|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1660-2057 |
6.34e-144 |
|
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: 451.71 E-value: 6.34e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1660 GFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGAatldgedfsgdsdltggglgqalfsgpasalvsfstsggaedg 1739
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1740 sQDVRKNYHVVILKHVQAIFAHLGHSALQFYVPRglWTHFKLQGEPVNLREQQDAVEFFMSLFESLDEGLKALGHPQLMN 1819
Cdd:cd02659 38 -EDDDDNKSVPLALQRLFLFLQLSESPVKTTELT--DKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1820 ATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRLCVKKLPP 1899
Cdd:cd02659 115 NLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1900 VLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEgevvevGDNCQTIVETTKYELTGIVVHSGQASGGH 1979
Cdd:cd02659 195 VLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKE------GDSEKKDSESYIYELHGVLVHSGDAHGGH 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2046230126 1980 YFSYILSKNPGngkcQWYKFDDGEVTECKMHEDEEmkaQCFGGDYMGEIYDNNlkrmqYRRQKRWWNAYMLFYTRCDQ 2057
Cdd:cd02659 269 YYSYIKDRDDG----KWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYERKSP 334
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
2191-2559 |
1.68e-94 |
|
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.
Pssm-ID: 463438 Cd Length: 407 Bit Score: 313.08 E-value: 1.68e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 2191 PSRLGEYILMAPSPEVRTVFVKLVVFFCH-----FAINDEPLTGYDGA----NLCEQVLISVLRLL---KSEAADYGKHL 2258
Cdd:pfam12030 1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCDPDDLEeewrSLSDSVLEAVVALLdhlWKEFHTHLRSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 2259 PHYFSLFSMYVGLGTREKQQLLRLN-VPLQFIQVALDDGPGPAIKYQYPE------------FSKLHQVVSHLIRCSDVS 2325
Cdd:pfam12030 81 DEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARmlrlvekrrppsYEKLIQLLSVLLRCCDLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 2326 EKCQSSNQNARPLPNpfkdatVTHEDLTPLSTECMDLL--FNRTG---YIKKVIEDTNVGDEGLKLLQYCSWENPHFSRA 2400
Cdd:pfam12030 161 LPPQSINEGAEPLPN------SLPDGPFPLTSEEADLLrpLGRTNgsiFVKKLLEIDQNPEATRKILRFLLWENPELSDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 2401 VLTELLWQCGFAYCHDMRHhTDLLLNILLIDDSWQHHRIHNALNGVAEEREGLLETIQRAKTHYQKRAYQIIKCLTqLFH 2480
Cdd:pfam12030 235 ILKTLLWGIRGAPAHLLRD-PFLRAAIVFCEDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCINCRL-GFD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 2481 KSPIALQMLNTNPtisrhwsiavewlqdelerqrgigcqynsySWSPPAQSNDNTN------------------------ 2536
Cdd:pfam12030 313 KEWFASQVLENIP------------------------------DWAPPLLSYPDSNvrsetedflqeelfshemgpdpqf 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2046230126 2537 -------------------GYMLERSQ---SAKNTWTMAYELCPD 2559
Cdd:pfam12030 363 rlreaarrlgiacleylrgTYVLRRSQverSAVETLQRVIELCPE 407
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1662-2052 |
1.27e-77 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 260.45 E-value: 1.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1662 CGLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGAATLDGEDFSGDsdltggglgqalfsgpasalvsfstsggaedgsq 1741
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1742 dvrknyhvvILKHVQAIFAHLGHSALQFYV-PRGLWTHFKLQGEPVNLREQQDAVEFFMSLFESLDEGLKA---LGHPQL 1817
Cdd:pfam00443 47 ---------LLCALRDLFKALQKNSKSSSVsPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1818 MNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLT------ESLEQYVKGELLEGADAYHCDKCDKKVVTVKR 1891
Cdd:pfam00443 118 ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1892 LCVKKLPPVLAIQLKRFEYDYErvCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVevgdncqtivettKYELTGIVVH 1971
Cdd:pfam00443 198 LKISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-------------DYRLVAVVVH 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1972 SGQASGGHYFSYIlsKNPGNGKcqWYKFDDGEVTECKMHEDEEMkaqcfggdymgeiydnnlkrmqyrrqkrwWNAYMLF 2051
Cdd:pfam00443 263 SGSLSSGHYIAYI--KAYENNR--WYKFDDEKVTEVDEETAVLS-----------------------------SSAYILF 309
|
.
gi 2046230126 2052 Y 2052
Cdd:pfam00443 310 Y 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1788-2052 |
3.10e-55 |
|
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: 193.85 E-value: 3.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1788 LREQQDAVEFFMSLFESLDEGLKALG--------HPQLMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDI----RNH 1855
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSkrtsdsssLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1856 SSLTESLEQYVKGELLEGADAYHCDKCdKKVVTVKRLCVKKLPPVLAIQLKRFEYDyERVCAIKFNDYFEFPRILDMEPY 1935
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1936 TVSGLAKLEGEvvevgdncqtiVETTKYELTGIVVHSGQ-ASGGHYFSYILSKNPGngkcQWYKFDDGEVTECKMHEDEE 2014
Cdd:cd02257 177 LSEGEKDSDSD-----------NGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDG----KWYKFNDDKVTEVSEEEVLE 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 2046230126 2015 MkaqcfggdymgeiydnnlkrmqyrrQKRWWNAYMLFY 2052
Cdd:cd02257 242 F-------------------------GSLSSSAYILFY 254
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1663-2053 |
2.07e-47 |
|
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: 173.76 E-value: 2.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1663 GLKNAGATCYMNSVLQQLYMVPAVRvgilrahgaatldgedfsgdsdltggglgQALFSGPASALVSFSTSGGAEDGSQD 1742
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFR-----------------------------KAVYECNSTEDAELKNMPPDKPHEPQ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1743 VrknyhvvILKHVQAIFAHLGHSALQFYVPRGLWTHFKLqgepvNLREQQDAVEF---FMSLFESLDEGLKALGHPQLMN 1819
Cdd:cd02668 52 T-------IIDQLQLIFAQLQFGNRSVVDPSGFVKALGL-----DTGQQQDAQEFsklFLSLLEAKLSKSKNPDLKNIVQ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1820 ATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRLCVKKLPP 1899
Cdd:cd02668 120 DLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1900 VLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTvsglaklegevveVGDNCQTIVettkYELTGIVVHSGQ-ASGG 1978
Cdd:cd02668 200 TLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYL-------------AESDEGSYV----YELSGVLIHQGVsAYSG 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2046230126 1979 HYFSYIlsKNPGNGKcqWYKFDDGEVteckmhedEEMkaqcfGGDYMGEIYDNNLKRMQYRRQKRWW----NAYMLFYT 2053
Cdd:cd02668 263 HYIAHI--KDEQTGE--WYKFNDEDV--------EEM-----PGKPLKLGNSEDPAKPRKSEIKKGThssrTAYMLVYK 324
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1662-2052 |
4.67e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 163.60 E-value: 4.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1662 CGLKNAGATCYMNSVLQQL-YMVPavrvgilrahGAATLDGEDFSGDSDLTGGGLGQALfsgpasalvsfstsggaedgs 1740
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLtHTPP----------LANYLLSREHSKDCCNEGFCMMCAL--------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1741 qdvrknyhvviLKHVQAIFAHLGhsalQFYVPRGLWTHFKLQGEPVNLREQQDAVEFFMSLFES-----LDEGLKALGHP 1815
Cdd:cd02661 51 -----------EAHVERALASSG----PGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAmqkacLDRFKKLKAVD 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1816 QLMNAT------LGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTV 1889
Cdd:cd02661 116 PSSQETtlvqqiFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKAS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1890 KRLCVKKLPPVLAIQLKRFEYDYERvcaiKFNDYFEFPRILDMEPYTVsglaklegevvevgdncQTIVETTKYELTGIV 1969
Cdd:cd02661 196 KQLTIHRAPNVLTIHLKRFSNFRGG----KINKQISFPETLDLSPYMS-----------------QPNDGPLKYKLYAVL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1970 VHSG-QASGGHYFSYILSKNPgngkcQWYKFDDGEVTECKMHedeemkaqcfggDYMGEiydnnlkrmqyrrqkrwwNAY 2048
Cdd:cd02661 255 VHSGfSPHSGHYYCYVKSSNG-----KWYNMDDSKVSPVSIE------------TVLSQ------------------KAY 299
|
....
gi 2046230126 2049 MLFY 2052
Cdd:cd02661 300 ILFY 303
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1790-2053 |
1.08e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 145.51 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1790 EQQDAVEFFMSLFESLDeglkalghpQLMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDI------RNHSSLTESLE 1863
Cdd:cd02674 21 DQQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1864 QYVKGELLEGADAYHCDKCDKKVVTVKRLCVKKLPPVLAIQLKRFEYDYERvcAIKFNDYFEFP-RILDMEPYTvsglak 1942
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGS--TRKLTTPVTFPlNDLDLTPYV------ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1943 legevvevgdNCQTIVETTKYELTGIVVHSGQASGGHYFSYILSKNPGngkcQWYKFDDGEVTecKMHEDEEMKAqcfgg 2022
Cdd:cd02674 164 ----------DTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN----DWYKFDDSRVT--KVSESSVVSS----- 222
|
250 260 270
....*....|....*....|....*....|.
gi 2046230126 2023 dymgeiydnnlkrmqyrrqkrwwNAYMLFYT 2053
Cdd:cd02674 223 -----------------------SAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1663-2020 |
8.94e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 145.98 E-value: 8.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1663 GLKNAGATCYMNSVLQQLYMVPavrvgILRAHGaatldgedFSGDSDLTGGglgqalFSGPASALVSfSTSGGAEDGSQD 1742
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNP-----LLRNYF--------LSDRHSCTCL------SCSPNSCLSC-AMDEIFQEFYYS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1743 VRKNYHvvilkhvqaIFAHLGHSAlqfyvprglWTHFK-LQGEpvnlrEQQDAVEFFMSLFESLDEGLKaLGHPQLMNA- 1820
Cdd:cd02660 62 GDRSPY---------GPINLLYLS---------WKHSRnLAGY-----SQQDAHEFFQFLLDQLHTHYG-GDKNEANDEs 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1821 --------TLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHS---------------SLTESLEQYVKGELLeGADAY 1877
Cdd:cd02660 118 hcnciihqTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAY 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1878 HCDKCDKKVVTVKRLCVKKLPPVLAIQLKRFEYDYERVCAiKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEVGDNcqti 1957
Cdd:cd02660 197 KCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSR-KIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDY---- 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2046230126 1958 vettKYELTGIVVHSGQASGGHYFSYIlsknpGNGKCQWYKFDDGEVTECKmhEDEEMKAQCF 2020
Cdd:cd02660 272 ----TYDLFAVVVHKGTLDTGHYTAYC-----RQGDGQWFKFDDAMITRVS--EEEVLKSQAY 323
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1660-2110 |
2.86e-37 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 154.64 E-value: 2.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1660 GFCGLKNAGATCYMNSVLQQLYMVPAVRVGIlrahgaatldgedfsgdsdltggglgqalfsgpasalvsFSTSGGAEDG 1739
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDV---------------------------------------YGIPTDHPRG 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1740 SQDVRknyhvvilkhvqaifahlghSALQ--FYvprglwtHFKLQGEPVNLRE--------------QQDAVEFFMSLFE 1803
Cdd:COG5077 233 RDSVA--------------------LALQrlFY-------NLQTGEEPVDTTEltrsfgwdsddsfmQHDIQEFNRVLQD 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1804 SLDEGLKALGHPQLMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDK-- 1881
Cdd:COG5077 286 NLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEKhg 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1882 -CDKKvvtvKRLCVKKLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEvgdncqtivet 1960
Cdd:COG5077 366 lQDAK----KGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDADKSENSDAV----------- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1961 tkYELTGIVVHSGQASGGHYFSYIlsKNPGNGkcQWYKFDDGEVTECKMHEDEEmkaQCFGGDYMGE--IYDNNlkrmqy 2038
Cdd:COG5077 431 --YVLYGVLVHSGDLHEGHYYALL--KPEKDG--RWYKFDDTRVTRATEKEVLE---ENFGGDHPYKdkIRDHS------ 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 2039 rRQKRWWNAYMLFYTRCDQ-----TPVQYE---PSVEQlSLTESRNMVLPLPKPIERSVRHQNIRFLHSRSIFSVEFFNF 2110
Cdd:COG5077 496 -GIKRFMSAYMLVYLRKSMlddllNPVAAVdipPHVEE-VLSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDY 573
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1663-2053 |
5.89e-30 |
|
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: 122.42 E-value: 5.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1663 GLKNAGATCYMNSVLQQLYmvpavrvgilrahgAATLdgedFSGDSDLtggglgqalFSgpasalvSFSTSggaedgsqd 1742
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY--------------FENL----LTCLKDL---------FE-------SISEQ--------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1743 vRKNYHVVilkhvqaifahlghsalqfyVPRGLWTHFKLQGEPVNLREQQDAVEFFMSLFESLDEGLKALG--------- 1813
Cdd:cd02663 38 -KKRTGVI--------------------SPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrkl 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1814 --------HPQLMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKK 1885
Cdd:cd02663 97 nnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1886 VVTVKRLCVKKLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPriLDMEPYTVSGLAKlegevvevgDNCQTivettkYEL 1965
Cdd:cd02663 177 QEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFP--LELRLFNTTDDAE---------NPDRL------YEL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1966 TGIVVHSGQ-ASGGHYFSYILSKNpgngkcQWYKFDDGEVTecKMHEdeemkaqcfggDYMGEIYDNNlkRMQYrrqkrw 2044
Cdd:cd02663 240 VAVVVHIGGgPNHGHYVSIVKSHG------GWLLFDDETVE--KIDE-----------NAVEEFFGDS--PNQA------ 292
|
....*....
gi 2046230126 2045 wNAYMLFYT 2053
Cdd:cd02663 293 -TAYVLFYQ 300
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1663-2008 |
7.75e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 117.21 E-value: 7.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1663 GLKNAGATCYMNSVLQQLYMvpavrvgilrahgaATldgeDFSGDsdltggglgqalfsgpasaLVSFSTSGGAEDgsqd 1742
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFM--------------AK----DFRRQ-------------------VLSLNLPRLGDS---- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1743 vrknyhVVILKHVQAIFAHLGHSALQFYVPRglwTHFKLQG--EPVNLREQQDAVEFFMSLFESLDeglkalghpQLMNA 1820
Cdd:cd02664 40 ------QSVMKKLQLLQAHLMHTQRRAEAPP---DYFLEASrpPWFTPGSQQDCSEYLRYLLDRLH---------TLIEK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1821 TLGGSFSDQKICQECPHRYSKEEPFSVFSVDIrnhSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRLCVKKLPPV 1900
Cdd:cd02664 102 MFGGKLSTTIRCLNCNSTSARTERFRDLDLSF---PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEY 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1901 LAIQLKRFEYDYERVCAIKFNDYFEFPRILD--MEPYTVSGLAKLEGEVVEVGDNCQTIVETTKYELTGIVVHSGQAS-G 1977
Cdd:cd02664 179 LILTLLRFSYDQKTHVREKIMDNVSINEVLSlpVRVESKSSESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSSeS 258
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2046230126 1978 GHYFSYILSKNPGNGKCQ----------------WYKFDDGEVTECK 2008
Cdd:cd02664 259 GHYFTYARDQTDADSTGQecpepkdaeendesknWYLFNDSRVTFSS 305
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1791-2052 |
3.29e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 114.02 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1791 QQDAVEFFMSLFESLDEGLKALghpqlmnatLGGSFSDQKICQECPHRYSKEEPFSVFS----VDIRNHSSLTESLEQYV 1866
Cdd:cd02667 51 QQDSHELLRYLLDGLRTFIDSI---------FGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKSECSIESCLKQFT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1867 KGELLEGADAYHCDKCDKkvvTVKRLCVKKLPPVLAIQLKRFEYDyERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGE 1946
Cdd:cd02667 122 EVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1947 vvevgdncqtivETTKYELTGIVVHSGQASGGHYFSYILSKNP-----------------GNGKCQWYKFDDGEVTEckM 2009
Cdd:cd02667 198 ------------SSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPqqrlsdltkskpaadeaGPGSGQWYYISDSDVRE--V 263
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2046230126 2010 HEDEEMKAQcfggdymgeiydnnlkrmqyrrqkrwwnAYMLFY 2052
Cdd:cd02667 264 SLEEVLKSE----------------------------AYLLFY 278
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1663-2016 |
6.04e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 96.24 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1663 GLKNAGATCYMNSVLQQLYMVPAV--RVGILRAHGAATLDGEDFSGDSDLTGggLGQALFSGPASALVSFSTSGgaeDGS 1740
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqwRYDDLENKFPSDVVDPANDLNCQLIK--LADGLLSGRYSKPASLKSEN---DPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1741 QDvrkNYHVVILKHVqaifahLGHSALQFYVPRglwthfklqgepvnlreQQDAVEFFMSLFESLDEGLKALGHPQLMNa 1820
Cdd:cd02658 76 QV---GIKPSMFKAL------IGKGHPEFSTMR-----------------QQDALEFLLHLIDKLDRESFKNLGLNPND- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1821 tLGGSFSDQKI-CQECPHRYSKEEPFSVFSVDIRNHS--------------SLTESLEQYVKGELLEgadaYHCDKCDKK 1885
Cdd:cd02658 129 -LFKFMIEDRLeCLSCKKVKYTSELSEILSLPVPKDEatekeegelvyepvPLEDCLKAYFAPETIE----DFCSTCKEK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1886 VVTVKRLCVKKLPPVLAIQLKRFEYDYERVcaikfndyfefPRILDMEpytvsglaklegevVEVGDNcqtiVETTKYEL 1965
Cdd:cd02658 204 TTATKTTGFKTFPDYLVINMKRFQLLENWV-----------PKKLDVP--------------IDVPEE----LGPGKYEL 254
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2046230126 1966 TGIVVHSG-QASGGHYFSYILSKNPGNGKcqWYKFDDGEVTECKmhEDEEMK 2016
Cdd:cd02658 255 IAFISHKGtSVHSGHYVAHIKKEIDGEGK--WVLFNDEKVVASQ--DPPEMK 302
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1663-2024 |
1.59e-19 |
|
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: 92.01 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1663 GLKNAGATCYMNSVLQQLYMVPAVRvgilrahgaatldgedfsgdsdltggglgqalfsgpaSALVSFSTSGGAEDGSQD 1742
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELR-------------------------------------DALKNYNPARRGANQSSD 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1743 vrknYHVVILKHvqaIFAHLGHSALQFyVPRGLWTHFKL------QGEPVNLREQQDAVEFFMSLFESLDEGLK-ALGHP 1815
Cdd:cd02657 44 ----NLTNALRD---LFDTMDKKQEPV-PPIEFLQLLRMafpqfaEKQNQGGYAQQDAEECWSQLLSVLSQKLPgAGSKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1816 QLMNATLGGSFSDQKICQECPHRYSKE-EPFSVFSVDIrNHSSLTESLEQYVKGELlEGADAYHCDKCDKKVVTVKRLCV 1894
Cdd:cd02657 116 SFIDQLFGIELETKMKCTESPDEEEVStESEYKLQCHI-SITTEVNYLQDGLKKGL-EEEIEKHSPTLGRDAIYTKTSRI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1895 KKLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDM-EPYTVSGLaklegevvevgdncqtivettkYELTGIVVHSG 1973
Cdd:cd02657 194 SRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLyELCTPSGY----------------------YELVAVITHQG 251
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2046230126 1974 Q-ASGGHYFSYILSKNPGngkcQWYKFDDGEVTEckmHEDEEMKAQCFGGDY 2024
Cdd:cd02657 252 RsADSGHYVAWVRRKNDG----KWIKFDDDKVSE---VTEEDILKLSGGGDW 296
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1787-2052 |
7.30e-15 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 76.64 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1787 NLREQQDAVEFFMSLFESLDEGLKalgHPqlmnatLGGSFSDQKICQECPHRYS-KEEPFSVFSVDIRNHS-----SLTE 1860
Cdd:cd02662 30 EFLEQQDAHELFQVLLETLEQLLK---FP------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSsgsgtTLEH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1861 SLEQYVKGELLEGadaYHCDKCDKKVVtvkrlcvkKLPPVLAIQLKRFEYDyERVCAIKFNDYFEFPRILDmepytvsgl 1940
Cdd:cd02662 101 CLDDFLSTEIIDD---YKCDRCQTVIV--------RLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERLP--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1941 aklegevvevgdncqtiveTTKYELTGIVVHSGQASGGHYFSY----------------ILSKNPGNGKCQWYKFDDGEV 2004
Cdd:cd02662 160 -------------------KVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvRMREGPSSTSHPWWRISDTTV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2046230126 2005 TECKmheDEEMKAQCFggdymgeiydnnlkrmqyrrqkrwwnAYMLFY 2052
Cdd:cd02662 221 KEVS---ESEVLEQKS--------------------------AYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1846-2006 |
1.83e-14 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 79.93 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1846 SVFSVD-------IRNHS---SLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRLCVKKLPPVLAIQLKRFEYDYERv 1915
Cdd:COG5560 655 SLFSYDplwtireIGAAErtiTLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1916 cAIKFNDYFEFPRI-LDMEPYTVSglaklegevvevGDNCQTIvettkYELTGIVVHSGQASGGHYFSYIlsKNPGNGkc 1994
Cdd:COG5560 734 -RDKIDDLVEYPIDdLDLSGVEYM------------VDDPRLI-----YDLYAVDNHYGGLSGGHYTAYA--RNFANN-- 791
|
170
....*....|..
gi 2046230126 1995 QWYKFDDGEVTE 2006
Cdd:COG5560 792 GWYLFDDSRITE 803
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1663-2054 |
6.19e-14 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 74.84 E-value: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1663 GLKNAGATCYMNSVLQQL-YMVPAVrvgilrahgaatldgedfsgdsdltggglgQALFSGPASALVSFStsggaedgsQ 1741
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKL------------------------------DELLDDLSKELKVLK---------N 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1742 DVRKNYHvvILKHVQAIfahlghsalqfYVPRGLWTHFKLQGEPVNLRE-QQDAVEFFMSLFESLdeglkalghpqlmNA 1820
Cdd:COG5533 42 VIRKPEP--DLNQEEAL-----------KLFTALWSSKEHKVGWIPPMGsQEDAHELLGKLLDEL-------------KL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1821 TLGGSFSDQ--KICQECPHRYSKeepfSVFSVDIrnhsSLTEslEQYVKG-----ELLEGADAYHCDKCDKKVVTVKRLC 1893
Cdd:COG5533 96 DLVNSFTIRifKTTKDKKKTSTG----DWFDIII----ELPD--QTWVNNlktlqEFIDNMEELVDDETGVKAKENEELE 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1894 V----------KKLPPVLAIQLKRFEYDyervcaikfndyfefprildmepytvSGLAKLEGEVVE------VGDNCQTI 1957
Cdd:COG5533 166 VqakqeyevsfVKLPKILTIQLKRFANL--------------------------GGNQKIDTEVDEkfelpvKHDQILNI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1958 VETTKYELTGIVVHSGQASGGHYFSYILSKNpgngkcQWYKFDDGEVTECKMHEDEEMKAQcfggdymgeiydnnlkrmq 2037
Cdd:COG5533 220 VKETYYDLVGFVLHQGSLEGGHYIAYVKKGG------KWEKANDSDVTPVSEEEAINEKAK------------------- 274
|
410
....*....|....*..
gi 2046230126 2038 yrrqkrwwNAYMLFYTR 2054
Cdd:COG5533 275 --------NAYLYFYER 283
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1791-2022 |
1.32e-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: 72.59 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1791 QQDAVEFFMSLFESLDEGLKALGHP------------QLMNAT-LGGSFSDQKicqecphRYSKEEPFSVFSVDIRNHSS 1857
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEAispgeksknpmvQLFYGTfLTEGVLEGK-------PFCNCETFGQYPLQVNGYGN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1858 LTESLEqyvkGELLEG-ADAYHCDKCDKkvVTVKRLcVKKLPPVLAIQLKRFEYDYERVCaiKFNDYFEFPRILDMEPyt 1936
Cdd:cd02665 95 LHECLE----AAMFEGeVELLPSDHSVK--SGQERW-FTELPPVLTFELSRFEFNQGRPE--KIHDKLEFPQIIQQVP-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1937 vsglaklegevvevgdncqtivettkYELTGIVVHSGQASGGHYFSYILSKNpgngKCQWYKFDDGEVTECKMhedEEMK 2016
Cdd:cd02665 164 --------------------------YELHAVLVHEGQANAGHYWAYIYKQS----RQEWEKYNDISVTESSW---EEVE 210
|
....*.
gi 2046230126 2017 AQCFGG 2022
Cdd:cd02665 211 RDSFGG 216
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1661-2014 |
1.86e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 74.16 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1661 FCGLKNAGATCYMNSVLQQLYMVPAVRVGIlrahgaatldgedfsgdsdltggglgQALFSGPASalvsfstsggaedgs 1740
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGL--------------------------KHLVSLISS--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1741 qdvrknyhvviLKHVQAIF---AHLGHSALQFYVPRGLWTHFKLQGEPVNLREQQDAVEFFMSLFESLDEGLKALGHPQL 1817
Cdd:cd02671 63 -----------VEQLQSSFllnPEKYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEKDFQGQL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1818 MNATLggsfsdqkiCQECPHRYSKEEPFSVFSVDIR-------------------NHSSLTESLEQYVKGELLEGADAYH 1878
Cdd:cd02671 132 VLRTR---------CLECETFTERREDFQDISVPVQeselskseesseispdpktEMKTLKWAISQFASVERIVGEDKYF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1879 CDKCDKKVVTVKRLCVKKLPPVLAIQLKRFEYDYERVCAI----KFNDYFEFPRILDMEpytvsglaklegevvEVGDNC 1954
Cdd:cd02671 203 CENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLE---------------EWSTKP 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2046230126 1955 QTIVettkYELTGIVVHSG-QASGGHYFSYIlsknpgngkcQWYKFDDGEVtecKMHEDEE 2014
Cdd:cd02671 268 KNDV----YRLFAVVMHSGaTISSGHYTAYV----------RWLLFDDSEV---KVTEEKD 311
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1663-2014 |
2.67e-09 |
|
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: 61.74 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1663 GLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGaatlDGEDFSGDSDLTGGGLGQAlfsgpasalVSFSTSGGAEDGSQD 1742
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDE----SKAELASDYPTERRIGGRE---------VSRSELQRSNQFVYE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1743 VRKnyhvvilkhvqaIFAHLGHSALQFYVPRGLWTHFKLqgepvnlrEQQDAVEFFMSLFESLDEGLKALG-HPQLMNAT 1821
Cdd:cd02666 70 LRS------------LFNDLIHSNTRSVTPSKELAYLAL--------RQQDVTECIDNVLFQLEVALEPISnAFAGPDTE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1822 LGGSFSDQ-------KICQ--------ECPHRYSKEEPFSVFSVDIR---------NHS-SLTESLEQYVKGELLEGADA 1876
Cdd:cd02666 130 DDKEQSDLikrlfsgKTKQqlvpesmgNQPSVRTKTERFLSLLVDVGkkgreivvlLEPkDLYDALDRYFDYDSLTKLPQ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1877 YHCDKCDKKVVTVKRL--CVKKLPPVlaiqlkrfeyDYERV-CAIKFNDYFEFPRILDMEpytvSGLAKLEGEVVEVGDN 1953
Cdd:cd02666 210 RSQVQAQLAQPLQRELisMDRYELPS----------SIDDIdELIREAIQSESSLVRQAQ----NELAELKHEIEKQFDD 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2046230126 1954 CQTIVettkYELTGIVVHSGQASGGHYFSYIlsKNPGNGkcQWYKFDDGEVTEckmHEDEE 2014
Cdd:cd02666 276 LKSYG----YRLHAVFIHRGEASSGHYWVYI--KDFEEN--VWRKYNDETVTV---VPASE 325
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1831-2001 |
5.51e-09 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 60.36 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1831 ICQECPHRYSKEEPFSVFSVDIRNHSSLTES----------LEQYVKGELLEGAdayHCDKCDKKVVTVKRLCVKKLPPV 1900
Cdd:pfam13423 141 RCSNCGHESVRESSTHVLDLIYPRKPSSNNKkppnqtfssiLKSSLERETTTKA---WCEKCKRYQPLESRRTVRNLPPV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1901 LAIQLKRFEYDYERVCAikfndyfefprildmepyTVSGLAKlegEV-VEVGDNCQTIVETTKYELTGIVVH-SGQASGG 1978
Cdd:pfam13423 218 LSLNAALTNEEWRQLWK------------------TPGWLPP---EIgLTLSDDLQGDNEIVKYELRGVVVHiGDSGTSG 276
|
170 180
....*....|....*....|....*.
gi 2046230126 1979 HYFSYI---LSKNPGNGKCQWYKFDD 2001
Cdd:pfam13423 277 HLVSFVkvaDSELEDPTESQWYLFND 302
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1648-2007 |
3.16e-07 |
|
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: 55.79 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1648 DYLPpvgarptkGFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRahgaatldgEDFSGDSDLTGGGLGQALfsgpasal 1727
Cdd:cd02669 114 PYLP--------GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL---------YENYENIKDRKSELVKRL-------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1728 vsfstsggaedgSQDVRKNYHVVILK-HVQAifahlgHSALQfYVPrglwthfKLQGEPVNLREQQDAVEFFMSLFESLd 1806
Cdd:cd02669 169 ------------SELIRKIWNPRNFKgHVSP------HELLQ-AVS-------KVSKKKFSITEQSDPVEFLSWLLNTL- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1807 eglkalgHPQLMnatlGGSFSDQKICQEC-------------PHRYSKEEPFSVFSVDIRNHSSLT-------------- 1859
Cdd:cd02669 222 -------HKDLG----GSKKPNSSIIHDCfqgkvqietqkikPHAEEEGSKDKFFKDSRVKKTSVSpfllltldlppppl 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1860 -------ESLEQYVKGELLegadayhcDKCDKKVVT-----VKRLCVKKLPPVLAIQLKRFEYdyervcaikfNDYF--- 1924
Cdd:cd02669 291 fkdgneeNIIPQVPLKQLL--------KKYDGKTETelkdsLKRYLISRLPKYLIFHIKRFSK----------NNFFkek 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1925 -----EFPRILDMEPYTVSGLAKLEGEVvevgdncqtivetTKYELTGIVVHSGQASGGHYFSYILSKNPGNgkcQWYKF 1999
Cdd:cd02669 353 nptivNFPIKNLDLSDYVHFDKPSLNLS-------------TKYNLVANIVHEGTPQEDGTWRVQLRHKSTN---KWFEI 416
|
....*...
gi 2046230126 2000 DDGEVTEC 2007
Cdd:cd02669 417 QDLNVKEV 424
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1790-2001 |
7.45e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 46.75 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1790 EQQDAVEFFMSLFESLDEGLKALghpqLMNATLGGS--FSDQKICQEcphrysKEEPFSVFSVDIRNHSSLTESLEQYVK 1867
Cdd:cd02670 22 EQQDPEEFFNFITDKLLMPLLEP----KVDIIHGGKkdQDDDKLVNE------RLLQIPVPDDDDGGGITLEQCLEQYFN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1868 GELLegadayhcdkcdkkvvtvkrlcvKKLPPVLAIQLKRFEYDYERvcAIKFNDYFEFPRILDMEPY---TVSGLAKLE 1944
Cdd:cd02670 92 NSVF-----------------------AKAPSCLIICLKRYGKTEGK--AQKMFKKILIPDEIDIPDFvadDPRACSKCQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2046230126 1945 GEVVEVGDNCQTIVETTKYELT--GIVVHSGQA-SGGHYFSYIlSKNPGNGKC--------QWYKFDD 2001
Cdd:cd02670 147 LECRVCYDDKDFSPTCGKFKLSlcSAVCHRGTSlETGHYVAFV-RYGSYSLTEtdneaynaQWVFFDD 213
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1820-2006 |
1.11e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 43.66 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1820 ATLGGSFSdqKICQECPHRYSKEEPFSV----------FSVDIRNHSSLTESL---EQYVK-GELLEGADAYHCDKCDKK 1885
Cdd:cd02672 66 STLIQNFT--RFLLETISQDQLGTPFSCgtsrnsvsllYTLSLPLGSTKTSKEstfLQLLKrSLDLEKVTKAWCDTCCKY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046230126 1886 VVTVKRLCVKKLPPVLAIQLKRfeydYERVCAIKFNDYF-EFPRILDMEPYTVSGLAKLEGEVVEVGDNcqtivETTKYE 1964
Cdd:cd02672 144 QPLEQTTSIRHLPDILLLVLVI----NLSVTNGEFDDINvVLPSGKVMQNKVSPKAIDHDKLVKNRGQE-----SIYKYE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2046230126 1965 LTGIVVH-SGQASGGHYFSYILSKNPGNGKCQWYKFDDGEVTE 2006
Cdd:cd02672 215 LVGYVCEiNDSSRGQHNVVFVIKVNEESTHGRWYLFNDFLVTP 257
|
|
| |
