|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
121-421 |
2.60e-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: 2.60e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 121 GAGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGGFCMLCLMQNHMVQAFANSGNAIKPVSFIRDLKKIARH 200
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 201 FRFGNQEDAHEFLRYTIDAMQKACLNGYAKL---DRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQ 277
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 278 AANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQ 357
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568975997 358 SSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 421
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
122-420 |
1.19e-77 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 257.76 E-value: 1.19e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 122 AGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSC--HQGGFCMLCLMQNHMVQAFANS-GNAIKPVSFIRDLKKIA 198
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrYNKDINLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 199 RHFRFGNQEDAHEFLRYTIDAMQKAClngyaKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQA 278
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 279 ANIVR------ALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLN 350
Cdd:pfam00443 156 SAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568975997 351 IRPYMSQSS----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SNGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 420
Cdd:pfam00443 236 LSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.03e-73 |
|
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: 247.29 E-value: 1.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCH--QGGFCMLCLMQNhMVQAFANSGNAiKPVSFIRDLK---KI 197
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLscSPNSCLSCAMDE-IFQEFYYSGDR-SPYGPINLLYlswKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 198 ARHFRFGNQEDAHEFLRYTIDAMQKACLNGYAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQ 277
Cdd:cd02660 80 SRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 278 AANIVRA---------------LELFVKSDVLsGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGG---KI 339
Cdd:cd02660 160 KSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 340 TKDVGYPEFLNIRPYMSQSSGDPVM---------YGLYAVLVHSGySCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVV 410
Cdd:cd02660 239 DTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEV 317
|
330
....*....|
gi 568975997 411 LNQQAYVLFY 420
Cdd:cd02660 318 LKSQAYLLFY 327
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
123-420 |
1.60e-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: 227.37 E-value: 1.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLtytpplanyllskeharschqggfcmlclmqnhmvqafansgnaikpvsfirdlkkiarhfr 202
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 203 FGNQEDAHEFLRYTIDAMQKACLNGYAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDP--YLDIALEIRQAA- 279
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPq 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 280 -NIVRALELFVKSDVLSGENAYMCaKCKKKVPASKRFTIHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYM 355
Cdd:cd02257 99 vSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568975997 356 SQ------SSGDPVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVL-----NQQAYVLFY 420
Cdd:cd02257 178 SEgekdsdSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.83e-55 |
|
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: 194.14 E-value: 1.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYTPPLANyLLSKeharschqggfcmlclmqnhmvqafansgnaiKPVSFIRDLKKIARHFR 202
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSE--------------------------------TPKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 203 FGNQEDAHEFLRYTIDAMQkaclngyakldrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIAL----EIRQA 278
Cdd:cd02667 48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 279 ANIVRALELFVKSDVLSGENAYMCAKCKKkvpASKRFTIHRTSNVLTLSLKRF-----ANFSggKITKDVGYPEFLNIRP 353
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 354 YMSQS-----SGDPVMYGLYAVLVHSGySCHAGHYYCYVKASN----------------------GQWYQMNDSLVHSSN 406
Cdd:cd02667 186 FCDPKcnsseDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 568975997 407 VKVVLNQQAYVLFY 420
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.99e-52 |
|
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: 183.64 E-value: 1.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLtytpplanyllskeharschqggfcmlclmqnhmvqafansgnaikpvsfirdlkkiarhfr 202
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 203 FGNQEDAHEFLRYTIDamqkaclngyaKLDRqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQAANIV 282
Cdd:cd02674 19 SADQQDAQEFLLFLLD-----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 283 RA------LELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIR 352
Cdd:cd02674 82 PKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 353 PY-MSQSSGDPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 420
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-423 |
4.50e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 183.61 E-value: 4.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLS---KEHARSCHQGgfcmLCLMQnhmVQaFANSGNAIKPVSFIRDLKKIar 199
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQ---RL-FLFLQLSESPVKTTELTDKT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 200 hFRFG-------NQEDAHEFLRYTIDAMQKaclngyaKLdRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIA 272
Cdd:cd02659 74 -RSFGwdslntfEQHDVQEFFRVLFDKLEE-------KL-KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 273 LEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNF-----SGGKITKDVGYPE 347
Cdd:cd02659 145 VAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-EFdfetmMRIKINDRFEFPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 348 FLNIRPYMSQSSG-----------DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQ- 414
Cdd:cd02659 224 ELDMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECf 302
|
330 340 350
....*....|....*....|....*....|
gi 568975997 415 ---------------------AYVLFYLRI 423
Cdd:cd02659 303 ggeetqktydsgprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
5.60e-43 |
|
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: 159.01 E-value: 5.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYtpplaNYLLSkeharschqggfCMLCLMQNhMVQAFANSGnAIKPVSFIRDLKKIARHFR 202
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLT------------CLKDLFES-ISEQKKRTG-VISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 203 FGNQEDAHEFLRYTIDAMQKaCLNGYAKLDRQ----------TQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIA 272
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIAE-ILDAERKAEKAnrklnnnnnaEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 273 LEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGGKITK---DVGYPEF 348
Cdd:cd02663 141 IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRYIKlfyRVVFPLE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 349 LNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNGQWYQMND---SLVHSSNVKVVLNQ-----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 |
1.02e-37 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 144.56 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSkehaRSCHQGGFCMLCLMQNHMVQAFA--NSGNAIKPVS-FIRDLKkiAR 199
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS----LNLPRLGDSQSVMKKLQLLQAHLmhTQRRAEAPPDyFLEASR--PP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 200 HFRFGNQEDAHEFLRYTIDamqkaclngyaKLDrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYD--PYLDIALeirq 277
Cdd:cd02664 75 WFTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 278 aANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLN--I 351
Cdd:cd02664 134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSlpV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 352 RPYMSQS----------SGD-------PVMYGLYAVLVHSGYSCHAGHYYCYV---------------------KASNGQ 393
Cdd:cd02664 213 RVESKSSesplekkeeeSGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKN 292
|
330 340 350
....*....|....*....|....*....|....
gi 568975997 394 WYQMNDSLVHSSNVKVVLN-------QQAYVLFY 420
Cdd:cd02664 293 WYLFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-402 |
2.78e-37 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 143.33 E-value: 2.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSkeharschqggfcmlCLMQNHMVQAFANSGNAIKPVSFIRDLKKIARHFR 202
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 203 FGN-------------------QEDAHEFLRYTIDAMQkaclngyAKLDRQT--QATTLVHQIFGGYLRSRVKCSVCKSV 261
Cdd:cd02668 66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-------AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 262 SDTYDPYLDIALEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA----NFSGG 337
Cdd:cd02668 139 SSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKK 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568975997 338 KITKDVGYPEFLNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLV 402
Cdd:cd02668 219 KLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.88e-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: 111.26 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSC----------------HQGGFCMLCLMQNHMVQAFANSGNAIK 186
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSdvvdpandlncqliklADGLLSGRYSKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 187 PVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngyaKLDRQTQATTLvhqiFGGYLRSRVKCSVCKSVSDTYD 266
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES-----FKNLGLNPNDL----FKFMIEDRLECLSCKKVKYTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 267 ---------PYLDIA-----LEIRQAANIVRALELFVKSDVLsgenAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA 332
Cdd:cd02658 152 lseilslpvPKDEATekeegELVYEPVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 333 NFSGG---KITKDVGYPEFLnirpymsqssgDPVMYGLYAVLVHSGYSCHAGHYYCYVK---ASNGQWYQMNDSLVHSSN 406
Cdd:cd02658 228 LLENWvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQ 296
|
330
....*....|....
gi 568975997 407 VKVVLNQQAYVLFY 420
Cdd:cd02658 297 DPPEMKKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
123-423 |
4.24e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 109.51 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLT-YTPPLANYLLSKEHA----RSCHQGGFCMlcLMQNHMVQAFANsgnaikpvSFIRDLKKI 197
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlKNVIRKPEPD--LNQEEALKLFTA--------LWSSKEHKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 198 ARHFRFGNQEDAHEFLRYTIDAMqkaclngyaKLDRQTQATTLVHQIFGGYLRSRVkcsvcKSVSDTYdpyldIALEIRQ 277
Cdd:COG5533 71 GWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKTST-----GDWFDII-----IELPDQT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 278 AANIVRALELFV---------KSDVLSGENAYMCAKCKKKVPASKRftihRTSNVLTLSLKRFANFSGG-KITKDVGYPE 347
Cdd:COG5533 132 WVNNLKTLQEFIdnmeelvddETGVKAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDEKF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 348 FLNIRPymSQSSGD--PVMYGLYAVLVHSGySCHAGHYYCYVKaSNGQWYQMNDSLVHSSNVKVVLN---QQAYVLFYLR 422
Cdd:COG5533 208 ELPVKH--DQILNIvkETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
|
.
gi 568975997 423 I 423
Cdd:COG5533 284 I 284
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
123-453 |
4.87e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 113.04 E-value: 4.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYTPPLAN--YLLSKEHARschqGGFCMLCLMQnhmvQAFANSGNAIKPV-------SFIRD 193
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVdtteltrSFGWD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 194 lkkIARHFrfgNQEDAHEFLRYTIDAMQKAClngyakldRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIAL 273
Cdd:COG5077 267 ---SDDSF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 274 EIRQAANIVRALELFVKSDVLSGENAYMCAKcKKKVPASKRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFL 349
Cdd:COG5077 333 NVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 350 NIRPYMS----QSSGDPVMYGLYAVLVHSGySCHAGHYYCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ----------- 413
Cdd:COG5077 412 DLLPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdk 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568975997 414 -----------QAYVLFYLRipgskKSPEGPVSRvgatlPSRPKVVPEHSK 453
Cdd:COG5077 491 irdhsgikrfmSAYMLVYLR-----KSMLDDLLN-----PVAAVDIPPHVE 531
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
122-420 |
1.51e-24 |
|
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: 106.13 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 122 AGLHNLGNTCFLNSTIQCLTYTPPLAN---YLLSKEHARSCHQGGFcmlclMQNHmvQAFANSGNAIKPVSFIRDLKKIA 198
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSF-----LLNP--EKYNDELANQAPRRLLNALREVN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 199 RHFRFGNQEDAHEFLRYTIDAMQKaclngyakldrqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQA 278
Cdd:cd02671 98 PMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 279 -------------------ANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFS---- 335
Cdd:cd02671 161 elskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 336 --GG--KITKDVGYPEFLNIRPYMSQSSGDpvMYGLYAVLVHSGYSCHAGHYYCYVKasngqWYQMNDSLVHSSNVKVVL 411
Cdd:cd02671 241 cyGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFL 313
|
330
....*....|....*...
gi 568975997 412 N---------QQAYVLFY 420
Cdd:cd02671 314 EalspntsstSTPYLLFY 331
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-402 |
2.03e-20 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 93.16 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGGFCMLCLMQNHMVQAFANSGNAIKPVSFIRDLKKIARHF- 201
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQFa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 202 ---RFGN--QEDAHEFLRYTIDAMQkaclngyAKLDRQTQATTLVHQIFGGYLRSRVKC---SVCKSVSDTYDPYLDIAL 273
Cdd:cd02657 81 ekqNQGGyaQQDAEECWSQLLSVLS-------QKLPGAGSKGSFIDQLFGIELETKMKCtesPDEEEVSTESEYKLQCHI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 274 EIRQAANIVRA-LELFVK------SDVLSGENAYmcakckkkvpaSKRFTIHRTSNVLTLSLKRF-----ANfSGGKITK 341
Cdd:cd02657 154 SITTEVNYLQDgLKKGLEeeiekhSPTLGRDAIY-----------TKTSRISRLPKYLTVQFVRFfwkrdIQ-KKAKILR 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975997 342 DVGYPEFLNIRPYMSQSSgdpvMYGLYAVLVHSGYSCHAGHYYCYVKASN-GQWYQMNDSLV 402
Cdd:cd02657 222 KVKFPFELDLYELCTPSG----YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKV 279
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
3.36e-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 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: 88.19 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTytpplanyllskeharSChqggfcmlclmqnhmvqafansgnaikpVSFIRDLKkiarhfR 202
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALA----------------SL----------------------------PSLIEYLE------E 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 203 FGNQEDAHEFLRYTIDAMQKACLNgyakldrqtqattlvhqIFGGYLRSRVKCSVCKSVS-DTYDPYLDIALEIRQA--- 278
Cdd:cd02662 31 FLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQssg 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 279 --ANIVRALELFVKSDVLSGenaYMCAKCKKKVPASKRftihrtsnVLTLSLKRFAnFSG-GKITKD---VGYPEFLNir 352
Cdd:cd02662 94 sgTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ--------ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 353 pymsqssgdPVMYGLYAVLVHSGySCHAGHYYCYVKAS---------------------NGQWYQMNDSLV-HSSNVKVV 410
Cdd:cd02662 160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVkEVSESEVL 229
|
330
....*....|
gi 568975997 411 LNQQAYVLFY 420
Cdd:cd02662 230 EQKSAYMLFY 239
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
122-402 |
1.17e-18 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 88.10 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 122 AGLHNLGNTCFLNSTIQCLTYTPPLANYLLSkeHARSCHQGGFCMLC----LMqnHM--------VQAfANsgnaikpvs 189
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCelgfLF--DMlekakgknCQA-SN--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 190 FIRDLKKIARHFRFGNQEDAHE-------------FLRYTIDAMQKaclNGYAKLDRQTQATTLVHQIFGGYLRSRVKCS 256
Cdd:pfam13423 67 FLRALSSIPEASALGLLDEDREtnsaislssliqsFNRFLLDQLSS---EENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 257 VCKSVSDTYDPYLDIALEI-RQAANIVRALELFVKSDVL----SGENAY--MCAKCKKKVPASKRFTIHRTSNVLTLSLK 329
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYpRKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 330 RFaNFSGGKITKDVGY-PEFLNIRPYM-SQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASN--------GQWYQMND 399
Cdd:pfam13423 224 LT-NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYLFND 302
|
...
gi 568975997 400 SLV 402
Cdd:pfam13423 303 FLV 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
123-275 |
4.53e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 86.86 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHA----RSCHQGgfcmlclMQNHMVQAFAN------SGN--AIKPVSF 190
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEesinEENPLG-------MHGSVASAYADlikqlyDGNlhAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 191 IRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNG------------YAKLDRQTQAT-------------TLVHQIF 245
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHED-LNRiikkpytskpdlSPGDDVVVKKKakecwwehlkrndSIITDLF 418
|
170 180 190
....*....|....*....|....*....|
gi 568975997 246 GGYLRSRVKCSVCKSVSDTYDPYLDIALEI 275
Cdd:COG5560 419 QGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
285-422 |
8.61e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 85.71 E-value: 8.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 285 LELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQSSGD 361
Cdd:COG5560 681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975997 362 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLR 422
Cdd:COG5560 761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-413 |
3.21e-13 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 73.12 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGGFcmlclmqnHMVQAFA-------NSgNAIK----PVSFI 191
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKS--------ELVKRLSelirkiwNP-RNFKghvsPHELL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 192 RDLKKI-ARHFRFGNQEDAHEFLRYTIDAMqKACLNGYAKldrqtQATTLVHQIFGGYLR-----------------SRV 253
Cdd:cd02669 192 QAVSKVsKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegskdKFF 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 254 KCSVCKSVSDTydPYLDIALEIRQAA--------NIVRALELFvksDVLSGENAYMCAKCKKKVpasKRFTIHRTSNVLT 325
Cdd:cd02669 266 KDSRVKKTSVS--PFLLLTLDLPPPPlfkdgneeNIIPQVPLK---QLLKKYDGKTETELKDSL---KRYLISRLPKYLI 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 326 LSLKRF--ANFSGGKITKDVGYP-EFLNIRPYMSQ---SSGDPVMYGLYAVLVHSGYSCHAGHYYCYV-KASNGQWYQMN 398
Cdd:cd02669 338 FHIKRFskNNFFKEKNPTIVNFPiKNLDLSDYVHFdkpSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQ 417
|
330
....*....|....*
gi 568975997 399 DslvhsSNVKVVLNQ 413
Cdd:cd02669 418 D-----LNVKEVLPQ 427
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
124-420 |
5.81e-10 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 61.01 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 124 LHNLGNTCFLNSTIQCLTytpplanyllskeharschqggfcmlclmqnhmvqafansgnaikpvsfirDLKKIARHFRF 203
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS---------------------------------------------------SIGKINTEFDN 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 204 GNQEDAHEFLRYTI----DAMQKACLNGYAKLDRQTQATTLvhQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQaa 279
Cdd:cd02673 31 DDQQDAHEFLLTLLeaidDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMID-- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 280 NIVRALELFVKSDVLSGENAYMCAKCKKKVpASKRFTIHRTSNVLTLSLKRF-ANFSGGKITKDVgypeflniRPYMSQS 358
Cdd:cd02673 107 NKLDIDELLISNFKTWSPIEKDCSSCKCES-AISSERIMTFPECLSINLKRYkLRIATSDYLKKN--------EEIMKKY 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568975997 359 SGDPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSLVH---SSNVKVVLNQQAYVLFY 420
Cdd:cd02673 178 CGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRpvsKNDVSTNARSSGYLIFY 244
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
479-989 |
3.09e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.49 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 479 PAPEEVGVPVSRNGSLPGLKLQNGCAPAKT----PAGSPSPRLTPTPTHMPTILDEPGKKVKKSAPLQSLTTSPTTSQGS 554
Cdd:PHA03247 2593 PQSARPRAPVDDRGDPRGPAPPSPLPPDTHapdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGR 2672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 555 PGTGESRSQRPGSWASRDTIFSTSPklLAR----AITNGHRLKGEGSGVDLEKGDSSSSSPEHSASSDPAkAPQTAESRA 630
Cdd:PHA03247 2673 AAQASSPPQRPRRRAARPTVGSLTS--LADppppPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPA-PPAVPAGPA 2749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 631 AHACDSQGTNCPT---AGHPKALLNGVDAKMVKLKSPALSSTTTEPTSLMSPP-PAKKLALSAKKASTLRRATGNDIGSP 706
Cdd:PHA03247 2750 TPGGPARPARPPTtagPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLP 2829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 707 SPSAFCDlTSPMKATHPV---------VASTGPVSK---TRTAAPAPRPSTHPHSASLSSSSAKPlgTSEPQSCRPSAWT 774
Cdd:PHA03247 2830 PPTSAQP-TAPPPPPGPPppslplggsVAPGGDVRRrppSRSPAAKPAAPARPPVRRLARPAVSR--STESFALPPDQPE 2906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 775 PLPQvnghftshlHQLPEASEALHSPSKKRKKTPNGDPQRLGIDTLLPQclrGAPAAARRKRKKRCSEGEGATAPKQEGQ 854
Cdd:PHA03247 2907 RPPQ---------PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT---TDPAGAGEPSGAVPQPWLGALVPGRVAV 2974
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 855 FQDQSWSSGSQKE--EGTQPQVNGHQVSHIldsyhvssrkrRKRKRSEGLSQEATPSQDLIQHSCSPVDHSEPEARTELQ 932
Cdd:PHA03247 2975 PRFRVPQPAPSREapASSTPPLTGHSLSRV-----------SSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLF 3043
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 568975997 933 KKKKKKRRKRKPEPQqdeeskhPGDQRSPrPSVTPVPALSVNGHLPSDCLGLGQAPL 989
Cdd:PHA03247 3044 DSDSERSDLEALDPL-------PPEPHDP-FAHEPDPATPEAGARESPSSQFGPPPL 3092
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-421 |
1.81e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 50.25 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 123 GLHNLGNTCFLNSTIQCLTytpplanyllskeharSCHQGGFCMLCLMQNHMVQAFANSGNAIKPVsfirdlKKIarhfr 202
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLF----------------SQQQDVSEFTHLLLDWLEDAFQAAAEAISPG------EKS----- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 203 fgnqedaheflrytidamqkacLNGYAKLDRQTQATTLVHqiFGGYLRsrvKCSVCKSVSDTYDPY--LDIALEirqAAN 280
Cdd:cd02665 54 ----------------------KNPMVQLFYGTFLTEGVL--EGKPFC---NCETFGQYPLQVNGYgnLHECLE---AAM 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 281 IVRALELF--VKSDVLSGENAYMcakckkKVPAskrftihrtsnVLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMs 356
Cdd:cd02665 104 FEGEVELLpsDHSVKSGQERWFT------ELPP-----------VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE- 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568975997 357 qssgdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMND-SLVHSSNVKVV-------LNQQAYVLFYL 421
Cdd:cd02665 166 ----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDiSVTESSWEEVErdsfgggRNPSAYCLMYI 228
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
642-807 |
5.29e-05 |
|
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: 47.60 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 642 PTAGHPKALLNGVDAKMVKLKSPALSSTTTEPTSlMSPPPAKKLALSAKKASTLRRATGND-IGSPSPSAFCD---LTSP 717
Cdd:pfam05109 487 PVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNA-TSPTPAVTTPTPNATSPTLGKTSPTSaVTTPTPNATSPtpaVTTP 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 718 M-KATHPVVASTGPVSKTRTAAP----------APRPSTHPHSASLSSSSakPLGTSEPQSCRPSAWTPLPQVNGHFTSH 786
Cdd:pfam05109 566 TpNATIPTLGKTSPTSAVTTPTPnatsptvgetSPQANTTNHTLGGTSST--PVVTSPPKNATSAVTTGQHNITSSSTSS 643
|
170 180
....*....|....*....|.
gi 568975997 787 LHQLPEASEALHSPSKKRKKT 807
Cdd:pfam05109 644 MSLRPSSISETLSPSTSDNST 664
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
122-402 |
1.56e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 45.17 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 122 AGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSchqggfcmlcLMQNHMVQAFANSGNAIKPVS------FIRDLK 195
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKA----------ELASDYPTERRIGGREVSRSElqrsnqFVYELR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 196 KIARHFRFGN----------------QEDAHEFLRYTIDAMQKA-----CLNGYAKLDRQTQATTLVHQIF-GGYLRSRV 253
Cdd:cd02666 72 SLFNDLIHSNtrsvtpskelaylalrQQDVTECIDNVLFQLEVAlepisNAFAGPDTEDDKEQSDLIKRLFsGKTKQQLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 254 KCS--VCKSVSDTYDPYLDIALEIRQAANIVR----------ALELFVKSDVL------SGENAYMCAKCKKKVPASKRF 315
Cdd:cd02666 152 PESmgNQPSVRTKTERFLSLLVDVGKKGREIVvllepkdlydALDRYFDYDSLtklpqrSQVQAQLAQPLQRELISMDRY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 316 TIHRTSNVlTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQSSG-DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQ 393
Cdd:cd02666 232 ELPSSIDD-IDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDlKSYGYRLHAVFIHRG-EASSGHYWVYIKdFEENV 309
|
....*....
gi 568975997 394 WYQMNDSLV 402
Cdd:cd02666 310 WRKYNDETV 318
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
424-773 |
1.65e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 424 PGSKKSPEGPVSRVGATLPSRPkvvPEHSKKSPGNGVVPSPLMAKRQDSVMMRKLPaPEEVGVPVSRNGSLPGLKLQNGC 503
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPP---PERPRDDPAPGRVSRPRRARRLGRAAQASSP-PQRPRRRAARPTVGSLTSLADPP 2702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 504 APAKTPAGSPSPRLTPTPThmpTILDEPGKKVKKSAPLQSLTTSPTTSQGSPGTGESRSQR-----PGSWASRDTIFSTS 578
Cdd:PHA03247 2703 PPPPTPEPAPHALVSATPL---PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPpttagPPAPAPPAAPAAGP 2779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 579 PKLLARAITNGHRLKGEGSGVDLEKGDSSSSSPEHSASSDPAKAPQTAESRAAHACDSQGTNCPTAGHPKALLNG--VDA 656
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsvAPG 2859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 657 KMVKLKSPALSSTTTEPTSlmSPPPAKKLALSAKKASTLRRATGNDIGSPSPSafcdltsPMKATHPVVASTGPVSktrt 736
Cdd:PHA03247 2860 GDVRRRPPSRSPAAKPAAP--ARPPVRRLARPAVSRSTESFALPPDQPERPPQ-------PQAPPPPQPQPQPPPP---- 2926
|
330 340 350
....*....|....*....|....*....|....*..
gi 568975997 737 AAPAPRPSTHPHSASLSSSSAKPLGTSEPQSCRPSAW 773
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
479-777 |
2.11e-03 |
|
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: 41.87 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 479 PAPEEVGVPVSRNGSLPGLKLQNGCAPAKTPAGSPSPRLTPTPTHMPTILDEPGKKVKKSAPLQSLTTSPTTSQGSPGTG 558
Cdd:pfam17823 92 PHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 559 esrSQRPGSWASRDTIFSTSPKLLARAITnghrlkgegsgvdlekGDSSSSSPEHSASSDPAKAPQTAESRAAHACDSQG 638
Cdd:pfam17823 172 ---SPAPRTAASSTTAASSTTAASSAPTT----------------AASSAPATLTPARGISTAATATGHPAAGTALAAVG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 639 TNCPTAGHPKALLNGVD-AKMVKLKSPALSSTTTEPTSLMSPPPAKKLALSakkastlrRATGNDIGSPSPSAfcdltsP 717
Cdd:pfam17823 233 NSSPAAGTVTAAVGTVTpAALATLAAAAGTVASAAGTINMGDPHARRLSPA--------KHMPSDTMARNPAA------P 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975997 718 MKAThpvvaSTGPVSKTRTAAP----APRPSTHPHSASLSSSSAKPLG--------TSEPQSCRPSAwTPLP 777
Cdd:pfam17823 299 MGAQ-----AQGPIIQVSTDQPvhntAGEPTPSPSNTTLEPNTPKSVAstnlavvtTTKAQAKEPSA-SPVP 364
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
428-745 |
9.38e-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: 40.28 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 428 KSPEGPVSrvGATLPSRPKVVPEHSKKSPGNGVVPSPLMAkrqdsvmmrklPAPEEVGVPVSRNGSLPGLKLQNGCAPAk 507
Cdd:pfam05109 423 KAPESTTT--SPTLNTTGFAAPNTTTGLPSSTHVPTNLTA-----------PASTGPTVSTADVTSPTPAGTTSGASPV- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 508 TPagSPSPRLTPTPTHMPTiLDEPGKKVKKSAPLQS----LTTSPTTSQGSPGTGESRsqrPGSWASRDTIFSTSPKLLA 583
Cdd:pfam05109 489 TP--SPSPRDNGTESKAPD-MTSPTSAVTTPTPNATsptpAVTTPTPNATSPTLGKTS---PTSAVTTPTPNATSPTPAV 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 584 RAITNGHRLKGEGSgvdlekgdssssspehsasSDPAKAPQTAESRAAHAcdSQGTNCPTAGHPKALLNGVDAKMVKLKS 663
Cdd:pfam05109 563 TTPTPNATIPTLGK-------------------TSPTSAVTTPTPNATSP--TVGETSPQANTTNHTLGGTSSTPVVTSP 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975997 664 P--ALSSTTTEPTSLMSpppakklalSAKKASTLRRATGNDIGSPSPSAFCDLTSPM-KATHPV----VASTGPVSKT-- 734
Cdd:pfam05109 622 PknATSAVTTGQHNITS---------SSTSSMSLRPSSISETLSPSTSDNSTSHMPLlTSAHPTggenITQVTPASTSth 692
|
330
....*....|...
gi 568975997 735 --RTAAPAPRPST 745
Cdd:pfam05109 693 hvSTSSPAPRPGT 705
|
|
| |
