|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-417 |
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: 585.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTFLQMWFLNLELRQALYLCPSSEDAAGGGIPKDRDYEPQSICEHLQYLFALLQNSKRRYIDPSGFVKA 169
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 170 LGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQLTD 249
Cdd:cd02668 81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 250 CITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDMEPF-MEQK 328
Cdd:cd02668 161 CIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAESD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 329 NGVYVYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTHCS 408
Cdd:cd02668 241 EGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTHSS 315
|
....*....
gi 1443721010 409 RNAYMLVYR 417
Cdd:cd02668 316 RTAYMLVYK 324
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-416 |
7.29e-62 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 213.07 E-value: 7.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 89 VGLTNLGATCYVNTFLQMWFLNLELRQALYLCPSSedaagggIPKDRDYEPQSICEHLQYLF-ALLQNSKRRYIDPSGFV 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPL-------SEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 168 KALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELE 238
Cdd:pfam00443 74 KSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 239 LNIQGHK------QLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNTY 312
Cdd:pfam00443 150 LPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 313 IGFSELLDMEPFM-----EQKNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEkmegkklqlgiEED 387
Cdd:pfam00443 228 VEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------EVD 295
|
330 340
....*....|....*....|....*....
gi 1443721010 388 LAEPSKSQtrkpkcgkgthcsrNAYMLVY 416
Cdd:pfam00443 296 EETAVLSS--------------SAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-455 |
2.85e-48 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 187.39 E-value: 2.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 72 FHNIDDPNceRRKKNAFVGLTNLGATCYVNTFLQMWFLNLELRQALYlcpssedaaggGIPKDRDYEPQSICEHLQYLFA 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-----------GIPTDHPRGRDSVALALQRLFY 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 152 LLQNSkRRYIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQKQFCGEYAYVTVCNQCGRES 228
Cdd:COG5077 246 NLQTG-EEPVDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNYES 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 229 KLVSKFYELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKK 308
Cdd:COG5077 322 ARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 309 LNTYIGFSELLDMEPFMEQ-----KNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDI---EKMEGKKL 380
Cdd:COG5077 401 INDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVLEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 381 QLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTREK-----APAVEVPAFLQELVERDNCKFEEWCNEMAEMR 455
Cdd:COG5077 480 NFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLDdllnpVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIH 552
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
936-1031 |
1.64e-41 |
|
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: 147.05 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 936 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDTATLGSLGVIPESVILLKADEPIADYAAMD-- 1012
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
|
90
....*....|....*....
gi 1443721010 1013 DVMQVCMPEEGFKGTGLLG 1031
Cdd:cd01795 81 DVSRARVPEEGFKGTALLG 99
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
481-552 |
1.10e-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: 67.01 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 481 GSPYDFISLEWLQKWL----DESTPPKPIDNT--ACLCSHGKLHPDKISIMK--RISEYVADFFYRRYGGGPRLNVKALC 552
Cdd:pfam06337 1 GDKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
477-554 |
5.87e-10 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 56.98 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 477 PAEAGSPYDFISLEWLQKWLD-----ESTPPKPIDNTACLCSHG--KLHPDKI--SIMKRISEYVADFFYRRYGGGPR-L 546
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpI 80
|
....*...
gi 1443721010 547 NVKALCKD 554
Cdd:smart00695 81 PRKVVCQG 88
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
941-999 |
2.14e-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: 43.40 E-value: 2.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443721010 941 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDTaTLGSLGVIPESVILL 999
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
946-999 |
2.83e-04 |
|
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: 40.23 E-value: 2.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1443721010 946 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDTaTLGSLGVIPESVILL 999
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 ... |
90-417 |
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: 585.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTFLQMWFLNLELRQALYLCPSSEDAAGGGIPKDRDYEPQSICEHLQYLFALLQNSKRRYIDPSGFVKA 169
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 170 LGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQLTD 249
Cdd:cd02668 81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 250 CITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDMEPF-MEQK 328
Cdd:cd02668 161 CIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAESD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 329 NGVYVYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTHCS 408
Cdd:cd02668 241 EGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTHSS 315
|
....*....
gi 1443721010 409 RNAYMLVYR 417
Cdd:cd02668 316 RTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
88-417 |
1.10e-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: 266.05 E-value: 1.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 88 FVGLTNLGATCYVNTFLQMWFLNLELRQALYLCPssedaagggiPKDRDYEPQSICEHLQYLFALLQNSKRRYIDPSGFV 167
Cdd:cd02659 2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIP----------PTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 168 KALG-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQ 242
Cdd:cd02659 72 KTRSfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 243 GHKQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDME 322
Cdd:cd02659 149 GKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDME 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 323 PFMEQ------------KNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEKM---EGKKLQLGIEED 387
Cdd:cd02659 229 PYTEKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGEET 307
|
330 340 350
....*....|....*....|....*....|
gi 1443721010 388 LAEPSKSQTRKPKCGkgthcsrNAYMLVYR 417
Cdd:cd02659 308 QKTYDSGPRAFKRTT-------NAYMLFYE 330
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-416 |
7.29e-62 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 213.07 E-value: 7.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 89 VGLTNLGATCYVNTFLQMWFLNLELRQALYLCPSSedaagggIPKDRDYEPQSICEHLQYLF-ALLQNSKRRYIDPSGFV 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPL-------SEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 168 KALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELE 238
Cdd:pfam00443 74 KSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 239 LNIQGHK------QLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNTY 312
Cdd:pfam00443 150 LPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 313 IGFSELLDMEPFM-----EQKNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEkmegkklqlgiEED 387
Cdd:pfam00443 228 VEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------EVD 295
|
330 340
....*....|....*....|....*....
gi 1443721010 388 LAEPSKSQtrkpkcgkgthcsrNAYMLVY 416
Cdd:pfam00443 296 EETAVLSS--------------SAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
90-417 |
1.88e-59 |
|
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: 204.25 E-value: 1.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNtflqmwflnlelrqalylcpssedaagggipkdrdyepqSIcehLQYLFAllqnskrryidpsgfvka 169
Cdd:cd02257 1 GLNNLGNTCYLN---------------------------------------SV---LQALFS------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 170 lgldtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGH 244
Cdd:cd02257 21 ------EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVK 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 245 KQ----LTDCITEFLKEEKLEGDNRYFCEtCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSELLD 320
Cdd:cd02257 95 GLpqvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 321 MEPFMEQK-------NGVYVYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEgkklqlgiEEDLAEPSK 393
Cdd:cd02257 173 LSPYLSEGekdsdsdNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVLEFGS 244
|
330 340
....*....|....*....|....
gi 1443721010 394 SqtrkpkcgkgthcSRNAYMLVYR 417
Cdd:cd02257 245 L-------------SSSAYILFYE 255
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-455 |
2.85e-48 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 187.39 E-value: 2.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 72 FHNIDDPNceRRKKNAFVGLTNLGATCYVNTFLQMWFLNLELRQALYlcpssedaaggGIPKDRDYEPQSICEHLQYLFA 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-----------GIPTDHPRGRDSVALALQRLFY 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 152 LLQNSkRRYIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQKQFCGEYAYVTVCNQCGRES 228
Cdd:COG5077 246 NLQTG-EEPVDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNYES 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 229 KLVSKFYELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKK 308
Cdd:COG5077 322 ARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 309 LNTYIGFSELLDMEPFMEQ-----KNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDI---EKMEGKKL 380
Cdd:COG5077 401 INDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVLEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 381 QLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTREK-----APAVEVPAFLQELVERDNCKFEEWCNEMAEMR 455
Cdd:COG5077 480 NFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLDdllnpVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIH 552
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
176-417 |
9.05e-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: 158.60 E-value: 9.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 176 QQQDAQEFsklfMSLLEDTLskqknpdvRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNI-----QGHKQ-LTD 249
Cdd:cd02674 21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 250 CITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFS-ELLDMEPFM--E 326
Cdd:cd02674 89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPlNDLDLTPYVdtR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 327 QKNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEgkklqlgieedlaepsksqtrkpkcgKGTH 406
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS--------------------------ESSV 219
|
250
....*....|.
gi 1443721010 407 CSRNAYMLVYR 417
Cdd:cd02674 220 VSSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-369 |
1.48e-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: 157.82 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTFLQMWflnlelrqaLYLCPSSEDAAGGGIPKD-RDYEPQSICEHLQYLFALLQNSkRRYIDPSGFVK 168
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCL---------THTPPLANYLLSREHSKDcCNEGFCMMCALEAHVERALASS-GPGSAPRIFSS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 169 AL-----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NIVQKQFCGEYAYVTVCNQCGRESKLVSKFY 235
Cdd:cd02661 73 NLkqiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 236 ELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHkkKLNTYIGF 315
Cdd:cd02661 153 DLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQISF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1443721010 316 SELLDMEPFMEQKNGV-YVYELSAVLIHRGVSAYSGHYIAHVKDPqTGEWYKFND 369
Cdd:cd02661 229 PETLDLSPYMSQPNDGpLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDD 282
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
936-1031 |
1.64e-41 |
|
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: 147.05 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 936 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDTATLGSLGVIPESVILLKADEPIADYAAMD-- 1012
Cdd:cd01795 1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
|
90
....*....|....*....
gi 1443721010 1013 DVMQVCMPEEGFKGTGLLG 1031
Cdd:cd01795 81 DVSRARVPEEGFKGTALLG 99
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-369 |
2.77e-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: 146.10 E-value: 2.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTFLQMWFLNLELR-QALYLCPSSEDaagggipkdrdyEPQSICEHLQYLFALLQNSKRRYIDP-SGFV 167
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRrQVLSLNLPRLG------------DSQSVMKKLQLLQAHLMHTQRRAEAPpDYFL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 168 KAL---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrniVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIqgh 244
Cdd:cd02664 69 EASrppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 245 KQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKL--------------- 309
Cdd:cd02664 134 PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKImdnvsinevlslpvr 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 310 --NTYIGFSELLDMEPFMEQKNGVYV---YELSAVLIHRGVSAYSGHYIAHVKDPQTGE--------------------W 364
Cdd:cd02664 214 veSKSSESPLEKKEEESGDDGELVTRqvhYRLYAVVVHSGYSSESGHYFTYARDQTDADstgqecpepkdaeendesknW 293
|
....*
gi 1443721010 365 YKFND 369
Cdd:cd02664 294 YLFND 298
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-416 |
1.55e-37 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 143.22 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTFLQ-MWFLNLelrqalYLCpssedaagggipkdrdyepqsicehLQYLFALLQNSKRRY--IDPSGF 166
Cdd:cd02663 1 GLENFGNTCYCNSVLQaLYFENL------LTC-------------------------LKDLFESISEQKKRTgvISPKKF 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 167 VKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNIVQKQFCGEYAYVTVCNQCGRE 227
Cdd:cd02663 50 ITRLKrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCETV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 228 SKLVSKFYELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKK 307
Cdd:cd02663 130 SSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 308 KLNTYIGFSelLDMEPFMEQKNGVYV---YELSAVLIHRGVSAYSGHYIAHVKdpQTGEWYKFNDEDIEKMEGKKLqlgi 384
Cdd:cd02663 210 KLFYRVVFP--LELRLFNTTDDAENPdrlYELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAV---- 281
|
330 340 350
....*....|....*....|....*....|..
gi 1443721010 385 eEDLAEPSKSQTrkpkcgkgthcsrNAYMLVY 416
Cdd:cd02663 282 -EEFFGDSPNQA-------------TAYVLFY 299
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-369 |
3.66e-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: 139.82 E-value: 3.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTFLQMwFLNLELRQALYLcpSSEDAAGGGIPKdrdyEPQSICEHLQYLFA-LLQNSKRRyidPSGFVK 168
Cdd:cd02660 2 GLINLGATCFMNVILQA-LLHNPLLRNYFL--SDRHSCTCLSCS----PNSCLSCAMDEIFQeFYYSGDRS---PYGPIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 169 AL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVS 232
Cdd:cd02660 72 LLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 233 KFYELELNIQGHKQ---------------LTDCITEFLKEEKLeGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRF 297
Cdd:cd02660 149 PFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 298 VFDrQTGHKKKLNTYIGFSELLDMEPFM----------EQKNGVYVYELSAVLIHRGvSAYSGHYIAHVKDpQTGEWYKF 367
Cdd:cd02660 228 EHS-LNKTSRKIDTYVQFPLELNMTPYTsssigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQWFKF 304
|
..
gi 1443721010 368 ND 369
Cdd:cd02660 305 DD 306
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-377 |
5.57e-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: 138.62 E-value: 5.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTFLQMWFLNLELRQAL-YLCPSSEDAAGGgipkdrdyePQSICEHLQYLFALLQNSKRRyIDPSGFVK 168
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALkNYNPARRGANQS---------SDNLTNALRDLFDTMDKKQEP-VPPIEFLQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 169 ALGL---------DTGQ--QQDAQE-FSKLFMSLLEDTLSKQKNPDVrniVQKQFCGEYAYVTVC-NQCGRESKLVSKFY 235
Cdd:cd02657 71 LLRMafpqfaekqNQGGyaQQDAEEcWSQLLSVLSQKLPGAGSKGSF---IDQLFGIELETKMKCtESPDEEEVSTESEY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 236 ELELNIqGHKQLTDCITEFLKEeKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGF 315
Cdd:cd02657 148 KLQCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKF 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 316 SELLDMEPFMEQKNgvyVYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFND--------EDIEKMEG 377
Cdd:cd02657 226 PFELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-399 |
1.13e-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: 121.15 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 78 PNCERRKKNA--FVGLTNLGATCYVNTFLQMwflnlelrqaLYLCPSSEDA----AGGGIPKDrdyEPQSICEHLQYLFa 151
Cdd:cd02671 12 ATSCEKRENLlpFVGLNNLGNTCYLNSVLQV----------LYFCPGFKHGlkhlVSLISSVE---QLQSSFLLNPEKY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 152 llqNSKRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNIVQKQFCGEYAYVTVCNQCG- 225
Cdd:cd02671 78 ---NDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLECEt 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 226 ---------------RESKLVSKFYELELNIQGH---KQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLP 287
Cdd:cd02671 143 fterredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 288 CTLNLQLMRF----VFDRQTGHKKKLNTYIGFSELLDMEPFMEqKNGVYVYELSAVLIHRGVSAYSGHYIAHVKdpqtge 363
Cdd:cd02671 223 EVITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR------ 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 1443721010 364 WYKFNDEDIEKMEGKKLqlgieEDLAEPSKSQTRKP 399
Cdd:cd02671 296 WLLFDDSEVKVTEEKDF-----LEALSPNTSSTSTP 326
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-417 |
2.65e-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: 118.64 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTflqmwflnleLRQALYLCPSSEDAAGGGiPKDrdyepqsicehlqyLFALLQNSKRRYIDpsgfvka 169
Cdd:cd02667 1 GLSNLGNTCFFNA----------VMQNLSQTPALRELLSET-PKE--------------LFSQVCRKAPQFKG------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 170 lgldtGQQQDAQEFSKLfmsLLEDtlskqknpdVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELEL----NIQGHK 245
Cdd:cd02667 49 -----YQQQDSHELLRY---LLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSEC 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 246 QLTDCITEFLKEEKLEGDNRYFCETCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNTYIGFSELLDMEPFM 325
Cdd:cd02667 112 SIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAPFC 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 326 EQKNGV------YVYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQTGEWYKFNDEDIEkmegk 378
Cdd:cd02667 188 DPKCNSsedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVR----- 261
|
330 340 350
....*....|....*....|....*....|....*....
gi 1443721010 379 klqlgiEEDLAEPSKSQtrkpkcgkgthcsrnAYMLVYR 417
Cdd:cd02667 262 ------EVSLEEVLKSE---------------AYLLFYE 279
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-370 |
2.09e-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 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: 113.96 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTFLQMWFlNLELRQALYlcpsseDAAGGGIPKDRDYEPQSI-CEHLQYLFALL-------------QN 155
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLF-SIPSFQWRY------DDLENKFPSDVVDPANDLnCQLIKLADGLLsgryskpaslkseND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 156 SKRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNIVQKQFCgeyayvtvCNQCGR 226
Cdd:cd02658 74 PYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CLSCKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 227 ESKLVSKFYELELNIQGHKQ--------------LTDCITEFLKEEKLEgdnrYFCETCQSKQNATRKIRLLSLPCTLNL 292
Cdd:cd02658 146 VKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 293 QLMRFVFDrQTGHKKKLNTYIGFSELLDMEPfmeqkngvyvYELSAVLIHRGVSAYSGHYIAHVK--DPQTGEWYKFNDE 370
Cdd:cd02658 222 NMKRFQLL-ENWVPKKLDVPIDVPEELGPGK----------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFNDE 290
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-374 |
2.02e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 91.66 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTFLQmwflnlelrqALYLCPSsedaagggipkdrdyepqsICEHLQylfallqnskrRYIdpsgfvka 169
Cdd:cd02662 1 GLVNLGNTCFMNSVLQ----------ALASLPS-------------------LIEYLE-----------EFL-------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 170 lgldtgQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnivqkqFCGEYAYVTVCNQCGRESKL-VSKFYELELNIQGHKQ-- 246
Cdd:cd02662 33 ------EQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSSgs 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 247 ---LTDCITEFLKEEKLEGdnrYFCETCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSELLDmep 323
Cdd:cd02662 95 gttLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP--- 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443721010 324 fmeqkngVYVYELSAVLIHRGvSAYSGHYIAH------VKDPQTGE--------------WYKFNDEDIEK 374
Cdd:cd02662 160 -------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKE 222
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
90-375 |
4.76e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 85.62 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 90 GLTNLGATCYVNTFLQMWFLNLELRQALYLCPSSE-----DAAGGgipkdrDYEPQSICEHLqYLFALLQNSKRRYIDPS 164
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKElkvlkNVIRK------PEPDLNQEEAL-KLFTALWSSKEHKVGWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 165 GfvkalglDTGQQQDAQEFsklfMSLLEDTLskqKNPDVRnivqkqfCGEYAYVTVCNQCGRESK------LVSKFYELE 238
Cdd:COG5533 74 P-------PMGSQEDAHEL----LGKLLDEL---KLDLVN-------SFTIRIFKTTKDKKKTSTgdwfdiIIELPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 239 LNIQGHKQ-LTDCITEFLKEEKL--EGDNRYFCETCQSKQNATRKirllSLPCTLNLQLMRFVFDrqtGHKKKLNTYIGf 315
Cdd:COG5533 133 VNNLKTLQeFIDNMEELVDDETGvkAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANL---GGNQKIDTEVD- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443721010 316 sELLDMEPFMEQKNGV---YVYELSAVLIHRGvSAYSGHYIAHVKdpQTGEWYKFNDEDIEKM 375
Cdd:COG5533 205 -EKFELPVKHDQILNIvkeTYYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
247-374 |
8.05e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 88.79 E-value: 8.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 247 LTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNTYIGFS-ELLDMEPFM 325
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVE 754
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1443721010 326 EQK-NGVYVYELSAVLIHRGVSAySGHYIAHVKDPQTGEWYKFNDEDIEK 374
Cdd:COG5560 755 YMVdDPRLIYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLFDDSRITE 803
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
89-369 |
2.07e-17 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 84.24 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 89 VGLTNLGATCYVNTFLQMWFLNLELRQALYLCPSSEDAagggipkdrdYEPQSICEhLQYLFALLQNSKRRYIDPSGFVK 168
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECL----------KEHCLLCE-LGFLFDMLEKAKGKNCQASNFLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 169 ALG----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNIVQKQFCGEYAYVTVCNQCGRES 228
Cdd:pfam13423 70 ALSsipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGHES 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 229 KLVSKFYELELN------IQGHKQLTDCITEFLKEE-KLEGDNRYFCETCQSKQNATRKIRLLSLPC--TLNLQLMRFVF 299
Cdd:pfam13423 150 VRESSTHVLDLIyprkpsSNNKKPPNQTFSSILKSSlERETTTKAWCEKCKRYQPLESRRTVRNLPPvlSLNAALTNEEW 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443721010 300 DRQTGHKKKLNTYIGfselLDMEPFMEQKNGVYVYELSAVLIHRGVSAYSGHYIAHVK-------DPQTGEWYKFND 369
Cdd:pfam13423 230 RQLWKTPGWLPPEIG----LTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-373 |
3.13e-14 |
|
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: 75.22 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 89 VGLTNLGATCYVNTFLQMWFLNLELRQA-----------LYLCPSSEDAAGGGIPKDRDYEPQSICEHLQYLFALLQNSK 157
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnfdeskaelASDYPTERRIGGREVSRSELQRSNQFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 158 RRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNIVQKQFCGEY----AYVTVCNQ 223
Cdd:cd02666 82 TRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTkqqlVPESMGNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 224 CGRESK-------LV-SKFYELELNIQGHKQ-LTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKI---------RLLS 285
Cdd:cd02666 159 PSVRTKterflslLVdVGKKGREIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 286 LPCTLNLQLMRFVFDRQTGHKKKLNTYigfseLLDMEP-FMEQKNgvYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEW 364
Cdd:cd02666 239 DIDELIREAIQSESSLVRQAQNELAEL-----KHEIEKqFDDLKS--YGYRLHAVFIHRG-EASSGHYWVYIKDFEENVW 310
|
....*....
gi 1443721010 365 YKFNDEDIE 373
Cdd:cd02666 311 RKYNDETVT 319
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
176-416 |
6.33e-14 |
|
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: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 176 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVRNivqkqFCGEYAYVTVCNqcGRESKLVSKFYELELNIQGHK 245
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMVQL-----FYGTFLTEGVLE--GKPFCNCETFGQYPLQVNGYG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 246 QLTDCITEFLKEEKLEGDnryfcETCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFSELLDMEPfm 325
Cdd:cd02665 94 NLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVP-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 326 eqkngvyvYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKlqlgIEEDlaepsksqtrkpkcGKGT 405
Cdd:cd02665 164 --------YELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEE----VERD--------------SFGG 216
|
250
....*....|.
gi 1443721010 406 HCSRNAYMLVY 416
Cdd:cd02665 217 GRNPSAYCLMY 227
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
481-552 |
1.10e-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: 67.01 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 481 GSPYDFISLEWLQKWL----DESTPPKPIDNT--ACLCSHGKLHPDKISIMK--RISEYVADFFYRRYGGGPRLNVKALC 552
Cdd:pfam06337 1 GDKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-376 |
5.79e-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: 69.27 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 86 NAFVGLTNLGATCYVNTFLQMWFLNLELRQALYLCPSSEDAAGggipkdrdyepqsICEHLQYLFALL----QNSK--RR 159
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKD-------------RKSELVKRLSELirkiWNPRnfKG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 160 YIDPSGFVKALGL------DTGQQQDAQEFsklfMSLLEDTLSKQ---KNPDVRNIVQKQFCGEY-----AYVTVCNQCG 225
Cdd:cd02669 184 HVSPHELLQAVSKvskkkfSITEQSDPVEF----LSWLLNTLHKDlggSKKPNSSIIHDCFQGKVqietqKIKPHAEEEG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 226 RESKL----------VSKFYELELNIQG-----HKQLTDCITEFLKEEKLegdNRYFCETCQSKQNATRKIRLLSLPCTL 290
Cdd:cd02669 260 SKDKFfkdsrvkktsVSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 291 NLQLMRFvfDRQTGHKKKLNTYIGFS-ELLDMEPFMEQ---KNGVYV-YELSAVLIHRGVSAYSGHYIAHVKDPQTGEWY 365
Cdd:cd02669 337 IFHIKRF--SKNNFFKEKNPTIVNFPiKNLDLSDYVHFdkpSLNLSTkYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWF 414
|
330
....*....|.
gi 1443721010 366 KFNDEDIEKME 376
Cdd:cd02669 415 EIQDLNVKEVL 425
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
171-372 |
5.35e-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: 61.01 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 171 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNIVQKQFCGEYAYVT----VCNQCGRESKLVSKFYELELNIQG 243
Cdd:cd02673 27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 244 HK--QLTDCITEFLKEEKLEGDnryfCETCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIgfselldM 321
Cdd:cd02673 107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1443721010 322 EPFMEQKNGvyvYELSAVLIHRGVSAYSGHYIAHVKDPQTG-EWYKFNDEDI 372
Cdd:cd02673 175 KKYCGTDAK---YSLVAVICHLGESPYDGHYIAYTKELYNGsSWLYCSDDEI 223
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
477-554 |
5.87e-10 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 56.98 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 477 PAEAGSPYDFISLEWLQKWLD-----ESTPPKPIDNTACLCSHG--KLHPDKI--SIMKRISEYVADFFYRRYGGGPR-L 546
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpI 80
|
....*...
gi 1443721010 547 NVKALCKD 554
Cdd:smart00695 81 PRKVVCQG 88
|
|
| Ubl_ubiquitin_like |
cd17039 |
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
946-999 |
7.45e-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: 47.21 E-value: 7.45e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1443721010 946 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDTaTLGSLGVIPESVILL 999
Cdd:cd17039 15 VDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK-TLSDYGIKDGSTIHL 67
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
75-369 |
6.93e-06 |
|
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: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 75 IDDPNCERRKKNAFVGLTNLGATCYVNTFLQMWFLNLELRQALYLcpssedaagggIPKDRDYEPQSICEhLQYLFALLq 154
Cdd:cd02672 2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAI-----------ILVACPKESCLLCE-LGYLFSTL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 155 nskrryidpsgfvkalgldtgqqqdAQEFSKLFmslLEDTLSKQKNPDvrnivqkqfcgeyayvtvcNQCGRESKLVSKF 234
Cdd:cd02672 69 -------------------------IQNFTRFL---LETISQDQLGTP-------------------FSCGTSRNSVSLL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443721010 235 YELELNIQGHKQLTD-----CITEFLKEEKlegDNRYFCETCQSKQNATRKIRLLSLPCTLNLQL---MRFV------FD 300
Cdd:cd02672 102 YTLSLPLGSTKTSKEstflqLLKRSLDLEK---VTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLvinLSVTngefddIN 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443721010 301 RQTGHKKKLNTYIGFSELLDMEPFMEQKN-GVYVYELSAVLIHRGVSAYSGHYIAHVKDPQT----GEWYKFND 369
Cdd:cd02672 179 VVLPSGKVMQNKVSPKAIDHDKLVKNRGQeSIYKYELVGYVCEINDSSRGQHNVVFVIKVNEesthGRWYLFND 252
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
941-999 |
2.14e-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: 43.40 E-value: 2.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443721010 941 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDTaTLGSLGVIPESVILL 999
Cdd:smart00213 12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
946-999 |
2.83e-04 |
|
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: 40.23 E-value: 2.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1443721010 946 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDTaTLGSLGVIPESVILL 999
Cdd:pfam00240 15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQ-TLGEYGIEDGSTIHL 67
|
|
| Ubl_Ddi1_like |
cd01796 |
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ... |
946-1000 |
3.26e-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: 40.23 E-value: 3.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1443721010 946 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDTATLGSLGVIPESVILLK 1000
Cdd:cd01796 18 VSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDDKKTLEALGLKDGDLLLLR 72
|
|
| Ubl_AtNPL4_like |
cd17055 |
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ... |
934-991 |
5.22e-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: 39.51 E-value: 5.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443721010 934 RHRKvrGEKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGK---ILSDDTATLGSLGV 991
Cdd:cd17055 6 RSRD--GTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLSLDPGpdlLTAKSSATLSQLGL 64
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