|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-506 |
3.26e-132 |
|
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: 405.12 E-value: 3.26e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 198 GAGMLNVGNTCYLNSTLQALFHIPALANWLVSEtAHVENCNISESCGsgGCIICAMAKTLQTTQSNQTAVRPFLiyTKLR 277
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSR-EHSKDCCNEGFCM--MCALEAHVERALASSGPGSAPRIFS--SNLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 278 QICKHMVVGRQEDAHEFLRFLVEAMEKAYLMRFRNYKELDQLVKETTPLSQIFGGYLRSEVRCLSCNHVSITFQHFQDLL 357
Cdd:cd02661 76 QISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 358 LDIRKADTLEEAFDGYFSRERLEDMG-YKCEGCKKKVSATKQFSLERAPITLCIQLKRFSMM-GNKLTKQISFKPRIDLS 435
Cdd:cd02661 156 LDIKGADSLEDALEQFTKPEQLDGENkYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFrGGKINKQISFPETLDLS 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251765101 436 RFAARSPAastQPLSYRLVSMVTHLGVSQHCGHYTAIGLTESGSYYNFDDSYVRPIAMQSVCNTNAYIMFY 506
Cdd:cd02661 236 PYMSQPND---GPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
199-506 |
6.72e-70 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 236.57 E-value: 6.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 199 AGMLNVGNTCYLNSTLQALFHIPALANWLVSETAHVENCNISESCGsggcIICAMAKTLQ--TTQSNQTAVRPFLIYTKL 276
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN----LLCALRDLFKalQKNSKSSSVSPKMFKKSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 277 RQICKHMVVGRQEDAHEFLRFLVEAMEKAylmrfrnyKELDQLVKETTPLSQIFGGYLRSEVRCLSCNHVSITFQHFQDL 356
Cdd:pfam00443 77 GKLNPDFSGYKQQDAQEFLLFLLDGLHED--------LNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 357 LLDIRKADTL-------EEAFDGYFSRERLEDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFS---MMGNKLTKQI 426
Cdd:pfam00443 149 SLPIPGDSAElktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynrSTWEKLNTEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 427 SFKPRIDLSRFAARSPAASTQPL-SYRLVSMVTHLGvSQHCGHYTA-IGLTESGSYYNFDDSYVRPIAMQ-SVCNTNAYI 503
Cdd:pfam00443 229 EFPLELDLSRYLAEELKPKTNNLqDYRLVAVVVHSG-SLSSGHYIAyIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYI 307
|
...
gi 251765101 504 MFY 506
Cdd:pfam00443 308 LFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
200-507 |
1.75e-61 |
|
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: 210.80 E-value: 1.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHipalanwlvsetahvencnisescgsggciicamaktlqttqsnqtavrpfliytklrqi 279
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 280 ckhmvvgRQEDAHEFLRFLVEAMEKAYlmrFRNYKELDQLVKETTPLSQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLD 359
Cdd:cd02257 21 -------EQQDAHEFLLFLLDKLHEEL---KKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLP 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 360 I----RKADTLEEAFDGYFSRERLEDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFS----MMGNKLTKQISFKPR 431
Cdd:cd02257 91 LpvkgLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSfnedGTKEKLNTKVSFPLE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 432 IDLSRFAARSP---AASTQPLSYRLVSMVTHLGVSQHCGHYTAIGL-TESGSYYNFDDSYVRPIAMQSV-----CNTNAY 502
Cdd:cd02257 171 LDLSPYLSEGEkdsDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVlefgsLSSSAY 250
|
....*
gi 251765101 503 IMFYE 507
Cdd:cd02257 251 ILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-506 |
2.47e-58 |
|
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: 204.53 E-value: 2.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHIPALANWLVSEtahvENCNISESCGSGGCIICAMAKTLQTTQSNQTaVRPFLIYTKLR-- 277
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSD----RHSCTCLSCSPNSCLSCAMDEIFQEFYYSGD-RSPYGPINLLYls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 278 -QICKHMVVGRQEDAHEFLRFLVEAMEKAYLMRFRNYKELDQLvkeTTPLSQIFGGYLRSEVRCLSCNHVSITFQHFQDL 356
Cdd:cd02660 77 wKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHC---NCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 357 LLDI------RKAD---------TLEEAFDGYFSRERLEDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFSMMGN- 420
Cdd:cd02660 154 SLDIpnkstpSWALgesgvsgtpTLSDCLDRFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 421 ---KLTKQISFKPRIDLSRF--AARSPAASTQPLS----YRLVSMVTHLGvSQHCGHYTAIGLTESGSYYNFDDSYVRPI 491
Cdd:cd02660 234 tsrKIDTYVQFPLELNMTPYtsSSIGDTQDSNSLDpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRV 312
|
330
....*....|....*
gi 251765101 492 AMQSVCNTNAYIMFY 506
Cdd:cd02660 313 SEEEVLKSQAYLLFY 327
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-507 |
1.06e-45 |
|
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: 168.20 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHIPALANWLVSETAHVENCNISEscgsggcIICAMAKT---LQTTQSNQTAVRPFLiytKL 276
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKS-------VPLALQRLflfLQLSESPVKTTELTD---KT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 277 RQICKHMV-VGRQEDAHEFLRFLVEAMEKAylMRfrnYKELDQLVKettplsQIFGGYLRSEVRCLSCNHVSITFQHFQD 355
Cdd:cd02659 74 RSFGWDSLnTFEQHDVQEFFRVLFDKLEEK--LK---GTGQEGLIK------NLFGGKLVNYIICKECPHESEREEYFLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 356 LLLDIRKADTLEEAFDGYFSRERLE-DMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRF-----SMMGNKLTKQISFK 429
Cdd:cd02659 143 LQVAVKGKKNLEESLDAYVQGETLEgDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfeTMMRIKINDRFEFP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 430 PRIDLSRFAARSPAAS--------TQPLSYRLVSMVTHLGvSQHCGHYTA-IGLTESGSYYNFDDSYVRPIAMQSV---C 497
Cdd:cd02659 223 LELDMEPYTEKGLAKKegdsekkdSESYIYELHGVLVHSG-DAHGGHYYSyIKDRDDGKWYKFNDDVVTPFDPNDAeeeC 301
|
330 340
....*....|....*....|....*....
gi 251765101 498 -------------------NTNAYIMFYE 507
Cdd:cd02659 302 fggeetqktydsgprafkrTTNAYMLFYE 330
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-507 |
6.42e-44 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 159.38 E-value: 6.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHipalanwlvsetahvencnisescgsggciicamaktlqttqsnqtavrpfliytklrqi 279
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 280 ckhmvvgRQEDAHEFLRFLVEamekaylmrfrnykELDQLVkettplSQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLD 359
Cdd:cd02674 21 -------DQQDAQEFLLFLLD--------------GLHSII------VDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLP 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 360 IRKAD------TLEEAFDGYFSRERLEDM-GYKCEGCKKKVSATKQFSLERAPITLCIQLKRFS---MMGNKLTKQISFK 429
Cdd:cd02674 74 IPSGSgdapkvTLEDCLRLFTKEETLDGDnAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSfsrGSTRKLTTPVTFP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 430 PRI-DLSRFAarSPAASTQPLSYRLVSMVTHLGvSQHCGHYTA---IGLTesGSYYNFDDSYVRPIAMQSVCNTNAYIMF 505
Cdd:cd02674 154 LNDlDLTPYV--DTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAyckNNET--NDWYKFDDSRVTKVSESSVVSSSAYILF 228
|
..
gi 251765101 506 YE 507
Cdd:cd02674 229 YE 230
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-507 |
2.30e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 144.84 E-value: 2.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHIPALANwLVSETahvencnisescgsggciicamaktlqttqsnqtavrPFLIYTKLRQI 279
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSET-------------------------------------PKELFSQVCRK 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 280 CKHMVVGRQEDAHEFLRFLVEAMEkaylmrfrnykeldqlvketTPLSQIFGGYLRSEVRCLSCNHVSITFQHFQDLLL- 358
Cdd:cd02667 43 APQFKGYQQQDSHELLRYLLDGLR--------------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLp 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 359 ---DIRKADTLEEAFDGYFSRERLEDMG-YKCEGCKKkvsATKQFSLERAPITLCIQLKRFSMMGN----KLTKQISFKP 430
Cdd:cd02667 103 rsdEIKSECSIESCLKQFTEVEILEGNNkFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSanlrKVSRHVSFPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 431 RIDLSRF---AARSPAASTQPLsYRLVSMVTHLGvSQHCGHYTA----------------------IGLTESGSYYNFDD 485
Cdd:cd02667 180 ILDLAPFcdpKCNSSEDKSSVL-YRLYGVVEHSG-TMRSGHYVAyvkvrppqqrlsdltkskpaadEAGPGSGQWYYISD 257
|
330 340
....*....|....*....|..
gi 251765101 486 SYVRPIAMQSVCNTNAYIMFYE 507
Cdd:cd02667 258 SDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-507 |
1.69e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 141.02 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHIPALAN--WLVSETAHVENCNISESCGSGGCIICAMAKTL--QTTQSNQTAVRPFLIYTK 275
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKavYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIfaQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 276 LRqickhMVVGRQEDAHEFLRFLVEAMEkAYLMRFRNyKELDQLVKettplsQIFGGYLRSEVRCLSCNHVSITFQHFQD 355
Cdd:cd02668 81 LG-----LDTGQQQDAQEFSKLFLSLLE-AKLSKSKN-PDLKNIVQ------DLFRGEYSYVTQCSKCGRESSLPSKFYE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 356 LLLDIRKADTLEEAFDGYFSRERLE-DMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRF-----SMMGNKLTKQISFK 429
Cdd:cd02668 148 LELQLKGHKTLEECIDEFLKEEQLTgDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFvfdrkTGAKKKLNASISFP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 430 PRIDLSRFAARSPaasTQPLSYRLVSMVTHLGVSQHCGHYTA-IGLTESGSYYNFDDSYVRPIAMQSV------------ 496
Cdd:cd02668 228 EILDMGEYLAESD---EGSYVYELSGVLIHQGVSAYSGHYIAhIKDEQTGEWYKFNDEDVEEMPGKPLklgnsedpakpr 304
|
330 340
....*....|....*....|
gi 251765101 497 ---------CNTNAYIMFYE 507
Cdd:cd02668 305 kseikkgthSSRTAYMLVYK 324
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-507 |
1.01e-34 |
|
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: 135.53 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHIPALaNWLVSETAHVENCNISescGSGGCIICAMAKTLQTTQSNQTAVrPFLIYTKLRQI 279
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSF-QWRYDDLENKFPSDVV---DPANDLNCQLIKLADGLLSGRYSK-PASLKSENDPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 280 CKHM-------VVG---------RQEDAHEFLRFLVEAMEKaylmrfrnykelDQLVKETTPLSQIFGGYLRSEVRCLSC 343
Cdd:cd02658 76 QVGIkpsmfkaLIGkghpefstmRQQDALEFLLHLIDKLDR------------ESFKNLGLNPNDLFKFMIEDRLECLSC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 344 NHVSITFQHFQDLLLDIRKAD--------------TLEEAFDGYFSRERLEdmgYKCEGCKKKVSATKQFSLERAPITLC 409
Cdd:cd02658 144 KKVKYTSELSEILSLPVPKDEatekeegelvyepvPLEDCLKAYFAPETIE---DFCSTCKEKTTATKTTGFKTFPDYLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 410 IQLKRFSMMGNKLTKQISFKPRIDLSRFAARspaastqplsYRLVSMVTHLGVSQHCGHYTAI---GLTESGSYYNFDDS 486
Cdd:cd02658 221 INMKRFQLLENWVPKKLDVPIDVPEELGPGK----------YELIAFISHKGTSVHSGHYVAHikkEIDGEGKWVLFNDE 290
|
330 340
....*....|....*....|...
gi 251765101 487 YVrpIAMQSVCN--TNAYIMFYE 507
Cdd:cd02658 291 KV--VASQDPPEmkKLGYIYFYQ 311
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-507 |
1.88e-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: 125.50 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHipalaNWLVSETAHVENCNISESCGSGgciICAMAKTLQTTQSNQTAVRPFLiytklrqi 279
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLTCLKDLFESISEQKKRTG---VISPKKFITRLKRENELFDNYM-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 280 ckhmvvgrQEDAHEFLRFLV----EAMEKAYLMRFRNYKELDQLVKETTP--LSQIFGGYLRSEVRCLSCNHVSITFQHF 353
Cdd:cd02663 65 --------HQDAHEFLNFLLneiaEILDAERKAEKANRKLNNNNNAEPQPtwVHEIFQGILTNETRCLTCETVSSRDETF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 354 QDLLLDIRKADTLEEAFDGYFSRERL-EDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFSMMGN-----KLTKQIS 427
Cdd:cd02663 137 LDLSIDVEQNTSITSCLRQFSATETLcGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQlnryiKLFYRVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 428 FKPRIdlsRFAARSPAASTQPLSYRLVSMVTHLGVSQHCGHYTAIGLTESGsYYNFDDSYVRPIAMQSVCN--------T 499
Cdd:cd02663 217 FPLEL---RLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGG-WLLFDDETVEKIDENAVEEffgdspnqA 292
|
....*...
gi 251765101 500 NAYIMFYE 507
Cdd:cd02663 293 TAYVLFYQ 300
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-507 |
3.29e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 125.68 E-value: 3.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHIPALANWLVSETAHVENCNISescgsggciicaMAKTLQTTQSnqtavrpFLIYTKLRQI 279
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQS------------VMKKLQLLQA-------HLMHTQRRAE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 280 CKHMVV-----------GRQEDAHEFLRFLVEamekaylmrfrnykELDQLVKETtplsqiFGGYLRSEVRCLSCNHVSI 348
Cdd:cd02664 62 APPDYFleasrppwftpGSQQDCSEYLRYLLD--------------RLHTLIEKM------FGGKLSTTIRCLNCNSTSA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 349 TFQHFQDLLLDIrkaDTLEEAFDGYFSRERL-EDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFS-----MMGNKL 422
Cdd:cd02664 122 RTERFRDLDLSF---PSVQDLLNYFLSPEKLtGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqktHVREKI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 423 TKQISFKPRIDL-----SRFAARSPAAS-----------TQPLSYRLVSMVTHLGVSQHCGHY----------------- 469
Cdd:cd02664 199 MDNVSINEVLSLpvrveSKSSESPLEKKeeesgddgelvTRQVHYRLYAVVVHSGYSSESGHYftyardqtdadstgqec 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 251765101 470 ----TAIGLTESGSYYNFDDSYVRPIAMQSVCNT-------NAYIMFYE 507
Cdd:cd02664 279 pepkDAEENDESKNWYLFNDSRVTFSSFESVQNVtsrfpkdTPYILFYE 327
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-507 |
1.76e-22 |
|
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: 97.82 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHIPALANWLVSETAhvencnisescgsggciicamaktlqttqsnqtavrpfliytklrqi 279
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLE----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 280 ckhmvvgrQEDAHEFLRFLVEAmekaylmrfrnykeLDQLVKetTPlsqiFGGYLRSEVRCLSCNHVS-ITFQHFQDLLL 358
Cdd:cd02662 34 --------QQDAHELFQVLLET--------------LEQLLK--FP----FDGLLASRIVCLQCGESSkVRYESFTMLSL 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 359 DIRKAD-----TLEEAFDGYFSRERLEDmgYKCEGCKKKVSatkqfsleRAPITLCIQLKRFSMMGN----KLTKQISFK 429
Cdd:cd02662 86 PVPNQSsgsgtTLEHCLDDFLSTEIIDD--YKCDRCQTVIV--------RLPQILCIHLSRSVFDGRgtstKNSCKVSFP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 430 PRIdlsrfaarspaastQPLSYRLVSMVTHLGvSQHCGHYTA---------------------IGLTESGSYYNFDDSYV 488
Cdd:cd02662 156 ERL--------------PKVLYRLRAVVVHYG-SHSSGHYVCyrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTV 220
|
330 340
....*....|....*....|
gi 251765101 489 RPIAMQSVCNT-NAYIMFYE 507
Cdd:cd02662 221 KEVSESEVLEQkSAYMLFYE 240
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
199-489 |
7.67e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 95.34 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 199 AGMLNVGNTCYLNSTLQALFHIPALAN---WLVSETAHVENCNISescgsggciiCAMAKTLQTTQSNQTAVRPFLiyTK 275
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSS----------FLLNPEKYNDELANQAPRRLL--NA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 276 LRQICKHMVVGRQEDAHEFLRFLVEamekaylmrfrNYKELdqlvkettpLSQIFGGYLRSEVRCLSCNHVSITFQHFQD 355
Cdd:cd02671 93 LREVNPMYEGYLQHDAQEVLQCILG-----------NIQEL---------VEKDFQGQLVLRTRCLECETFTERREDFQD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 356 LLLDIRKAD-------------------TLEEAFDGYFSRERL--EDMgYKCEGCKKKVSATKQFSLERAPITLCIQLKR 414
Cdd:cd02671 153 ISVPVQESElskseesseispdpktemkTLKWAISQFASVERIvgEDK-YFCENCHHYTEAERSLLFDKLPEVITIHLKC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 415 FSMMGNKltkqisFKPRIDLSRFAARSPAASTQPL----------SYRLVSMVTHLGVSQHCGHYTAiglteSGSYYNFD 484
Cdd:cd02671 232 FAANGSE------FDCYGGLSKVNTPLLTPLKLSLeewstkpkndVYRLFAVVMHSGATISSGHYTA-----YVRWLLFD 300
|
....*
gi 251765101 485 DSYVR 489
Cdd:cd02671 301 DSEVK 305
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
200-488 |
5.21e-19 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 93.40 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHIPALANwLVSETAhvencniSESCGSGGCIICAMAK---TLQTTQ---SNQTAVRPFlIY 273
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRK-DVYGIP-------TDHPRGRDSVALALQRlfyNLQTGEepvDTTELTRSF-GW 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 274 TKLRQICKHmvvgrqeDAHEFLRFLVEAMEKAylMRfrnykelDQLVKETtpLSQIFGGYLRSEVRCLSCNHVSITFQHF 353
Cdd:COG5077 266 DSDDSFMQH-------DIQEFNRVLQDNLEKS--MR-------GTVVENA--LNGIFVGKMKSYIKCVNVNYESARVEDF 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 354 QDLLLDIRKADTLEEAFDGYFSRERLE-DMGYKCEGcKKKVSATKQFSLERAPITLCIQLKRFSM-----MGNKLTKQIS 427
Cdd:COG5077 328 WDIQLNVKGMKNLQESFRRYIQVETLDgDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYdferdMMVKINDRYE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251765101 428 FKPRIDLSRFAARSPAAS-TQPLSYRLVSMVTHLGvSQHCGHYTAIGLTE-SGSYYNFDDSYV 488
Cdd:COG5077 407 FPLEIDLLPFLDRDADKSeNSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRV 468
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
200-507 |
5.77e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 79.85 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQAL-FHIPALANWLVSETAHVEncnisescgsggciicAMAKTLQTTQSNQTAVRPFLIYTKLRQ 278
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELK----------------VLKNVIRKPEPDLNQEEALKLFTALWS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 279 ICKHMVV-----GRQEDAHEFLRFLVEAME--KAYLMRFRNYKELDQLVKETT-PLSQIfggylrsevrclscnHVSITF 350
Cdd:COG5533 65 SKEHKVGwippmGSQEDAHELLGKLLDELKldLVNSFTIRIFKTTKDKKKTSTgDWFDI---------------IIELPD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 351 QHFqdllLDIRKadTLEEAFDGYFSRERLEDMGYKCEGCKKKVSATKQF--SLERAPITLCIQLKRFsmmGNKLTKQ--- 425
Cdd:COG5533 130 QTW----VNNLK--TLQEFIDNMEELVDDETGVKAKENEELEVQAKQEYevSFVKLPKILTIQLKRF---ANLGGNQkid 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 426 ISFKPRIDLSrFAARSPAASTQPLSYRLVSMVTHLGvSQHCGHYTAIgLTESGSYYNFDDSYVRPIAMQSVCNT---NAY 502
Cdd:COG5533 201 TEVDEKFELP-VKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAY-VKKGGKWEKANDSDVTPVSEEEAINEkakNAY 277
|
....*
gi 251765101 503 IMFYE 507
Cdd:COG5533 278 LYFYE 282
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-488 |
1.94e-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 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: 78.53 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHIPALANWLVSETAhvencNISESCGSGGCIICAMAKTLQTTQSNQTAVRPFLIYTKLR-- 277
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNP-----ARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRma 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 278 --QICKHMVVG--RQEDAHEFLRFLveamekayLMRFRNykELDQLVKETTPLSQIFGGYLRSEVRCL-SCNHVSITFQH 352
Cdd:cd02657 76 fpQFAEKQNQGgyAQQDAEECWSQL--------LSVLSQ--KLPGAGSKGSFIDQLFGIELETKMKCTeSPDEEEVSTES 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 353 FQDLLLDIRKADTLEEAFDGYfsRERL-EDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFSMMGN-----KLTKQI 426
Cdd:cd02657 146 EYKLQCHISITTEVNYLQDGL--KKGLeEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDiqkkaKILRKV 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251765101 427 SFKPRIDLSRFAARSPAastqplsYRLVSMVTHLGVSQHCGHYTA-IGLTESGSYYNFDDSYV 488
Cdd:cd02657 224 KFPFELDLYELCTPSGY-------YELVAVITHQGRSADSGHYVAwVRRKNDGKWIKFDDDKV 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
200-360 |
1.15e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 75.69 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 200 GMLNVGNTCYLNSTLQALFHIPALANWLVSEtAHVENCNISESCGSGGCIICAMAKTLQTTQS-NQTAVRPFLIYTKLRQ 278
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSD-EYEESINEENPLGMHGSVASAYADLIKQLYDgNLHAFTPSGFKKTIGS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 279 IcKHMVVG-RQEDAHEFLRFLVEAM--------EKAYLMRFRNYKELDQLVKET-------------TPLSQIFGGYLRS 336
Cdd:COG5560 346 F-NEEFSGyDQQDSQEFIAFLLDGLhedlnriiKKPYTSKPDLSPGDDVVVKKKakecwwehlkrndSIITDLFQGMYKS 424
|
170 180
....*....|....*....|....
gi 251765101 337 EVRCLSCNHVSITFQHFQDLLLDI 360
Cdd:COG5560 425 TLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
199-472 |
1.41e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 73.07 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 199 AGMLNVGNTCYLNSTLQALFHIPALANWLVSETAhvENCnISESCgsggcIICAM---------AKTL--QTtqSNqtav 267
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLA--TEC-LKEHC-----LLCELgflfdmlekAKGKncQA--SN---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 268 rpFLiyTKLRQICKHMVVGRQEDAHE-------------FLRFLVEAMEKAYLMRFRNYKEldqlvkETTPLSQIFGGYL 334
Cdd:pfam13423 67 --FL--RALSSIPEASALGLLDEDREtnsaislssliqsFNRFLLDQLSSEENSTPPNPSP------AESPLEQLFGIDA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 335 RSEVRCLSCNHVSI--TFQHFQDLLLDIRKADTLEEAFDGYF------SRERleDMGYK--CEGCKKKVSATKQFSLERA 404
Cdd:pfam13423 137 ETTIRCSNCGHESVreSSTHVLDLIYPRKPSSNNKKPPNQTFssilksSLER--ETTTKawCEKCKRYQPLESRRTVRNL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251765101 405 PITLCIQLKRFSMMGNKLTKQISF-KPRIDLSRFAARSPAASTQplSYRLVSMVTHLGVSQHCGHYTAI 472
Cdd:pfam13423 215 PPVLSLNAALTNEEWRQLWKTPGWlPPEIGLTLSDDLQGDNEIV--KYELRGVVVHIGDSGTSGHLVSF 281
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
365-507 |
2.29e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 74.92 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 365 TLEEAFDGYFSRERL--EDMGYkCEGCKKKVSATKQFSLERAPITLCIQLKRFSmmgnkltKQISFKPRI---------- 432
Cdd:COG5560 676 TLQDCLNEFSKPEQLglSDSWY-CPGCKEFRQASKQMELWRLPMILIIHLKRFS-------SVRSFRDKIddlveypidd 747
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251765101 433 -DLSRFAarSPAASTQpLSYRLVSMVTHLGVSQHcGHYTA-IGLTESGSYYNFDDSYVRPIAMQSVCNTNAYIMFYE 507
Cdd:COG5560 748 lDLSGVE--YMVDDPR-LIYDLYAVDNHYGGLSG-GHYTAyARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
203-507 |
5.25e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 64.09 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 203 NVGNTCYLNSTLQALfhipalanwlvsetahvencnisescgsggciicamaktlqttqSNQTAVRPFLIYTKlrqickh 282
Cdd:cd02673 4 NTGNSCYFNSTMQAL--------------------------------------------SSIGKINTEFDNDD------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 283 mvvgrQEDAHEFLRFLVEAMEKAYLMRFRNYKELDQLVKETTPLSQIFGGYLRSEVrCLSCNH--VSITFQHFQDLLLDI 360
Cdd:cd02673 33 -----QQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLEAFKYTIESSYV-CIGCSFeeNVSDVGNFLDVSMID 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 361 RKADTLEEAFDGYFSRERLEDmgyKCEGCKKKVSATKQfSLERAPITLCIQLKRFsmmgnkltkqisfKPRIDLSRFAAR 440
Cdd:cd02673 107 NKLDIDELLISNFKTWSPIEK---DCSSCKCESAISSE-RIMTFPECLSINLKRY-------------KLRIATSDYLKK 169
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251765101 441 SPAA----STQPLSYRLVSMVTHLGVSQHCGHYTAI--GLTESGSYYNFDDSYVRPIAMQSVCN---TNAYIMFYE 507
Cdd:cd02673 170 NEEImkkyCGTDAKYSLVAVICHLGESPYDGHYIAYtkELYNGSSWLYCSDDEIRPVSKNDVSTnarSSGYLIFYD 245
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
199-489 |
1.20e-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: 61.35 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 199 AGMLNVGNTCYLNSTLQALFHIPALANWLVseTAHVENCNISESCGS----GGCIIcaMAKTLQTTQ------------- 261
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVL--NFDESKAELASDYPTerriGGREV--SRSELQRSNqfvyelrslfndl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 262 --SNQTAVRPF--LIYTKLrqickhmvvgRQEDAHEFL---RFLVEAMEKAYLMRFRNYKELDQLVKETTPLSQIFGGYL 334
Cdd:cd02666 78 ihSNTRSVTPSkeLAYLAL----------RQQDVTECIdnvLFQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 335 RSEVRCLSCNHVSIT--FQHFQDLLLDIRK----------ADTLEEAFDGYFSRERLEDM-GYKCEGCKKKVSAT-KQFS 400
Cdd:cd02666 148 QQLVPESMGNQPSVRtkTERFLSLLVDVGKkgreivvllePKDLYDALDRYFDYDSLTKLpQRSQVQAQLAQPLQrELIS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 401 LERapITLCIQLKRF-SMMGNKLTKQISFKPRIDLSRFAARSPAAST----QPLSYRLVSMVTHLGVSQHcGHY-TAIGL 474
Cdd:cd02666 228 MDR--YELPSSIDDIdELIREAIQSESSLVRQAQNELAELKHEIEKQfddlKSYGYRLHAVFIHRGEASS-GHYwVYIKD 304
|
330
....*....|....*
gi 251765101 475 TESGSYYNFDDSYVR 489
Cdd:cd02666 305 FEENVWRKYNDETVT 319
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
287-507 |
8.46e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 48.68 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 287 RQEDAHEFLRFLVEAMEKAYLmrfrnykeldqlvketTPLSQIFGG--YLRSEVRCLSCNHVSITFQHFQDLlldirKAD 364
Cdd:cd02670 22 EQQDPEEFFNFITDKLLMPLL----------------EPKVDIIHGgkKDQDDDKLVNERLLQIPVPDDDDG-----GGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 365 TLEEAFDGYFSrerledmgykcegckkkvsaTKQFSLerAPITLCIQLKRFSMMGNKLTKQISF---KPRIDLSRFAARS 441
Cdd:cd02670 81 TLEQCLEQYFN--------------------NSVFAK--APSCLIICLKRYGKTEGKAQKMFKKiliPDEIDIPDFVADD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765101 442 PAA-----------------STQPLSYRLV--SMVTHLGVSQHCGHYTAIGLTESGSYYNFDDSYvrpiamqsvcnTNAY 502
Cdd:cd02670 139 PRAcskcqlecrvcyddkdfSPTCGKFKLSlcSAVCHRGTSLETGHYVAFVRYGSYSLTETDNEA-----------YNAQ 207
|
....*
gi 251765101 503 IMFYE 507
Cdd:cd02670 208 WVFFD 212
|
|
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