|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
121-421 |
3.42e-180 |
|
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: 528.00 E-value: 3.42e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 121 GAGLHNLGNTCFLNSTVQCLTYTPPLANYLLSKEHSRSCHQSGFCMICVMQNHIIQAFANTANAIKPVSFIRDLKKIARH 200
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 201 FRFGSQEDAHEFLRYTIDAMQKACLNGYPKL---DRQTQATTLVHQIFGGYLRSRVKCSICKSVSDTYDPYLDIALEIRQ 277
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 278 AANIVRALELFVKPDVLSGENAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQ 357
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 770478837 358 SSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSMVHSSNIKVVLNQQAYVLFYL 421
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
122-420 |
3.63e-77 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 256.22 E-value: 3.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 122 AGLHNLGNTCFLNSTVQCLTYTPPLANYLLSKEHSRSCHQSGFC--MICVMQNHIIQAFANTAN-AIKPVSFIRDLKKIA 198
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSsSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 199 RHFRFGSQEDAHEFLRYTIDAMQKAClngypKLDRQTQATTLVHQIFGGYLRSRVKCSICKSVSDTYDPYLDIALEIRQA 278
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 279 ANIVR------ALELFVKPDVLSGENAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLN 350
Cdd:pfam00443 156 SAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 770478837 351 IRPYMSQSS----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SNGQWYQMNDSMV-HSSNIKVVLNQQAYVLFY 420
Cdd:pfam00443 236 LSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.64e-74 |
|
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: 249.60 E-value: 1.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLTYTPPLANYLLSKEHSRSCH--QSGFCMICVMQNhIIQAFANTANAiKPVSFIRDLK---KI 197
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLscSPNSCLSCAMDE-IFQEFYYSGDR-SPYGPINLLYlswKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 198 ARHFRFGSQEDAHEFLRYTIDAMQKACLNGYPKLDRQTQATTLVHQIFGGYLRSRVKCSICKSVSDTYDPYLDIALEIRQ 277
Cdd:cd02660 80 SRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 278 AANIVRA---------------LELFVKPDVLsGENAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFANFSGG---KI 339
Cdd:cd02660 160 KSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 340 TKDVGYPEFLNIRPYMSQSSGDPVM---------YGLYAVLVHSGySCHAGHYYCYVKASNGQWYQMNDSMVHSSNIKVV 410
Cdd:cd02660 239 DTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEV 317
|
330
....*....|
gi 770478837 411 LNQQAYVLFY 420
Cdd:cd02660 318 LKSQAYLLFY 327
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
123-420 |
6.72e-67 |
|
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: 225.83 E-value: 6.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLtytpplanyllskehsrschqsgfcmicvmqnhiiqafantanaikpvsfirdlkkiarhfr 202
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 203 FGSQEDAHEFLRYTIDAMQKACLNGYPKLDRQTQATTLVHQIFGGYLRSRVKCSICKSVSDTYDP--YLDIALEIRQAA- 279
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPq 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 280 -NIVRALELFVKPDVLSGENAYMCaKCKKKVPATKRFTVHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYM 355
Cdd:cd02257 99 vSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 770478837 356 SQ------SSGDPVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSMVHSSNIKVVL-----NQQAYVLFY 420
Cdd:cd02257 178 SEgekdsdSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
9.71e-54 |
|
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: 189.13 E-value: 9.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLTYTPPLANyLLSKehsrschqsgfcmicvmqnhiiqafantanaiKPVSFIRDLKKIARHFR 202
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSE--------------------------------TPKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 203 FGSQEDAHEFLRYTIDAMQkaclngypkldrqtqatTLVHQIFGGYLRSRVKCSICKSVSDTYDPYLDIAL----EIRQA 278
Cdd:cd02667 48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 279 ANIVRALELFVKPDVLSGENAYMCAKCKKkvpATKRFTVHRTSNVLTLSLKRF-----ANFSggKITKDVGYPEFLNIRP 353
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 354 YMSQS-----SGDPVMYGLYAVLVHSGySCHAGHYYCYVKASN----------------------GQWYQMNDSMVHSSN 406
Cdd:cd02667 186 FCDPKcnsseDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 770478837 407 IKVVLNQQAYVLFY 420
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
2.82e-51 |
|
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: 180.18 E-value: 2.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLtytpplanyllskehsrschqsgfcmicvmqnhiiqafantanaikpvsfirdlkkiarhfr 202
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 203 FGSQEDAHEFLRYTIDamqkaclngypKLDRqtqattLVHQIFGGYLRSRVKCSICKSVSDTYDPYLDIALEIRQAANIV 282
Cdd:cd02674 19 SADQQDAQEFLLFLLD-----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 283 RA------LELFVKPDVLSGENAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIR 352
Cdd:cd02674 82 PKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 353 PY-MSQSSGDPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSMVHSSNIKVVLNQQAYVLFY 420
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-423 |
5.06e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 180.53 E-value: 5.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLTYTPPLANYLLS------KEHSRSchqsgfcMICVMQnhiiQAFANTANAIKPVSFIRDLKK 196
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSipptedDDDNKS-------VPLALQ----RLFLFLQLSESPVKTTELTDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 197 IarhFRFGS-------QEDAHEFLRYTIDAMQKaclngypKLdRQTQATTLVHQIFGGYLRSRVKCSICKSVSDTYDPYL 269
Cdd:cd02659 73 T---RSFGWdslntfeQHDVQEFFRVLFDKLEE-------KL-KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 270 DIALEIRQAANIVRALELFVKPDVLSGENAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFaNF-----SGGKITKDVG 344
Cdd:cd02659 142 DLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-EFdfetmMRIKINDRFE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 345 YPEFLNIRPYMSQSSG-----------DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSMVHSSNIKVVLN 412
Cdd:cd02659 221 FPLELDMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEE 299
|
330 340 350
....*....|....*....|....*....|...
gi 770478837 413 QQ----------------------AYVLFYLRI 423
Cdd:cd02659 300 ECfggeetqktydsgprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
7.24e-41 |
|
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: 152.85 E-value: 7.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLTYtpplaNYLLSkehsrsCHQSGFCmiCVMQNHiiqafaNTANAIKPVSFIRDLKKIARHFR 202
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLT------CLKDLFE--SISEQK------KRTGVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 203 FGSQEDAHEFLRYTIDAMQKaCLNGYPKLDRQ----------TQATTLVHQIFGGYLRSRVKCSICKSVSDTYDPYLDIA 272
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIAE-ILDAERKAEKAnrklnnnnnaEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 273 LEIRQAANIVRALELFVKPDVLSGENAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFA-NFSGGKITK---DVGYPEF 348
Cdd:cd02663 141 IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRYIKlfyRVVFPLE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 349 LNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNGQWYQMNDSMV---HSSNIKVVLNQ-----QAYVLFY 420
Cdd:cd02663 221 LRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVekiDENAVEEFFGDspnqaTAYVLFY 299
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.85e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 140.70 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLTYTPPLANYLLSkEHSRSCHQSGFCMICVMQNHIIQAFANTANAIKPVSFIRDLKkiARHFR 202
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS-LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASR--PPWFT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 203 FGSQEDAHEFLRYTIDamqkaclngypKLDrqtqatTLVHQIFGGYLRSRVKCSICKSVSDTYD--PYLDIALeirqaAN 280
Cdd:cd02664 78 PGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF-----PS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 281 IVRALELFVKPDVLSGENAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLN--IRPY 354
Cdd:cd02664 136 VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSlpVRVE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 355 MSQS----------SGD-------PVMYGLYAVLVHSGYSCHAGHYYCYV---------------------KASNGQWYQ 396
Cdd:cd02664 216 SKSSesplekkeeeSGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYL 295
|
330 340 350
....*....|....*....|....*....|.
gi 770478837 397 MNDSMVHSSNIKVVLN-------QQAYVLFY 420
Cdd:cd02664 296 FNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-402 |
2.41e-35 |
|
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: 137.55 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLTYTPPLANYLLSkehsrschqsgfcmiCVMQNHIIQAFANTANAIKPVSFIRDLKKIARHFR 202
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 203 FGS-------------------QEDAHEFLRYTIDAMQkACLNGYPKLDrqtqATTLVHQIFGGYLRSRVKCSICKSVSD 263
Cdd:cd02668 66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-AKLSKSKNPD----LKNIVQDLFRGEYSYVTQCSKCGRESS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 264 TYDPYLDIALEIRQAANIVRALELFVKPDVLSGENAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFA----NFSGGKI 339
Cdd:cd02668 141 LPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKKKL 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 770478837 340 TKDVGYPEFLNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSMV 402
Cdd:cd02668 221 NASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
123-423 |
2.10e-27 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 113.36 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLT-YTPPLANYL--LSKEHSrschqsgfcmicVMQNHIIQAFA--NTANAIKPVSFIRDLK-- 195
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddLSKELK------------VLKNVIRKPEPdlNQEEALKLFTALWSSKeh 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 196 KIARHFRFGSQEDAHEFLRYTIDAMqkaclngypKLDRQTQATTLVHQIFGGYlrsrvKCSICKSVSDTYdpyldIALEI 275
Cdd:COG5533 69 KVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDK-----KKTSTGDWFDII-----IELPD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 276 RQAANIVRALELFVK------PD---VLSGENAYMCAKCKKKVPATKRftvhRTSNVLTLSLKRFANFSGG-KITKDVGY 345
Cdd:COG5533 130 QTWVNNLKTLQEFIDnmeelvDDetgVKAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 346 PEFLNIRPymSQSSGD--PVMYGLYAVLVHSGySCHAGHYYCYVKaSNGQWYQMNDSMVHSSNIKVVLN---QQAYVLFY 420
Cdd:COG5533 206 KFELPVKH--DQILNIvkETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFY 281
|
...
gi 770478837 421 LRI 423
Cdd:COG5533 282 ERI 284
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
3.21e-26 |
|
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: 110.49 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLTYTPPLANYLLSKEHS--------RSCHQSGFCMI--------CVMQNHIIQAFANTANAIK 186
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKfpsdvvdpANDLNCQLIKLadgllsgrYSKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 187 PVSFIRDLKKIARHFRFGSQEDAHEFLRYTIDAMQKAClngypKLDRQTQATTLvhqiFGGYLRSRVKCSICKSVSDTYD 266
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES-----FKNLGLNPNDL----FKFMIEDRLECLSCKKVKYTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 267 ---------PYLDIA-----LEIRQAANIVRALELFVKPDVLsgenAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFA 332
Cdd:cd02658 152 lseilslpvPKDEATekeegELVYEPVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 333 NFSGG---KITKDVGYPEFLnirpymsqssgDPVMYGLYAVLVHSGYSCHAGHYYCYVK---ASNGQWYQMNDSmvhssn 406
Cdd:cd02658 228 LLENWvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDE------ 290
|
330 340
....*....|....*....|.
gi 770478837 407 iKVVLNQQ-------AYVLFY 420
Cdd:cd02658 291 -KVVASQDppemkklGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
122-420 |
4.36e-25 |
|
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: 107.67 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 122 AGLHNLGNTCFLNSTVQCLTYTPPLAN---YLLSKEHSRSCHQSGFcmicvMQNHiiQAFANTANAIKPVSFIRDLKKIA 198
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSF-----LLNP--EKYNDELANQAPRRLLNALREVN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 199 RHFRFGSQEDAHEFLRYTIDAMQKaclngypkldrqtqattLVHQIFGGYLRSRVKCSICKSVSDTYDPYLDIALEIRQA 278
Cdd:cd02671 98 PMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 279 -------------------ANIVRALELFVKPDVLSGENAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFANFS---- 335
Cdd:cd02671 161 elskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 336 --GG--KITKDVGYPEFLNIRPYMSQSSGDpvMYGLYAVLVHSGYSCHAGHYYCYVKasngqWYQMNDSMVHSSNIKVVL 411
Cdd:cd02671 241 cyGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFL 313
|
330
....*....|....*...
gi 770478837 412 N---------QQAYVLFY 420
Cdd:cd02671 314 EalspntsstSTPYLLFY 331
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
123-422 |
3.08e-24 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 110.35 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLTYTPPLAN--YLLSKEHSRSCHQSGFcmicVMQnhiiQAFANTANAIKPVsfirDLKKIARH 200
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSVAL----ALQ----RLFYNLQTGEEPV----DTTELTRS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 201 FRFGS-----QEDAHEFLRYTIDAMQKAClngypkldRQTQATTLVHQIFGGYLRSRVKCSICKSVSDTYDPYLDIALEI 275
Cdd:COG5077 263 FGWDSddsfmQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 276 RQAANIVRALELFVKPDVLSGENAYMCAKcKKKVPATKRFTVHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFLNI 351
Cdd:COG5077 335 KGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 352 RPYMS----QSSGDPVMYGLYAVLVHSGySCHAGHYYCYVKAS-NGQWYQMNDSMVHSSNIKVVLNQ------------- 413
Cdd:COG5077 414 LPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkir 492
|
330
....*....|....*...
gi 770478837 414 ---------QAYVLFYLR 422
Cdd:COG5077 493 dhsgikrfmSAYMLVYLR 510
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-402 |
2.35e-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: 90.08 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLTYTPPLANYLLSKEHSRSCHQSGFCMICVMQNHIIQAFANTANAIKPVSFIRDLKKIARHF- 201
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQFa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 202 ---RFG--SQEDAHEFLRYTIDAMQKaclngypKLDRQTQATTLVHQIFGGYLRSRVKC---SICKSVSDTYDPYLDIAL 273
Cdd:cd02657 81 ekqNQGgyAQQDAEECWSQLLSVLSQ-------KLPGAGSKGSFIDQLFGIELETKMKCtesPDEEEVSTESEYKLQCHI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 274 EIRQaanIVRALElfvkpdvlSGENAYMCAKCKKKVPATKRFTVH-RTSNV------LTLSLKRF-----ANfSGGKITK 341
Cdd:cd02657 154 SITT---EVNYLQ--------DGLKKGLEEEIEKHSPTLGRDAIYtKTSRIsrlpkyLTVQFVRFfwkrdIQ-KKAKILR 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 770478837 342 DVGYPEFLNIRPYMSQSSgdpvMYGLYAVLVHSGYSCHAGHYYCYVKASN-GQWYQMNDSMV 402
Cdd:cd02657 222 KVKFPFELDLYELCTPSG----YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKV 279
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
5.90e-18 |
|
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: 84.34 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNStvqcltytpplanyllskehsrschqsgfcmicvmqnhIIQAFAntanAIKpvSFIRDLKkiarhfR 202
Cdd:cd02662 1 GLVNLGNTCFMNS--------------------------------------VLQALA----SLP--SLIEYLE------E 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 203 FGSQEDAHEFLRYTIDAMQKACLNgyPkldrqtqattlvhqiFGGYLRSRVKCSICKSVS-DTYDPYLDIALEIRQA--- 278
Cdd:cd02662 31 FLEQQDAHELFQVLLETLEQLLKF--P---------------FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQssg 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 279 --ANIVRALELFVKPDVLSGenaYMCAKCKKKVPATKRftvhrtsnVLTLSLKRFAnFSG-GKITKD---VGYPEFLNir 352
Cdd:cd02662 94 sgTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ--------ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 353 pymsqssgdPVMYGLYAVLVHSGySCHAGHYYCYVKAS---------------------NGQWYQMNDS---MVHSSNik 408
Cdd:cd02662 160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTtvkEVSESE-- 227
|
330
....*....|..
gi 770478837 409 VVLNQQAYVLFY 420
Cdd:cd02662 228 VLEQKSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
285-422 |
7.83e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 86.09 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 285 LELFVKPDVLSGENAYMCAKCKKKVPATKRFTVHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQSSGD 361
Cdd:COG5560 681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 770478837 362 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSMVHSSNIKVVLNQQAYVLFYLR 422
Cdd:COG5560 761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
123-275 |
8.83e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 85.71 E-value: 8.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 123 GLHNLGNTCFLNSTVQCLTYTPPLANYLLSKEHSRSCHQSGFCmicVMQNHIIQAFAN------TAN--AIKPVSFIRDL 194
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPL---GMHGSVASAYADlikqlyDGNlhAFTPSGFKKTI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 195 KKIARHFRFGSQEDAHEFLRYTIDAMQKAcLNG------------YPKLDRQTQAT-------------TLVHQIFGGYL 249
Cdd:COG5560 344 GSFNEEFSGYDQQDSQEFIAFLLDGLHED-LNRiikkpytskpdlSPGDDVVVKKKakecwwehlkrndSIITDLFQGMY 422
|
170 180
....*....|....*....|....*.
gi 770478837 250 RSRVKCSICKSVSDTYDPYLDIALEI 275
Cdd:COG5560 423 KSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
122-402 |
1.11e-15 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 79.24 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 122 AGLHNLGNTCFLNSTVQCLTYTPPLANYLLSkeHSRSCHQSGFCMIC-------VMQNhiiqafANTANaIKPVSFIRDL 194
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCelgflfdMLEK------AKGKN-CQASNFLRAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 195 KKIARHFRFGSQEDAHE-------------FLRYTIDAMQKACLNGYPKLdrqTQATTLVHQIFGGYLRSRVKCSICKSV 261
Cdd:pfam13423 72 SSIPEASALGLLDEDREtnsaislssliqsFNRFLLDQLSSEENSTPPNP---SPAESPLEQLFGIDAETTIRCSNCGHE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 262 SDTYDPYLDIALEIRQAA----------NIVRALELFVKPDVLSgeNAyMCAKCKKKVPATKRFTVHRTSNVLTLSLKRF 331
Cdd:pfam13423 149 SVRESSTHVLDLIYPRKPssnnkkppnqTFSSILKSSLERETTT--KA-WCEKCKRYQPLESRRTVRNLPPVLSLNAALT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 332 aNFSGGKITKDVGY-PEFLNIRPYM-SQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASN--------GQWYQMNDSM 401
Cdd:pfam13423 226 -NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYLFNDFL 304
|
.
gi 770478837 402 V 402
Cdd:pfam13423 305 V 305
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-399 |
9.07e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 68.50 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 116 RVYRVG-AGLHNLGNTCFLNSTVQCLTYTPPLANYLLSKEHSRSCHQSGFcmicvmqnHIIQAFAN------TANAIK-- 186
Cdd:cd02669 113 KPYLPGfVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKS--------ELVKRLSElirkiwNPRNFKgh 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 187 --PVSFIRDLKKI-ARHFRFGSQEDAHEFLRYTIDAMqKACLNGYPKldrqtQATTLVHQIFGGYLR------------- 250
Cdd:cd02669 185 vsPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeee 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 251 ----SRVKCSICKSVSDTydPYLDIALEIRQAA--------NIVRALELFvkpDVLSGENAYMCAKCKKKVpatKRFTVH 318
Cdd:cd02669 259 gskdKFFKDSRVKKTSVS--PFLLLTLDLPPPPlfkdgneeNIIPQVPLK---QLLKKYDGKTETELKDSL---KRYLIS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 319 RTSNVLTLSLKRF--ANFSGGKITKDVGYP-EFLNIRPYMSQ---SSGDPVMYGLYAVLVHSGYSCHAGHYYCYV-KASN 391
Cdd:cd02669 331 RLPKYLIFHIKRFskNNFFKEKNPTIVNFPiKNLDLSDYVHFdkpSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKST 410
|
....*...
gi 770478837 392 GQWYQMND 399
Cdd:cd02669 411 NKWFEIQD 418
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
124-420 |
9.89e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 54.46 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 124 LHNLGNTCFLNSTVQCLTYTpplanyllskehsrschqsgfcmicvmqNHIIQAFANTanaikpvsfirdlkkiarhfrf 203
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSI----------------------------GKINTEFDND---------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 204 gSQEDAHEFLRYTI----DAMQKACLNGYPKLDRQTQATTLvhQIFGGYLRSRVKCSICKSVSDTYDPYLDIALEIRQaa 279
Cdd:cd02673 32 -DQQDAHEFLLTLLeaidDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMID-- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 280 NIVRALELFVKPDVLSGENAYMCAKCKKKVPAT-KRFTvhRTSNVLTLSLKRF-ANFSGGKITKDVgypeflniRPYMSQ 357
Cdd:cd02673 107 NKLDIDELLISNFKTWSPIEKDCSSCKCESAISsERIM--TFPECLSINLKRYkLRIATSDYLKKN--------EEIMKK 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 770478837 358 SSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSMVHSSNIKVVLNQ---QAYVLFY 420
Cdd:cd02673 177 YCGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
423-743 |
2.86e-05 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 48.03 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 423 IPEKKNTDAKQNMVHSGRTNMTPEQLKKSTLNGPLSSPQVTKKLDPAQLRKIQSVDGGlGVPVARNCSGLQSPKLSNGTS 502
Cdd:pfam17823 47 VPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPHGTDLSEPATRE-GAADGAASRALAAAASSSPSS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 503 NSHALLKPASGPslieePLKKVKKPTAQPHSRSSTPAPSSGLHKTNSKQLPSSTSLKSLSDSSSADTSSSSESRESVGTR 582
Cdd:pfam17823 126 AAQSLPAAIAAL-----PSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAAS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 583 SAPagdpsSVNSPASPAkSTEEQKKLKPQALTNVTSEPISTMSPPPAKRLALSAKKASVRQ-SLSSSTEARPPSSFHLSS 661
Cdd:pfam17823 201 SAP-----ATLTPARGI-STAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATlAAAAGTVASAAGTINMGD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 662 DPTHFLSPASLHPHHRFSPHSLSLQSP----PSAHLSKD---LSPLKRPS-----STLEPLAPALSPQTNGHQPHSSprP 729
Cdd:pfam17823 275 PHARRLSPAKHMPSDTMARNPAAPMGAqaqgPIIQVSTDqpvHNTAGEPTpspsnTTLEPNTPKSVASTNLAVVTTT--K 352
|
330
....*....|....
gi 770478837 730 IQSQNLSASTTPLL 743
Cdd:pfam17823 353 AQAKEPSASPVPVL 366
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
591-727 |
9.19e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 46.68 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 591 SVNSP---ASPAKSTEEQKKLKPQALTNVTSEPISTMSPPPAKRLAlsakkasvrqslSSSTEARPPSSFHLSSDPTHFL 667
Cdd:pfam03154 147 SIPSPqdnESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTT------------QAATAGPTPSAPSVPPQGSPAT 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 668 SPASLHPHHRFSPHSLsLQSPPSAHLSKdlspLKRPSSTLEPLAPALSPQTNGHQPHSSP 727
Cdd:pfam03154 215 SQPPNQTQSTAAPHTL-IQQTPTLHPQR----LPSPHPPLQPMTQPPPPSQVSPQPLPQP 269
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
203-421 |
1.08e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 44.86 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 203 FGSQEDAHEFLRYTIDAMQKA-------------CLNGYPKLDRQTQATTLVHqiFGGYLRsrvKCSICKSVSDTYDPY- 268
Cdd:cd02665 19 FSQQQDVSEFTHLLLDWLEDAfqaaaeaispgekSKNPMVQLFYGTFLTEGVL--EGKPFC---NCETFGQYPLQVNGYg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 269 -LDIALEirqAANI-VRALELFVKPDVLSG-ENAYMcakckkKVPAtkrftvhrtsnVLTLSLKRFA--NFSGGKITKDV 343
Cdd:cd02665 94 nLHECLE---AAMFeGEVELLPSDHSVKSGqERWFT------ELPP-----------VLTFELSRFEfnQGRPEKIHDKL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 344 GYPEFLNIRPYMsqssgdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMNDSMVHSSNIKVV--------LNQQ 414
Cdd:cd02665 154 EFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVerdsfgggRNPS 221
|
....*..
gi 770478837 415 AYVLFYL 421
Cdd:cd02665 222 AYCLMYI 228
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
583-746 |
2.73e-04 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 45.04 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 583 SAPAGDP----SSVNSPASPAKST--EEQKKLK-PQALTNVTSEPISTMSPPPAKRLALSAKKASVRQSLSSSTEARPPS 655
Cdd:PHA03377 692 SVDAGRAqpseESHLSSMSPTQPIshEEQPRYEdPDDPLDLSLHPDQAPPPSHQAPYSGHEEPQAQQAPYPGYWEPRPPQ 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 656 SFHLS--SDPTHFLSPASL------------HPHHRFS----------PHSLSLQSPPSAHLSKDLSPLKRPSSTLEPLA 711
Cdd:PHA03377 772 APYLGyqEPQAQGVQVSSYpgyagpwglraqHPRYRHSwaywsqypghGHPQGPWAPRPPHLPPQWDGSAGHGQDQVSQF 851
|
170 180 190
....*....|....*....|....*....|....*..
gi 770478837 712 PALSPQTNGHQPHSS--PRPIQSQNLSASTTPLLASP 746
Cdd:PHA03377 852 PHLQSETGPPRLQLSqvPQLPYSQTLVSSSAPSWSSP 888
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
508-773 |
4.76e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 508 LKPASGP-SLIEEPLKKVKKPTAQPHSRSS-TPAPSSglhkTNSKQLPSSTSLKSLSDSSSADTSSSSESRESVGTRSAP 585
Cdd:PHA03247 2688 ARPTVGSlTSLADPPPPPPTPEPAPHALVSaTPLPPG----PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT 2763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 586 AGDPSSVnSPASPAKSTEEQKKLKPQALTNVTSEPISTMSPPPAKRLALSAKKASVRQSLS-SSTEARPPSSFHLSSDPT 664
Cdd:PHA03247 2764 AGPPAPA-PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpAGPLPPPTSAQPTAPPPP 2842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 665 HFLSPASLHPHHRFSPHS-LSLQSPPSAHLSKDLSPLKRPSSTLEPLAPALSPQTNGHQPHSSPRPIQ--SQNLSASTTP 741
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAPGGdVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQpqAPPPPQPQPQ 2922
|
250 260 270
....*....|....*....|....*....|..
gi 770478837 742 LLASPVVKNKKKKLKRSHSEVEQEYLTASAPE 773
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
588-729 |
1.17e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 588 DPSSVNSPASPAKSTEEQKKLKPQALTNVTSEPISTMSPPPAKRLALSAKKASVRQSLSSSTEARPPSSFHLSSDPTHFL 667
Cdd:PHA03307 760 NPSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPP 839
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 770478837 668 SPASLHPHHRFSPHSLSLQSPP----SAHLSKDLSPLKRPSSTLEPLAPALSPQTNGHQPHSSPRP 729
Cdd:PHA03307 840 GAAARPPPARSSESSKSKPAAAggraRGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRP 905
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
488-739 |
2.10e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.21 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 488 NCSGLQSPKLSNG-TSNSHA---LLKPAS-GPSLIEEPLKKVKKPTAQPHSRSSTPAPSSGLHKTNSKqlpsstslksls 562
Cdd:pfam05109 435 NTTGFAAPNTTTGlPSSTHVptnLTAPAStGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESK------------ 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 563 dsssadTSSSSESRESVGTRSAPAGDPS-SVNSPASPAKSTEEQKKLKPQALT----NVTSEPISTMSPPPAKRLALSAK 637
Cdd:pfam05109 503 ------APDMTSPTSAVTTPTPNATSPTpAVTTPTPNATSPTLGKTSPTSAVTtptpNATSPTPAVTTPTPNATIPTLGK 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 638 KASVRQSLSSSTEARPPSSFHLS---SDPTHFLSPASLHPHHRFSPHSLSLQSPPSAH--LSKDLSPLK-RPSSTLEPLA 711
Cdd:pfam05109 577 TSPTSAVTTPTPNATSPTVGETSpqaNTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHniTSSSTSSMSlRPSSISETLS 656
|
250 260
....*....|....*....|....*....
gi 770478837 712 PALSPQTNGHQP-HSSPRPIQSQNLSAST 739
Cdd:pfam05109 657 PSTSDNSTSHMPlLTSAHPTGGENITQVT 685
|
|
| Cas10_III |
cd09701 |
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ... |
888-1090 |
3.20e-03 |
|
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, inactivated palm domain and Zn-ribbon; signature gene for type III
Pssm-ID: 187832 Cd Length: 909 Bit Score: 41.64 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 888 VVKEIGDANEKTEELRKTKKKKKKRKPKDFleENERQSNGGSLHIDLRETNR----IESSEMSNADKRKPDKSKPApviv 963
Cdd:cd09701 286 VVPDLERLLDETLECAVGDEKLIEEEILKT--FNEELENEGELVITLSKASRlltsLAPEREKALENELPPIISPL---- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 964 wdSQVQDGFKSSQNHEEAEDMSGKKSCavPVCW----------DGKKSCDVVQELLKNSSDKaygtevlsWEGDP-SLIS 1032
Cdd:cd09701 360 --LFDISPATQADIPNFWENKENKGIC--PVCGlrpqgptskaEEKERCDICDERRTDRAKE--------WLHSLeETIW 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 770478837 1033 RDAVQDS--RYAknLTV----IDEW-DSEFDSgKVKKIKKYKKDRRWNGNVFQKIQ---EHRNMWSVT 1090
Cdd:cd09701 428 IDEVADKndRIA--LIVgrfdLDKWlDGELLN-SLINIIPDTNNKTENKYLFTKNPsfaRLRRIWRTT 492
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
528-746 |
3.95e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 528 TAQPHSRSSTPAPSSGLHKTNSKQLPSSTSLKSLSDSSSADTSSSSESResvGTRSAPAGDPSSVnSPASPAKSTEEQKK 607
Cdd:PHA03307 60 AACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTP---PGPSSPDPPPPTP-PPASPPPSPAPDLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770478837 608 LKPQALTNVTSEPISTMSPPPAKRLALSAKKASVRQS--LSSSTE--ARPPSS----FHLSSDPTHfLSPASLHPHHRFS 679
Cdd:PHA03307 136 EMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAalPLSSPEetARAPSSppaePPPSTPPAA-ASPRPPRRSSPIS 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 770478837 680 PHSLSLQSPPSAHLSKDLSPLKRPSSTLEPLAPALSPQTNGHQPHSSPRPIQSQNLSA------STTPLLASP 746
Cdd:PHA03307 215 ASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEAsgwngpSSRPGPASS 287
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
122-163 |
5.31e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 40.55 E-value: 5.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 770478837 122 AGLHNLGNTCFLNSTVQCLTYTPPLANYLLSKEHSRSCHQSG 163
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASD 43
|
|
| |
