|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1666-2064 |
2.03e-146 |
|
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: 459.03 E-value: 2.03e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1666 GFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAhgaattdgedfsgdsdltggglgsalfsgpasalvslpsssstieD 1745
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI---------------------------------------------P 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1746 GLHDVRKNYHVVILKHVQAIFAHLGHSALQYYVPRglWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKALGQPQLM 1825
Cdd:cd02659 36 PTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELT--DKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLI 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1826 NATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLP 1905
Cdd:cd02659 114 KNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1906 PVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEgevvevGDNCQTNVETTKYELTGIVVHSGQASGG 1985
Cdd:cd02659 194 PVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKE------GDSEKKDSESYIYELHGVLVHSGDAHGG 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24651753 1986 HYFSYILSKNpangKCQWYKFDDGEVTECKMHEDEEmkaECFGGEYMGETYDNNlkrmqYRRQKRWWNAYMLFYTRCDQ 2064
Cdd:cd02659 268 HYYSYIKDRD----DGKWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYERKSP 334
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
2198-2566 |
1.33e-95 |
|
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: 316.16 E-value: 1.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 2198 PSRLGEYILMAPSPDVRTVFVKLVVFFCH-----FAINDEPLTGYDGA----NLCEQVLISVLRLL---KSEAADYGKHL 2265
Cdd:pfam12030 1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCDPDDLEeewrSLSDSVLEAVVALLdhlWKEFHTHLRSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 2266 PHYFSLFSMYVGLGTREKQQLLRLN-VPLQFIQVALDDGPGPAIKYQYPE------------FSKLHQVVSHLIRCSDVS 2332
Cdd:pfam12030 81 DEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARmlrlvekrrppsYEKLIQLLSVLLRCCDLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 2333 EKCQSSNQNARPLsnpfkdPNVAHEELTPLSTECMDLL--FNRTG---YIKKVIEDTNVGDEGLKLLQYCSWENPHFSRA 2407
Cdd:pfam12030 161 LPPQSINEGAEPL------PNSLPDGPFPLTSEEADLLrpLGRTNgsiFVKKLLEIDQNPEATRKILRFLLWENPELSDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 2408 VLTELLWQCGFAYCHDMRHhTDLLLNILLIDDSWQHHRIHNALNGVAEEREGLLETIQRAKTHYQKRAYQIIKCLTqLFH 2487
Cdd:pfam12030 235 ILKTLLWGIRGAPAHLLRD-PFLRAAIVFCEDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCINCRL-GFD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 2488 KSPIALQMLHT------------NSNITRHwsiAVEWLQGELdrqrgigcqyNSYSWSPPAQSNDNTNG----------- 2544
Cdd:pfam12030 313 KEWFASQVLENipdwappllsypDSNVRSE---TEDFLQEEL----------FSHEMGPDPQFRLREAArrlgiacleyl 379
|
410 420
....*....|....*....|....*...
gi 24651753 2545 ---YMLERSQ---SAKNTWSMAFELCPD 2566
Cdd:pfam12030 380 rgtYVLRRSQverSAVETLQRVIELCPE 407
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1668-2059 |
1.98e-78 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 262.76 E-value: 1.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1668 CGLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGAATTDGEDFSGDsdltggglgsalfsgpasalvslpsssstiedgl 1747
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1748 hdvrknyhvvILKHVQAIFAHL-GHSALQYYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKA---LGQPQ 1823
Cdd:pfam00443 47 ----------LLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENES 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1824 LMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLT------ESLEQYVKGELLEGADAYHCDKCDKKVVTVK 1897
Cdd:pfam00443 117 LITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1898 RVCVKKLPPVLAIQLKRFEYDYErvCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVevgdncqtnvettKYELTGIVV 1977
Cdd:pfam00443 197 QLKISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-------------DYRLVAVVV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1978 HSGQASGGHYFSYIlsKNPANGKcqWYKFDDGEVTECKMHEDEEMkaecfggeymgetydnnlkrmqyrrqkrwWNAYML 2057
Cdd:pfam00443 262 HSGSLSSGHYIAYI--KAYENNR--WYKFDDEKVTEVDEETAVLS-----------------------------SSAYIL 308
|
..
gi 24651753 2058 FY 2059
Cdd:pfam00443 309 FY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1795-2059 |
5.65e-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: 193.08 E-value: 5.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1795 LREQQDAVEFFMSLLESLDEGLKALG--------QPQLMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDI----RNH 1862
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSkrtsdsssLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1863 SSLTESLEQYVKGELLEGADAYHCDKCdKKVVTVKRVCVKKLPPVLAIQLKRFEYDyERVCAIKFNDYFEFPRILDMEPY 1942
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1943 TVSGlaklegevvevGDNCQTNVETTKYELTGIVVHSGQ-ASGGHYFSYILSKNpangKCQWYKFDDGEVTECKMHEDEE 2021
Cdd:cd02257 177 LSEG-----------EKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPS----DGKWYKFNDDKVTEVSEEEVLE 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 24651753 2022 MkaecfggeymgetydnnlkrmqyrrQKRWWNAYMLFY 2059
Cdd:cd02257 242 F-------------------------GSLSSSAYILFY 254
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1669-2060 |
2.22e-50 |
|
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: 182.62 E-value: 2.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1669 GLKNAGATCYMNSVLQQLYMVPAVRvgilrahgaattdgedfsgdsdltggglgsalfsgpaSALVSLPSSSSTIEDGLH 1748
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFR-------------------------------------KAVYECNSTEDAELKNMP 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1749 DVRKNYHVVILKHVQAIFAHLGHSALQYYVPRGLwthFKLLGepVNLREQQDAVEF---FMSLLESLDEGLKALGQPQLM 1825
Cdd:cd02668 44 PDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGF---VKALG--LDTGQQQDAQEFsklFLSLLEAKLSKSKNPDLKNIV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1826 NATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLP 1905
Cdd:cd02668 119 QDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1906 PVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYtvsglaklegevvevGDNCQTNVETtkYELTGIVVHSGQ-ASG 1984
Cdd:cd02668 199 PTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY---------------LAESDEGSYV--YELSGVLIHQGVsAYS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1985 GHYFSYIlsKNPANGKcqWYKFDDGEVTEC--KMHED--EEMKAECFGGEYMGETYDNNlkrmqyrrqkrwwNAYMLFYT 2060
Cdd:cd02668 262 GHYIAHI--KDEQTGE--WYKFNDEDVEEMpgKPLKLgnSEDPAKPRKSEIKKGTHSSR-------------TAYMLVYK 324
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1668-2018 |
2.72e-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: 164.37 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1668 CGLKNAGATCYMNSVLQQLYMVPAVrvgilrahgaattdgedfsgdsdltggglgsalfsgpASALVSlpsssstiedGL 1747
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPL-------------------------------------ANYLLS----------RE 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1748 HDVRKNYHVV-----ILKHVQAIFAHLGHSalqyYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLES-----LDEGLK 1817
Cdd:cd02661 35 HSKDCCNEGFcmmcaLEAHVERALASSGPG----SAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAmqkacLDRFKK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1818 ALGQPQLMNAT------LGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDK 1891
Cdd:cd02661 111 LKAVDPSSQETtlvqqiFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1892 KVVTVKRVCVKKLPPVLAIQLKRFEYDYERvcaiKFNDYFEFPRILDMEPYTVsglaklegevvevgdncQTNVETTKYE 1971
Cdd:cd02661 191 KVKASKQLTIHRAPNVLTIHLKRFSNFRGG----KINKQISFPETLDLSPYMS-----------------QPNDGPLKYK 249
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24651753 1972 LTGIVVHSG-QASGGHYFSYILSknpANGkcQWYKFDDGEVTECKMHE 2018
Cdd:cd02661 250 LYAVLVHSGfSPHSGHYYCYVKS---SNG--KWYNMDDSKVSPVSIET 292
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1797-2060 |
7.32e-39 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 145.89 E-value: 7.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1797 EQQDAVEFFMSLLESLDEGLKALGQPQLMNATlggsfsdqkICQECPHRYSKEEPFSVFSVDI------RNHSSLTESLE 1870
Cdd:cd02674 21 DQQDAQEFLLFLLDGLHSIIVDLFQGQLKSRL---------TCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1871 QYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERvcAIKFNDYFEFP-RILDMEPYTVSGlak 1949
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGS--TRKLTTPVTFPlNDLDLTPYVDTR--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1950 legevvevgdnCQTNVetTKYELTGIVVHSGQASGGHYFSYIlsKNPANGkcQWYKFDDGEVTecKMHEDEEMKAecfgg 2029
Cdd:cd02674 167 -----------SFTGP--FKYDLYAVVNHYGSLNGGHYTAYC--KNNETN--DWYKFDDSRVT--KVSESSVVSS----- 222
|
250 260 270
....*....|....*....|....*....|.
gi 24651753 2030 eymgetydnnlkrmqyrrqkrwwNAYMLFYT 2060
Cdd:cd02674 223 -----------------------SAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1669-2027 |
1.80e-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: 148.29 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1669 GLKNAGATCYMNSVLQQLYMVPavrvgILRAHgaattdgedfsgdsdltggglgsaLFSGPASALVSLPSSSSTIEDGLH 1748
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNP-----LLRNY------------------------FLSDRHSCTCLSCSPNSCLSCAMD 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1749 DVRKNYHVViLKHVQAIFAHLGHSAlqyyvprglWTHFKLLGEpvnlREQQDAVEFFMSLLESLDEG-LKALGQPQLMNA 1827
Cdd:cd02660 53 EIFQEFYYS-GDRSPYGPINLLYLS---------WKHSRNLAG----YSQQDAHEFFQFLLDQLHTHyGGDKNEANDESH 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1828 -------TLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHS---------------SLTESLEQYVKGELLeGADAYH 1885
Cdd:cd02660 119 cnciihqTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAYK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1886 CDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAiKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEVGDNcqtnv 1965
Cdd:cd02660 198 CSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSR-KIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDY----- 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24651753 1966 ettKYELTGIVVHSGQASGGHYFSYIlsknpANGKCQWYKFDDGEVTECKmhEDEEMKAECF 2027
Cdd:cd02660 272 ---TYDLFAVVVHKGTLDTGHYTAYC-----RQGDGQWFKFDDAMITRVS--EEEVLKSQAY 323
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1666-2117 |
5.31e-37 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 153.87 E-value: 5.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1666 GFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAhgaaTTDGEDfsgdsdltggglgsalfsGPASALVSLPSSSSTIED 1745
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI----PTDHPR------------------GRDSVALALQRLFYNLQT 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1746 GLHDVrknyhvvilkhvqaifahlghSALQYYVPRGlWTHFKLLgepvnlrEQQDAVEFFMSLLESLDEGLKALGQPQLM 1825
Cdd:COG5077 250 GEEPV---------------------DTTELTRSFG-WDSDDSF-------MQHDIQEFNRVLQDNLEKSMRGTVVENAL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1826 NATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDK---CDKKvvtvKRVCVK 1902
Cdd:COG5077 301 NGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEKhglQDAK----KGVIFE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1903 KLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEvgdncqtnvettkYELTGIVVHSGQA 1982
Cdd:COG5077 377 SLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDADKSENSDAV-------------YVLYGVLVHSGDL 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1983 SGGHYFSYIlsKNPANGkcQWYKFDDGEVTECKMHEDEEmkaECFGGEYMgetYDNNLKRMQyrRQKRWWNAYMLFYTRC 2062
Cdd:COG5077 444 HEGHYYALL--KPEKDG--RWYKFDDTRVTRATEKEVLE---ENFGGDHP---YKDKIRDHS--GIKRFMSAYMLVYLRK 511
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24651753 2063 DQ-----TPVQYE---PSVEQlSLAESRNMVLPLPKPIERSVRHQNIRFLHSRSIFSVEFFNF 2117
Cdd:COG5077 512 SMlddllNPVAAVdipPHVEE-VLSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDY 573
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1798-2060 |
1.54e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 127.04 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1798 QQDAVEFFMSLLESLDEGLKALGQPQL--------MNATLG---------GSFSDQKICQECPHRYSKEEPFSVFSVDIR 1860
Cdd:cd02663 65 HQDAHEFLNFLLNEIAEILDAERKAEKanrklnnnNNAEPQptwvheifqGILTNETRCLTCETVSSRDETFLDLSIDVE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1861 NHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPriLDME 1940
Cdd:cd02663 145 QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFP--LELR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1941 PYTVSGLAKlegevvevgDNCQTnvettkYELTGIVVHSGQ-ASGGHYFSYILSKNpangkcQWYKFDDGEVTECkmheD 2019
Cdd:cd02663 223 LFNTTDDAE---------NPDRL------YELVAVVVHIGGgPNHGHYVSIVKSHG------GWLLFDDETVEKI----D 277
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24651753 2020 EEMKAECFGGEymgetydNNLKrmqyrrqkrwwNAYMLFYT 2060
Cdd:cd02663 278 ENAVEEFFGDS-------PNQA-----------TAYVLFYQ 300
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1669-2015 |
4.27e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 123.76 E-value: 4.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1669 GLKNAGATCYMNSVLQQLYMVPAVRVGILRahgaattdgedfsgdsdltggglgsalfsgpasalvslpsssstiedgLH 1748
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS------------------------------------------------LN 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1749 DVRKNYHVVILKHVQAIFAHLGHSALQYYVPRGLWTHfKLLGEPVNLREQQDAVEFFMSLLESLDeglkalgqpQLMNAT 1828
Cdd:cd02664 33 LPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLE-ASRPPWFTPGSQQDCSEYLRYLLDRLH---------TLIEKM 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1829 LGGSFSDQKICQECPHRYSKEEPFSVFSVDIrnhSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVL 1908
Cdd:cd02664 103 FGGKLSTTIRCLNCNSTSARTERFRDLDLSF---PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1909 AIQLKRFEYDYERVCAIKFNDYFEFPRILDMePYTV------SGLAKLEGEVVEVGDNCqtnVETTKYELTGIVVHSGQA 1982
Cdd:cd02664 180 ILTLLRFSYDQKTHVREKIMDNVSINEVLSL-PVRVesksseSPLEKKEEESGDDGELV---TRQVHYRLYAVVVHSGYS 255
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 24651753 1983 S-GGHYFSYILSKNPANGKCQ----------------WYKFDDGEVTECK 2015
Cdd:cd02664 256 SeSGHYFTYARDQTDADSTGQecpepkdaeendesknWYLFNDSRVTFSS 305
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1798-2059 |
5.42e-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: 113.25 E-value: 5.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1798 QQDAVEFFMSLLESLDEGLKALgqpqlmnatLGGSFSDQKICQECPHRYSKEEPFSVFS----VDIRNHSSLTESLEQYV 1873
Cdd:cd02667 51 QQDSHELLRYLLDGLRTFIDSI---------FGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKSECSIESCLKQFT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1874 KGELLEGADAYHCDKCDKkvvTVKRVCVKKLPPVLAIQLKRFEYDyERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGE 1953
Cdd:cd02667 122 EVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1954 vvevgdncqtnvETTKYELTGIVVHSGQASGGHYFSYILSKNP-----------------ANGKCQWYKFDDGEVTEckM 2016
Cdd:cd02667 198 ------------SSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPqqrlsdltkskpaadeaGPGSGQWYYISDSDVRE--V 263
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 24651753 2017 HEDEEMKAEcfggeymgetydnnlkrmqyrrqkrwwnAYMLFY 2059
Cdd:cd02667 264 SLEEVLKSE----------------------------AYLLFY 278
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1669-2023 |
1.08e-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: 98.55 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1669 GLKNAGATCYMNSVLQQLYMVPAV--RVGILRAHGAATTDGEDFSGDSDLTGggLGSALFSGPASALVSLPSSSSTIEDG 1746
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqwRYDDLENKFPSDVVDPANDLNCQLIK--LADGLLSGRYSKPASLKSENDPYQVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1747 LHdvrknyhvvilkhvqaifahlghsalqyyvPRGlwthFK-LLGEpvNLRE-----QQDAVEFFMSLLESLDEGLKALG 1820
Cdd:cd02658 79 IK------------------------------PSM----FKaLIGK--GHPEfstmrQQDALEFLLHLIDKLDRESFKNL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1821 QPQLMNatLGGSFSDQKI-CQECPHRYSKEEPFSVFSVDIRNHS--------------SLTESLEQYVKGELLEgadaYH 1885
Cdd:cd02658 123 GLNPND--LFKFMIEDRLeCLSCKKVKYTSELSEILSLPVPKDEatekeegelvyepvPLEDCLKAYFAPETIE----DF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1886 CDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVcaikfndyfefPRILDMEpytvsglaklegevVEVGDncqtNV 1965
Cdd:cd02658 197 CSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWV-----------PKKLDVP--------------IDVPE----EL 247
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 24651753 1966 ETTKYELTGIVVHSG-QASGGHYFSYIlsKNPANGKCQWYKFDDGEVTECKmhEDEEMK 2023
Cdd:cd02658 248 GPGKYELIAFISHKGtSVHSGHYVAHI--KKEIDGEGKWVLFNDEKVVASQ--DPPEMK 302
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1669-2031 |
1.30e-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: 92.39 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1669 GLKNAGATCYMNSVLQQLYMVPAVRvGILRAHGAATTDGEDFSGDsdltggglgsaLFSGPASALVSLPSSSSTIedglh 1748
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELR-DALKNYNPARRGANQSSDN-----------LTNALRDLFDTMDKKQEPV----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1749 dvrknyhvvilkhVQAIFAHLGHSALQYYVPRGLWTHFKllgepvnlreQQDAVEFFMSLLESLDEGLK-ALGQPQLMNA 1827
Cdd:cd02657 64 -------------PPIEFLQLLRMAFPQFAEKQNQGGYA----------QQDAEECWSQLLSVLSQKLPgAGSKGSFIDQ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1828 TLGGSFSDQKICQECPHRYSKE-EPFSVFSVDIrNHSSLTESLEQYVKgELLEGADAYHCDKCDKKVVTVKRVCVKKLPP 1906
Cdd:cd02657 121 LFGIELETKMKCTESPDEEEVStESEYKLQCHI-SITTEVNYLQDGLK-KGLEEEIEKHSPTLGRDAIYTKTSRISRLPK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1907 VLAIQLKRFEYDYERVCAIKFNDYFEFPRILDM-EPYTVSGLaklegevvevgdncqtnvettkYELTGIVVHSGQ-ASG 1984
Cdd:cd02657 199 YLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLyELCTPSGY----------------------YELVAVITHQGRsADS 256
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24651753 1985 GHYFSYILSKNPAngkcQWYKFDDGEVTEckmHEDEEMKAECFGGEY 2031
Cdd:cd02657 257 GHYVAWVRRKNDG----KWIKFDDDKVSE---VTEEDILKLSGGGDW 296
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1667-2021 |
9.07e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 84.17 E-value: 9.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1667 FCGLKNAGATCYMNSVLQQLYMVPAVRVGIlrahgaattdgedfsgdsdltggglgsalfsgpaSALVSLPSSSSTIEDG 1746
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGL----------------------------------KHLVSLISSVEQLQSS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1747 LHDVRKNYHvvilkhvqaifahlghSALQYYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKALGQPQLMN 1826
Cdd:cd02671 70 FLLNPEKYN----------------DELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEKDFQGQLVL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1827 ATLggsfsdqkiCQECPHRYSKEEPFSVFSVDIR--NHSSLTESLE-----------------QYVKGELLEGADAYHCD 1887
Cdd:cd02671 134 RTR---------CLECETFTERREDFQDISVPVQesELSKSEESSEispdpktemktlkwaisQFASVERIVGEDKYFCE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1888 KCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAI----KFNDYFEFPRILDMEpytvsglaklegevvEVGDNCQT 1963
Cdd:cd02671 205 NCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLE---------------EWSTKPKN 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 24651753 1964 NVettkYELTGIVVHSG-QASGGHYFSYIlsknpangkcQWYKFDDGEVtecKMHEDEE 2021
Cdd:cd02671 270 DV----YRLFAVVMHSGaTISSGHYTAYV----------RWLLFDDSEV---KVTEEKD 311
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1794-2015 |
3.86e-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: 77.41 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1794 NLREQQDAVEFFMSLLESLDEGLKalgQPqlmnatLGGSFSDQKICQECPHRYS-KEEPFSVFSVDIRNHS-----SLTE 1867
Cdd:cd02662 30 EFLEQQDAHELFQVLLETLEQLLK---FP------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSsgsgtTLEH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1868 SLEQYVKGELLEGadaYHCDKCDKKVVtvkrvcvkKLPPVLAIQLKRFEYDyERVCAIKFNDYFEFPRILDmepytvsgl 1947
Cdd:cd02662 101 CLDDFLSTEIIDD---YKCDRCQTVIV--------RLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERLP--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1948 aklegevvevgdncqtnveTTKYELTGIVVHSGQASGGHYFSY----------------ILSKNPANGKCQWYKFDDGEV 2011
Cdd:cd02662 160 -------------------KVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvRMREGPSSTSHPWWRISDTTV 220
|
....
gi 24651753 2012 TECK 2015
Cdd:cd02662 221 KEVS 224
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1853-2062 |
3.01e-14 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 79.16 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1853 SVFSVD-------IRNHS---SLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERv 1922
Cdd:COG5560 655 SLFSYDplwtireIGAAErtiTLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1923 cAIKFNDYFEFPRI-LDMEPYTVSGLAKLEGevvevgdncqtnvettkYELTGIVVHSGQASGGHYFSYIlsKNPANGkc 2001
Cdd:COG5560 734 -RDKIDDLVEYPIDdLDLSGVEYMVDDPRLI-----------------YDLYAVDNHYGGLSGGHYTAYA--RNFANN-- 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24651753 2002 QWYKFDDGEVTECkmhEDEEMKAEcfggeymgetydnnlkrmqyrrqkrwwNAYMLFYTRC 2062
Cdd:COG5560 792 GWYLFDDSRITEV---DPEDSVTS---------------------------SAYVLFYRRK 822
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1669-2061 |
7.22e-14 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 74.84 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1669 GLKNAGATCYMNSVLQQLYMvpavrvgilrahgaattdgedfsgdsdltggglgsalfsgpasalvSLPSSSSTIEDGLh 1748
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAL----------------------------------------------YLPKLDELLDDLS- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1749 dvrKNYHVVILKHVQaifahlGHSALQY----YVPRGLWTHFKLLGEPVNLRE-QQDAVEFFMSLLESLdeglkalgqpq 1823
Cdd:COG5533 34 ---KELKVLKNVIRK------PEPDLNQeealKLFTALWSSKEHKVGWIPPMGsQEDAHELLGKLLDEL----------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1824 lmNATLGGSFSDQ--KICQECPHRYSKeepfSVFSVDIrnhsSLTEslEQYVKG-----ELLEGADAYHCDKCDKKVVT- 1895
Cdd:COG5533 94 --KLDLVNSFTIRifKTTKDKKKTSTG----DWFDIII----ELPD--QTWVNNlktlqEFIDNMEELVDDETGVKAKEn 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1896 -----VKR----VCVKKLPPVLAIQLKRFEYDyervcaikfndyfefprildmepytvSGLAKLEGEVVE------VGDN 1960
Cdd:COG5533 162 eelevQAKqeyeVSFVKLPKILTIQLKRFANL--------------------------GGNQKIDTEVDEkfelpvKHDQ 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1961 CQTNVETTKYELTGIVVHSGQASGGHYFSYILSKNpangkcQWYKFDDGEVTECKMHEDEEMKAEcfggeymgetydnnl 2040
Cdd:COG5533 216 ILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKGG------KWEKANDSDVTPVSEEEAINEKAK--------------- 274
|
410 420
....*....|....*....|.
gi 24651753 2041 krmqyrrqkrwwNAYMLFYTR 2061
Cdd:COG5533 275 ------------NAYLYFYER 283
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1798-2029 |
2.50e-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: 71.82 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1798 QQDAVEFFMSLLESLDEGLK-ALGQPQLMNATLG-------GSFSDQKICQEcpHRYSKEEPFSVFSVDIRNHSSLTESL 1869
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQaAAEAISPGEKSKNpmvqlfyGTFLTEGVLEG--KPFCNCETFGQYPLQVNGYGNLHECL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1870 EqyvkGELLEG-ADAyhcDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCaiKFNDYFEFPRILDMEPytvsgla 1948
Cdd:cd02665 100 E----AAMFEGeVEL---LPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPE--KIHDKLEFPQIIQQVP------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1949 klegevvevgdncqtnvettkYELTGIVVHSGQASGGHYFSYILSKNpangKCQWYKFDDGEVTECKMhedEEMKAECFG 2028
Cdd:cd02665 164 ---------------------YELHAVLVHEGQANAGHYWAYIYKQS----RQEWEKYNDISVTESSW---EEVERDSFG 215
|
.
gi 24651753 2029 G 2029
Cdd:cd02665 216 G 216
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1669-2008 |
1.10e-09 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 62.29 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1669 GLKNAGATCYMNSVLQQLYMVPAVRVGILrAHgAATTDGEDFSGDSDLtggGLgsaLFsgpasalvslpsssstieDGLH 1748
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLAL-SH-LATECLKEHCLLCEL---GF---LF------------------DMLE 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1749 DVRKnyhvvilKHVQA-----IFAHL-GHSALqyyvprGLWTHFKLLGEPVNLREQQDAVEFFmsLLESL-DEGLKALGQ 1821
Cdd:pfam13423 56 KAKG-------KNCQAsnflrALSSIpEASAL------GLLDEDRETNSAISLSSLIQSFNRF--LLDQLsSEENSTPPN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1822 PQ----LMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTES----------LEQYVKGELLEGAdayHCD 1887
Cdd:pfam13423 121 PSpaesPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYPRKPSSNNKkppnqtfssiLKSSLERETTTKA---WCE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1888 KCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAikfndyfefprildmepyTVSGLAKlegEV-VEVGDNCQTNVE 1966
Cdd:pfam13423 198 KCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWK------------------TPGWLPP---EIgLTLSDDLQGDNE 256
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24651753 1967 TTKYELTGIVVH-SGQASGGHYFSYI---LSKNPANGKCQWYKFDD 2008
Cdd:pfam13423 257 IVKYELRGVVVHiGDSGTSGHLVSFVkvaDSELEDPTESQWYLFND 302
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1669-2021 |
1.19e-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: 62.89 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1669 GLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGaattDGEDFSGDSDLTggglgsALFSGPASALVSLPSSSSTIedglH 1748
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDE----SKAELASDYPTE------RRIGGREVSRSELQRSNQFV----Y 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1749 DVRKnyhvvilkhvqaIFAHLGHSALQYYVPRGLWTHFKLLgepvnlreQQDAVEFFMSLLESLDEGLKALGQPQLMNAT 1828
Cdd:cd02666 69 ELRS------------LFNDLIHSNTRSVTPSKELAYLALR--------QQDVTECIDNVLFQLEVALEPISNAFAGPDT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1829 -LGGSFSDQ-------KICQ--------ECPHRYSKEEPFSVFSVDIR---------NHS-SLTESLEQYVKGELLEgad 1882
Cdd:cd02666 129 eDDKEQSDLikrlfsgKTKQqlvpesmgNQPSVRTKTERFLSLLVDVGkkgreivvlLEPkDLYDALDRYFDYDSLT--- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1883 ayhcdkcdkkvvtvkrvcvkKLPPVLAIQLKrfeydyervcaikfNDYFEFPRILDMEPYT----VSGLAKLEGEVVEVG 1958
Cdd:cd02666 206 --------------------KLPQRSQVQAQ--------------LAQPLQRELISMDRYElpssIDDIDELIREAIQSE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1959 DNCQTNVETTK------------------YELTGIVVHSGQASGGHYFSYIlsKNPANGkcQWYKFDDGEVTEckmHEDE 2020
Cdd:cd02666 252 SSLVRQAQNELaelkheiekqfddlksygYRLHAVFIHRGEASSGHYWVYI--KDFEEN--VWRKYNDETVTV---VPAS 324
|
.
gi 24651753 2021 E 2021
Cdd:cd02666 325 E 325
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1654-2014 |
7.94e-08 |
|
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: 57.71 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1654 DYLPpvgarptkGFCGLKNAGATCYMNSVLQQLYMVPAVRvgilrahgaattdgeDF--SGDSDLTGGGLgsalfsgpAS 1731
Cdd:cd02669 114 PYLP--------GFVGLNNIKNNDYANVIIQALSHVKPIR---------------NFflLYENYENIKDR--------KS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1732 ALVSLPSSSstiedglhdVRKNYHVVILK-HVQAifahlgHSALQYYVprglwthfKLLGEPVNLREQQDAVEFFMSLLE 1810
Cdd:cd02669 163 ELVKRLSEL---------IRKIWNPRNFKgHVSP------HELLQAVS--------KVSKKKFSITEQSDPVEFLSWLLN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1811 SLdegLKALGqpqlmnatlGGSFSDQKICQEC-------------PHRYSKEEPFSVFSVDIRNHSSLT----------- 1866
Cdd:cd02669 220 TL---HKDLG---------GSKKPNSSIIHDCfqgkvqietqkikPHAEEEGSKDKFFKDSRVKKTSVSpfllltldlpp 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1867 ----------ESLEQYVKGELLegadayhcDKCDKKVVT-----VKRVCVKKLPPVLAIQLKRFEYdyervcaikfNDYF 1931
Cdd:cd02669 288 pplfkdgneeNIIPQVPLKQLL--------KKYDGKTETelkdsLKRYLISRLPKYLIFHIKRFSK----------NNFF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1932 --------EFP-RILDMEPYtvsglaklegevveVGDNCQTNVETTKYELTGIVVHSGQASGGHYFSYILSKNPANgkcQ 2002
Cdd:cd02669 350 keknptivNFPiKNLDLSDY--------------VHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTN---K 412
|
410
....*....|..
gi 24651753 2003 WYKFDDGEVTEC 2014
Cdd:cd02669 413 WFEIQDLNVKEV 424
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1902-2008 |
1.82e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 45.60 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1902 KKLPPVLAIQLKRFEYDYERvcAIKFNDYFEFPRILDMEPY---TVSGLAKLEGEVVEVGDNCQTNVETTKYELT--GIV 1976
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGK--AQKMFKKILIPDEIDIPDFvadDPRACSKCQLECRVCYDDKDFSPTCGKFKLSlcSAV 173
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24651753 1977 VHSGQA-SGGHYFSYI--------LSKNPANGKcQWYKFDD 2008
Cdd:cd02670 174 CHRGTSlETGHYVAFVrygsysltETDNEAYNA-QWVFFDD 213
|
|
| Ubl_UBP24 |
cd17065 |
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ... |
994-1060 |
6.77e-04 |
|
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain.
Pssm-ID: 340585 Cd Length: 79 Bit Score: 40.76 E-value: 6.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24651753 994 DDMEIVTHSNETMAAFKRNLLKRIKgTSTANIKvdlFYANDEMIGVSDEINPLYQYTIRDKMNLTAK 1060
Cdd:cd17065 17 QEFTLEVHSNETLGSVRQKIAERLN-CPVDQVQ---IFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1827-2013 |
2.47e-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: 42.50 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1827 ATLGGSFSdqKICQECPHRYSKEEPFSV----------FSVDIRNHSSLTESL---EQYVK-GELLEGADAYHCDKCDKK 1892
Cdd:cd02672 66 STLIQNFT--RFLLETISQDQLGTPFSCgtsrnsvsllYTLSLPLGSTKTSKEstfLQLLKrSLDLEKVTKAWCDTCCKY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651753 1893 VVTVKRVCVKKLPPVLAIQLKRfeydYERVCAIKFNDYF-EFPRILDMEPYTVSGLAKLEGEVVEVGDNcqtnvETTKYE 1971
Cdd:cd02672 144 QPLEQTTSIRHLPDILLLVLVI----NLSVTNGEFDDINvVLPSGKVMQNKVSPKAIDHDKLVKNRGQE-----SIYKYE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24651753 1972 LTGIVVH-SGQASGGHYFSYILSKNPANGKCQWYKFDDGEVTE 2013
Cdd:cd02672 215 LVGYVCEiNDSSRGQHNVVFVIKVNEESTHGRWYLFNDFLVTP 257
|
|
|