILQA-LLHNPLLRNYFLsdrhSCTCLSCSPNS-------CLSCAMDEIFQeFYYSGDRS---PYGPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 165 KAL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLV 228
Cdd:cd02660 71 NLLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 229 SKFYELELNIQGHKQ---------------LTDCITEFLKEEKLeGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMR 293
Cdd:cd02660 148 DPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 294 FVFDrQTGHKKKLNTYIGFSELLDMEPFMEQKNGVYM----------YELSAVLIHRGvSAYSGHYIAHVKDpQTGEWYK 363
Cdd:cd02660 227 FEHS-LNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQdsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQWFK 303
|
...
gi 1707491019 364 FND 366
Cdd:cd02660 304 FDD 306
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-374 |
8.28e-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 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: 139.00 E-value: 8.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQMWFLNLELRQAL--YlcpsacgDGIPKDTDYEPQTICEHLQYLFALLQNSKRRyIDPSGFVKAL 167
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknY-------NPARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 168 GL---------DTGQ--QQDAQE-FSKLFMSLLEDTLSKQKNPDVrniVQKQFCGEYAYVTVC-NQCGRESKLVSKFYEL 234
Cdd:cd02657 73 RMafpqfaekqNQGGyaQQDAEEcWSQLLSVLSQKLPGAGSKGSF---IDQLFGIELETKMKCtESPDEEEVSTESEYKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 235 ELNIqGHKQLTDCITEFLKEeKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSE 314
Cdd:cd02657 150 QCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPF 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707491019 315 LLDMEPFMEQKNgvyMYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFND--------EDIEKMEG 374
Cdd:cd02657 228 ELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
935-1012 |
5.30e-31 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.
Pssm-ID: 340493 [Multi-domain] Cd Length: 99 Bit Score: 117.77 E-value: 5.30e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707491019 935 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSLDGKILSDDTATLGSLGVIPESVILLKADEPIADYAAMDD 1012
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADE 79
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-414 |
2.46e-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: 119.41 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTflqmwflnleLRQALYLCPSacgdgipkdtdyepqtICEHLQYLFALLQNSKRRyidpsgfvKALGL 169
Cdd:cd02667 1 GLSNLGNTCFFNA----------VMQNLSQTPA----------------LRELLSETPKELFSQVCR--------KAPQF 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 170 DTGQQQDAQEfskLFMSLLEDtlskqknpdVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELEL----NIQGHKQLT 245
Cdd:cd02667 47 KGYQQQDSHE---LLRYLLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSIE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 246 DCITEFLKEEKLEGDNRYFCETCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNTYIGFSELLDMEPFMEQK 325
Cdd:cd02667 115 SCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAPFCDPK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 326 NGV------YMYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQTGEWYKFNDEDIEkmegkklq 378
Cdd:cd02667 191 CNSsedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVR-------- 261
|
330 340 350
....*....|....*....|....*....|....*.
gi 1707491019 379 lgiEEDLAEPSKSQtrkpkcgkgthcsrnAYMLVYR 414
Cdd:cd02667 262 ---EVSLEEVLKSE---------------AYLLFYE 279
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-396 |
3.91e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 120.38 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 78 PNCERRKKNA--FVGLTNLGATCYVNTFLQMwflnlelrqaLYLCP-------SACGDGIPKdtdyepqticEHLQYLFA 148
Cdd:cd02671 12 ATSCEKRENLlpFVGLNNLGNTCYLNSVLQV----------LYFCPgfkhglkHLVSLISSV----------EQLQSSFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 149 LLQ---NSKRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNIVQKQFCGEYAYVTVCNQ 220
Cdd:cd02671 72 LNPekyNDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 221 CG----------------RESKLVSKFYELELNIQGH---KQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLL 281
Cdd:cd02671 140 CEtfterredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 282 SLPCTLNLQLMRF----VFDRQTGHKKKLNTYIGFSELLDMEPFMEqKNGVYMYELSAVLIHRGVSAYSGHYIAHVKdpq 357
Cdd:cd02671 220 KLPEVITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR--- 295
|
330 340 350
....*....|....*....|....*....|....*....
gi 1707491019 358 tgeWYKFNDEDIEKMEGKKLqlgieEDLAEPSKSQTRKP 396
Cdd:cd02671 296 ---WLLFDDSEVKVTEEKDF-----LEALSPNTSSTSTP 326
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-367 |
5.25e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 116.27 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQMWFlNLELRQALYlcpsacgDGIPKDTDYEPQTICEHLQYLFALL------------------Q 151
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLF-SIPSFQWRY-------DDLENKFPSDVVDPANDLNCQLIKLadgllsgryskpaslkseN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 152 NSKRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNIVQKQFCgeyayvtvCNQCG 222
Cdd:cd02658 73 DPYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CLSCK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 223 RESKLVSKFYELELNIQGHKQ--------------LTDCITEFLKEEKLEgdnrYFCETCQSKQNATRKIRLLSLPCTLN 288
Cdd:cd02658 145 KVKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 289 LQLMRFVFDrQTGHKKKLNTYIGFSELLDMEPfmeqkngvymYELSAVLIHRGVSAYSGHYIAHVK--DPQTGEWYKFND 366
Cdd:cd02658 221 INMKRFQLL-ENWVPKKLDVPIDVPEELGPGK----------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFND 289
|
.
gi 1707491019 367 E 367
Cdd:cd02658 290 E 290
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
1.23e-21 |
|
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: 95.90 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQmwflnlelrqALYLCPSacgdgipkdtdyepqtICEHLQylfallqnskrRYIdpsgfvkalgl 169
Cdd:cd02662 1 GLVNLGNTCFMNSVLQ----------ALASLPS----------------LIEYLE-----------EFL----------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 170 dtgQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnivqkqFCGEYAYVTVCNQCGRESKL-VSKFYELELNIQGHKQ----- 243
Cdd:cd02662 33 ---EQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSSgsgtt 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 244 LTDCITEFLKEEKLEGdnrYFCETCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSELLDmepfme 323
Cdd:cd02662 98 LEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP------ 159
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707491019 324 qkngVYMYELSAVLIHRGvSAYSGHYIAH------VKDPQTGE--------------WYKFNDEDIEK 371
Cdd:cd02662 160 ----KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKE 222
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
90-372 |
1.63e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 87.94 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 90 GLTNLGATCYVNTFLQMWFLNLELRQALYLCPS----ACGDGIPKDtdYEPQTICEHLqYLFALLQNSKRRYIDPSGfvk 165
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSkelkVLKNVIRKP--EPDLNQEEAL-KLFTALWSSKEHKVGWIP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 166 alglDTGQQQDAQEFsklfMSLLEDTLskqKNPDVRnivqkqfCGEYAYVTVCNQCGRESK------LVSKFYELELNIQ 239
Cdd:COG5533 75 ----PMGSQEDAHEL----LGKLLDEL---KLDLVN-------SFTIRIFKTTKDKKKTSTgdwfdiIIELPDQTWVNNL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 240 GHKQ-LTDCITEFLKEEKL--EGDNRYFCETCQSKQNATRKirllSLPCTLNLQLMRFVFDrqtGHKKKLNTYIGfsELL 316
Cdd:COG5533 137 KTLQeFIDNMEELVDDETGvkAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANL---GGNQKIDTEVD--EKF 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1707491019 317 DMEPFMEQKNGVYM---YELSAVLIHRGvSAYSGHYIAHVKdpQTGEWYKFNDEDIEKM 372
Cdd:COG5533 208 ELPVKHDQILNIVKetyYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
89-366 |
3.57e-18 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 87.33 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 89 VGLTNLGATCYVNTFLQMWFLNLELRQALYLCpsacgdgIPKDTDYEPQTICEhLQYLFALLQNSKRRYIDPSGFVKALG 168
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSH-------LATECLKEHCLLCE-LGFLFDMLEKAKGKNCQASNFLRALS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 169 ----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNIVQKQFCGEYAYVTVCNQCGRESKLV 228
Cdd:pfam13423 73 sipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGHESVRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 229 SKFYELELN------IQGHKQLTDCITEFLKEE-KLEGDNRYFCETCQSKQNATRKIRLLSLPC--TLNLQLMRFVFDRQ 299
Cdd:pfam13423 153 SSTHVLDLIyprkpsSNNKKPPNQTFSSILKSSlERETTTKAWCEKCKRYQPLESRRTVRNLPPvlSLNAALTNEEWRQL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707491019 300 TGHKKKLNTYIGfselLDMEPFMEQKNGVYMYELSAVLIHRGVSAYSGHYIAHVK-------DPQTGEWYKFND 366
Cdd:pfam13423 233 WKTPGWLPPEIG----LTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
244-371 |
1.00e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 89.56 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 244 LTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNTYIGFS-ELLDMEPFM 322
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVE 754
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1707491019 323 EQKNGVYM-YELSAVLIHRGVSAySGHYIAHVKDPQTGEWYKFNDEDIEK 371
Cdd:COG5560 755 YMVDDPRLiYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLFDDSRITE 803
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
173-413 |
1.07e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 72.21 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 173 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVRNivqkqFCGEYAYVTVCNqcGRESKLVSKFYELELNIQGHK 242
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMVQL-----FYGTFLTEGVLE--GKPFCNCETFGQYPLQVNGYG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 243 QLTDCITEFLKEEKLEGDnryfcETCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFSELLDMEPfm 322
Cdd:cd02665 94 NLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVP-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 323 eqkngvymYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKlqlgIEEDlaepsksqtrkpkcGKGT 402
Cdd:cd02665 164 --------YELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEE----VERD--------------SFGG 216
|
250
....*....|.
gi 1707491019 403 HCSRNAYMLVY 413
Cdd:cd02665 217 GRNPSAYCLMY 227
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
478-549 |
1.31e-13 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 67.39 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 478 GSPYDFISLEWLQKWL----DESTPPKPIDNT--ACLCSHGKLHPDKISLMK--RISEYVADYFYRRYGGGPRLNVKALC 549
Cdd:pfam06337 1 GDKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-370 |
8.99e-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: 71.37 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 89 VGLTNLGATCYVNTFLQMWFLNLELRQALyLCPSACGDGIPKDTDYEP---------------QTICEHLQYLFALLQNS 153
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLV-LNFDESKAELASDYPTERriggrevsrselqrsNQFVYELRSLFNDLIHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 154 KRRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNIVQKQFCGEY----AYVTVCN 219
Cdd:cd02666 81 NTRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTkqqlVPESMGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 220 QCGRESK-------LV-SKFYELELNIQGHKQ-LTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKI---------RLL 281
Cdd:cd02666 158 QPSVRTKterflslLVdVGKKGREIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 282 SLPCTLNLQLMRFVFDRQTGHKKKLNTYigfseLLDMEP-FMEQKNgvYMYELSAVLIHRGvSAYSGHYIAHVKDPQTGE 360
Cdd:cd02666 238 DDIDELIREAIQSESSLVRQAQNELAEL-----KHEIEKqFDDLKS--YGYRLHAVFIHRG-EASSGHYWVYIKDFEENV 309
|
330
....*....|
gi 1707491019 361 WYKFNDEDIE 370
Cdd:cd02666 310 WRKYNDETVT 319
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-373 |
5.08e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 70.04 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 86 NAFVGLTNLGATCYVNTFLQMWFLNLELRQALYLcpsacgdgipKDTDYEPQTICEHLQYLFALLQ----NSK--RRYID 159
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL----------YENYENIKDRKSELVKRLSELIrkiwNPRnfKGHVS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 160 PSGFVKALGL------DTGQQQDAQEFsklfMSLLEDTLSKQ---KNPDVRNIVQKQFCGE-----YAYVTVCNQCGRES 225
Cdd:cd02669 187 PHELLQAVSKvskkkfSITEQSDPVEF----LSWLLNTLHKDlggSKKPNSSIIHDCFQGKvqietQKIKPHAEEEGSKD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 226 KL----------VSKFYELELNIQG-----HKQLTDCITEFLKEEKLegdNRYFCETCQSKQNATRKIRLLSLPCTLNLQ 290
Cdd:cd02669 263 KFfkdsrvkktsVSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYLIFH 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 291 LMRFvfDRQTGHKKKLNTYIGFS-ELLDMEPFMEQ----KNGVYMYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFN 365
Cdd:cd02669 340 IKRF--SKNNFFKEKNPTIVNFPiKNLDLSDYVHFdkpsLNLSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQ 417
|
....*...
gi 1707491019 366 DEDIEKME 373
Cdd:cd02669 418 DLNVKEVL 425
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
168-369 |
1.95e-10 |
|
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: 62.93 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 168 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNIVQKQFCGEYAYVT----VCNQCGRESKLVSKFYELELNIQG 240
Cdd:cd02673 27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 241 HK--QLTDCITEFLKEEKLEGDnryfCETCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIgfselldM 318
Cdd:cd02673 107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1707491019 319 EPFMEQKNGvymYELSAVLIHRGVSAYSGHYIAHVKDPQTG-EWYKFNDEDI 369
Cdd:cd02673 175 KKYCGTDAK---YSLVAVICHLGESPYDGHYIAYTKELYNGsSWLYCSDDEI 223
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
474-551 |
2.06e-09 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 55.83 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 474 PAEAGSPYDFISLEWLQKWLD-----ESTPPKPIDNTACLCSHG--KLHPDKI--SLMKRISEYVADYFYRRYGGGPR-L 543
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpI 80
|
....*...
gi 1707491019 544 NVKALCKD 551
Cdd:smart00695 81 PRKVVCQG 88
|
|
| Ubl_ubiquitin_like |
cd17039 |
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
945-998 |
4.17e-07 |
|
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.
Pssm-ID: 340559 [Multi-domain] Cd Length: 68 Bit Score: 48.75 E-value: 4.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1707491019 945 VSANQTLKELKIQIMHAFSVAPFDQNLSLDGKILSDDTaTLGSLGVIPESVILL 998
Cdd:cd17039 15 VDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK-TLSDYGIKDGSTIHL 67
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
75-366 |
1.05e-05 |
|
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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 49.05 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 75 IDDPNCERRKKNAFVGLTNLGATCYVNTFLQMWFLNLELRQALYLCPSACgdgipkdtDYEPQTICEhLQYLFALLqnsk 154
Cdd:cd02672 2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAIILVAC--------PKESCLLCE-LGYLFSTL---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 155 rryidpsgfvkalgldtgqqqdAQEFSKLFmslLEDTLSKQKNPDvrnivqkqfcgeyayvtvcNQCGRESKLVSKFYEL 234
Cdd:cd02672 69 ----------------------IQNFTRFL---LETISQDQLGTP-------------------FSCGTSRNSVSLLYTL 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707491019 235 ELNIQGHKQLTD-----CITEFLKEEKlegDNRYFCETCQSKQNATRKIRLLSLPCTLNLQL---MRFV------FDRQT 300
Cdd:cd02672 105 SLPLGSTKTSKEstflqLLKRSLDLEK---VTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLvinLSVTngefddINVVL 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1707491019 301 GHKKKLNTYIGFSELLDMEPFMEQKN-GVYMYELSAVLIHRGVSAYSGHYIAHVKDPQT----GEWYKFND 366
Cdd:cd02672 182 PSGKVMQNKVSPKAIDHDKLVKNRGQeSIYKYELVGYVCEINDSSRGQHNVVFVIKVNEesthGRWYLFND 252
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
940-998 |
1.15e-05 |
|
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression
Pssm-ID: 214563 [Multi-domain] Cd Length: 72 Bit Score: 44.56 E-value: 1.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1707491019 940 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSLDGKILSDDTaTLGSLGVIPESVILL 998
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
945-998 |
6.22e-05 |
|
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.
Pssm-ID: 459726 [Multi-domain] Cd Length: 72 Bit Score: 42.54 E-value: 6.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1707491019 945 VSANQTLKELKIQIMHAFSVAPFDQNLSLDGKILSDDTaTLGSLGVIPESVILL 998
Cdd:pfam00240 15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQ-TLGEYGIEDGSTIHL 67
|
|
| Ubl_Ddi1_like |
cd01796 |
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ... |
945-999 |
1.06e-04 |
|
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, including yeast aspartyl protease DNA-damage inducible 1 (Ddi1) and Ddi1-like proteins from vertebrates and other eukaryotes, has been characterized by containing an N-terminal ubiquitin-like (Ubl) domain and a conserved retroviral aspartyl-protease-like domain (RVP) that is important in cell-cycle control. Yeast Ddi1 and many family members also contain a C-terminal ubiquitin-association (UBA) domain, however, Ddi1-like proteins from all vertebrates lack the UBA domain. Ddi1, also termed v-SNARE-master 1 (Vsm1), is an ubiquitin receptor involved in the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as an UBA-Ubl shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also termed transporter regulator RS1 (RS1), which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Ddi1-like proteins play a significant role in cell cycle control, growth control, and trafficking in yeast and may play a crucial role in embryogenesis in higher eukaryotes.
Pssm-ID: 340494 [Multi-domain] Cd Length: 73 Bit Score: 42.16 E-value: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1707491019 945 VSANQTLKELKIQIMHAFSVAPFDQNLSLDGKILSDDTATLGSLGVIPESVILLK 999
Cdd:cd01796 18 VSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDDKKTLEALGLKDGDLLLLR 72
|
|
| Ubl_AtNPL4_like |
cd17055 |
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ... |
933-990 |
3.88e-04 |
|
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins; The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2.
Pssm-ID: 340575 Cd Length: 73 Bit Score: 40.28 E-value: 3.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1707491019 933 RHRKvrGEKALLVSANQTLKELKIQIMHAFSVAPFDQNLSLDGK---ILSDDTATLGSLGV 990
Cdd:cd17055 6 RSRD--GTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLSLDPGpdlLTAKSSATLSQLGL 64
|
|
| |
