|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
150-450 |
6.15e-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: 6.15e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 150 GAGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGGFCMLCLMQNHMVQAFANSGNAIKPVSFIRDLKKIARH 229
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 230 FRFGNQEDAHEFLRYTIDAMQKACLNGYAKL---DRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQ 306
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 307 AANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQ 386
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083256 387 SSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 450
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
151-449 |
1.50e-77 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 257.76 E-value: 1.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 151 AGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSC--HQGGFCMLCLMQNHMVQAFANS-GNAIKPVSFIRDLKKIA 227
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrYNKDINLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 228 RHFRFGNQEDAHEFLRYTIDAMQKAClngyaKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQA 307
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 308 ANIVR------ALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLN 379
Cdd:pfam00443 156 SAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083256 380 IRPYMSQSS----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SNGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 449
Cdd:pfam00443 236 LSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-449 |
1.81e-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: 246.90 E-value: 1.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCH--QGGFCMLCLMQNhMVQAFANSGNAiKPVSFIRDLK---KI 226
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLscSPNSCLSCAMDE-IFQEFYYSGDR-SPYGPINLLYlswKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 227 ARHFRFGNQEDAHEFLRYTIDAMQKACLNGYAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQ 306
Cdd:cd02660 80 SRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 307 AANIVRA---------------LELFVKSDVLsGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGG---KI 368
Cdd:cd02660 160 KSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 369 TKDVGYPEFLNIRPYMSQSSGDPVM---------YGLYAVLVHSGySCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVV 439
Cdd:cd02660 239 DTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEV 317
|
330
....*....|
gi 1907083256 440 LNQQAYVLFY 449
Cdd:cd02660 318 LKSQAYLLFY 327
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
152-449 |
1.84e-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: 1.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLtytpplanyllskeharschqggfcmlclmqnhmvqafansgnaikpvsfirdlkkiarhfr 231
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 232 FGNQEDAHEFLRYTIDAMQKACLNGYAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDP--YLDIALEIRQAA- 308
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPq 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 309 -NIVRALELFVKSDVLSGENAYMCaKCKKKVPASKRFTIHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYM 384
Cdd:cd02257 99 vSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083256 385 SQ------SSGDPVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVL-----NQQAYVLFY 449
Cdd:cd02257 178 SEgekdsdSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-449 |
2.09e-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: 2.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYTPPLANyLLSKeharschqggfcmlclmqnhmvqafansgnaiKPVSFIRDLKKIARHFR 231
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSE--------------------------------TPKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 232 FGNQEDAHEFLRYTIDAMQkaclngyakldrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIAL----EIRQA 307
Cdd:cd02667 48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 308 ANIVRALELFVKSDVLSGENAYMCAKCKKkvpASKRFTIHRTSNVLTLSLKRF-----ANFSggKITKDVGYPEFLNIRP 382
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 383 YMSQS-----SGDPVMYGLYAVLVHSGySCHAGHYYCYVKASN----------------------GQWYQMNDSLVHSSN 435
Cdd:cd02667 186 FCDPKcnsseDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 1907083256 436 VKVVLNQQAYVLFY 449
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-449 |
2.07e-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: 2.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLtytpplanyllskeharschqggfcmlclmqnhmvqafansgnaikpvsfirdlkkiarhfr 231
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 232 FGNQEDAHEFLRYTIDamqkaclngyaKLDRqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQAANIV 311
Cdd:cd02674 19 SADQQDAQEFLLFLLD-----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 312 RA------LELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIR 381
Cdd:cd02674 82 PKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 382 PY-MSQSSGDPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 449
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-452 |
4.70e-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: 4.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYTPPLANYLLS---KEHARSCHQGgfcmLCLMQnhmVQaFANSGNAIKPVSFIRDLKKIar 228
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQ---RL-FLFLQLSESPVKTTELTDKT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 229 hFRFG-------NQEDAHEFLRYTIDAMQKaclngyaKLdRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIA 301
Cdd:cd02659 74 -RSFGwdslntfEQHDVQEFFRVLFDKLEE-------KL-KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 302 LEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNF-----SGGKITKDVGYPE 376
Cdd:cd02659 145 VAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-EFdfetmMRIKINDRFEFPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 377 FLNIRPYMSQSSG-----------DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQ- 443
Cdd:cd02659 224 ELDMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECf 302
|
330 340 350
....*....|....*....|....*....|
gi 1907083256 444 ---------------------AYVLFYLRI 452
Cdd:cd02659 303 ggeetqktydsgprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-449 |
5.79e-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: 5.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYtpplaNYLLSkeharschqggfCMLCLMQNhMVQAFANSGnAIKPVSFIRDLKKIARHFR 231
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLT------------CLKDLFES-ISEQKKRTG-VISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 232 FGNQEDAHEFLRYTIDAMQKaCLNGYAKLDRQ----------TQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIA 301
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIAE-ILDAERKAEKAnrklnnnnnaEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 302 LEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGGKITK---DVGYPEF 377
Cdd:cd02663 141 IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRYIKlfyRVVFPLE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 378 LNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNGQWYQMND---SLVHSSNVKVVLNQ-----QAYVLFY 449
Cdd:cd02663 221 LRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDetvEKIDENAVEEFFGDspnqaTAYVLFY 299
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-449 |
1.07e-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: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSkehaRSCHQGGFCMLCLMQNHMVQAFA--NSGNAIKPVS-FIRDLKkiAR 228
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS----LNLPRLGDSQSVMKKLQLLQAHLmhTQRRAEAPPDyFLEASR--PP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 229 HFRFGNQEDAHEFLRYTIDamqkaclngyaKLDrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYD--PYLDIALeirq 306
Cdd:cd02664 75 WFTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 307 aANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLN--I 380
Cdd:cd02664 134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSlpV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 381 RPYMSQS----------SGD-------PVMYGLYAVLVHSGYSCHAGHYYCYV---------------------KASNGQ 422
Cdd:cd02664 213 RVESKSSesplekkeeeSGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKN 292
|
330 340 350
....*....|....*....|....*....|....
gi 1907083256 423 WYQMNDSLVHSSNVKVVLN-------QQAYVLFY 449
Cdd:cd02664 293 WYLFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-431 |
2.88e-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: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSkeharschqggfcmlCLMQNHMVQAFANSGNAIKPVSFIRDLKKIARHFR 231
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 232 FGN-------------------QEDAHEFLRYTIDAMQkaclngyAKLDRQT--QATTLVHQIFGGYLRSRVKCSVCKSV 290
Cdd:cd02668 66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-------AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 291 SDTYDPYLDIALEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA----NFSGG 366
Cdd:cd02668 139 SSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKK 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083256 367 KITKDVGYPEFLNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLV 431
Cdd:cd02668 219 KLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-449 |
1.94e-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: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSC----------------HQGGFCMLCLMQNHMVQAFANSGNAIK 215
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSdvvdpandlncqliklADGLLSGRYSKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 216 PVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngyaKLDRQTQATTLvhqiFGGYLRSRVKCSVCKSVSDTYD 295
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES-----FKNLGLNPNDL----FKFMIEDRLECLSCKKVKYTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 296 ---------PYLDIA-----LEIRQAANIVRALELFVKSDVLsgenAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA 361
Cdd:cd02658 152 lseilslpvPKDEATekeegELVYEPVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 362 NFSGG---KITKDVGYPEFLnirpymsqssgDPVMYGLYAVLVHSGYSCHAGHYYCYVK---ASNGQWYQMNDSLVHSSN 435
Cdd:cd02658 228 LLENWvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQ 296
|
330
....*....|....
gi 1907083256 436 VKVVLNQQAYVLFY 449
Cdd:cd02658 297 DPPEMKKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
152-452 |
4.38e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 109.51 E-value: 4.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLT-YTPPLANYLLSKEHA----RSCHQGGFCMlcLMQNHMVQAFANsgnaikpvSFIRDLKKI 226
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlKNVIRKPEPD--LNQEEALKLFTA--------LWSSKEHKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 227 ARHFRFGNQEDAHEFLRYTIDAMqkaclngyaKLDRQTQATTLVHQIFGGYLRSRVkcsvcKSVSDTYdpyldIALEIRQ 306
Cdd:COG5533 71 GWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKTST-----GDWFDII-----IELPDQT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 307 AANIVRALELFV---------KSDVLSGENAYMCAKCKKKVPASKRftihRTSNVLTLSLKRFANFSGG-KITKDVGYPE 376
Cdd:COG5533 132 WVNNLKTLQEFIdnmeelvddETGVKAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDEKF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 377 FLNIRPymSQSSGD--PVMYGLYAVLVHSGySCHAGHYYCYVKaSNGQWYQMNDSLVHSSNVKVVLN---QQAYVLFYLR 451
Cdd:COG5533 208 ELPVKH--DQILNIvkETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
|
.
gi 1907083256 452 I 452
Cdd:COG5533 284 I 284
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
152-482 |
5.10e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 113.04 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYTPPLAN--YLLSKEHARschqGGFCMLCLMQnhmvQAFANSGNAIKPV-------SFIRD 222
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVdtteltrSFGWD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 223 lkkIARHFrfgNQEDAHEFLRYTIDAMQKAClngyakldRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIAL 302
Cdd:COG5077 267 ---SDDSF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 303 EIRQAANIVRALELFVKSDVLSGENAYMCAKcKKKVPASKRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFL 378
Cdd:COG5077 333 NVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 379 NIRPYMS----QSSGDPVMYGLYAVLVHSGySCHAGHYYCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ----------- 442
Cdd:COG5077 412 DLLPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdk 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907083256 443 -----------QAYVLFYLRipgskKSPEGPVSRvgatlPSRPKVVPEHSK 482
Cdd:COG5077 491 irdhsgikrfmSAYMLVYLR-----KSMLDDLLN-----PVAAVDIPPHVE 531
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
151-449 |
1.86e-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: 105.75 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 151 AGLHNLGNTCFLNSTIQCLTYTPPLAN---YLLSKEHARSCHQGGFcmlclMQNHmvQAFANSGNAIKPVSFIRDLKKIA 227
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSF-----LLNP--EKYNDELANQAPRRLLNALREVN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 228 RHFRFGNQEDAHEFLRYTIDAMQKaclngyakldrqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQA 307
Cdd:cd02671 98 PMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 308 -------------------ANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFS---- 364
Cdd:cd02671 161 elskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 365 --GG--KITKDVGYPEFLNIRPYMSQSSGDpvMYGLYAVLVHSGYSCHAGHYYCYVKasngqWYQMNDSLVHSSNVKVVL 440
Cdd:cd02671 241 cyGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFL 313
|
330
....*....|....*...
gi 1907083256 441 N---------QQAYVLFY 449
Cdd:cd02671 314 EalspntsstSTPYLLFY 331
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-431 |
2.10e-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: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGGFCMLCLMQNHMVQAFANSGNAIKPVSFIRDLKKIARHF- 230
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQFa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 231 ---RFGN--QEDAHEFLRYTIDAMQkaclngyAKLDRQTQATTLVHQIFGGYLRSRVKC---SVCKSVSDTYDPYLDIAL 302
Cdd:cd02657 81 ekqNQGGyaQQDAEECWSQLLSVLS-------QKLPGAGSKGSFIDQLFGIELETKMKCtesPDEEEVSTESEYKLQCHI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 303 EIRQAANIVRA-LELFVK------SDVLSGENAYmcakckkkvpaSKRFTIHRTSNVLTLSLKRF-----ANfSGGKITK 370
Cdd:cd02657 154 SITTEVNYLQDgLKKGLEeeiekhSPTLGRDAIY-----------TKTSRISRLPKYLTVQFVRFfwkrdIQ-KKAKILR 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083256 371 DVGYPEFLNIRPYMSQSSgdpvMYGLYAVLVHSGYSCHAGHYYCYVKASN-GQWYQMNDSLV 431
Cdd:cd02657 222 KVKFPFELDLYELCTPSG----YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKV 279
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-449 |
3.47e-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: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTytpplanyllskeharSChqggfcmlclmqnhmvqafansgnaikpVSFIRDLKkiarhfR 231
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALA----------------SL----------------------------PSLIEYLE------E 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 232 FGNQEDAHEFLRYTIDAMQKACLNgyakldrqtqattlvhqIFGGYLRSRVKCSVCKSVS-DTYDPYLDIALEIRQA--- 307
Cdd:cd02662 31 FLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQssg 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 308 --ANIVRALELFVKSDVLSGenaYMCAKCKKKVPASKRftihrtsnVLTLSLKRFAnFSG-GKITKD---VGYPEFLNir 381
Cdd:cd02662 94 sgTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ--------ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 382 pymsqssgdPVMYGLYAVLVHSGySCHAGHYYCYVKAS---------------------NGQWYQMNDSLV-HSSNVKVV 439
Cdd:cd02662 160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVkEVSESEVL 229
|
330
....*....|
gi 1907083256 440 LNQQAYVLFY 449
Cdd:cd02662 230 EQKSAYMLFY 239
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
151-431 |
1.21e-18 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 88.10 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 151 AGLHNLGNTCFLNSTIQCLTYTPPLANYLLSkeHARSCHQGGFCMLC----LMqnHM--------VQAfANsgnaikpvs 218
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCelgfLF--DMlekakgknCQA-SN--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 219 FIRDLKKIARHFRFGNQEDAHE-------------FLRYTIDAMQKaclNGYAKLDRQTQATTLVHQIFGGYLRSRVKCS 285
Cdd:pfam13423 67 FLRALSSIPEASALGLLDEDREtnsaislssliqsFNRFLLDQLSS---EENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 286 VCKSVSDTYDPYLDIALEI-RQAANIVRALELFVKSDVL----SGENAY--MCAKCKKKVPASKRFTIHRTSNVLTLSLK 358
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYpRKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 359 RFaNFSGGKITKDVGY-PEFLNIRPYM-SQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASN--------GQWYQMND 428
Cdd:pfam13423 224 LT-NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYLFND 302
|
...
gi 1907083256 429 SLV 431
Cdd:pfam13423 303 FLV 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
152-304 |
4.71e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 86.86 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHA----RSCHQGgfcmlclMQNHMVQAFAN------SGN--AIKPVSF 219
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEesinEENPLG-------MHGSVASAYADlikqlyDGNlhAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 220 IRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNG------------YAKLDRQTQAT-------------TLVHQIF 274
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHED-LNRiikkpytskpdlSPGDDVVVKKKakecwwehlkrndSIITDLF 418
|
170 180 190
....*....|....*....|....*....|
gi 1907083256 275 GGYLRSRVKCSVCKSVSDTYDPYLDIALEI 304
Cdd:COG5560 419 QGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
314-451 |
8.95e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 85.71 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 314 LELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQSSGD 390
Cdd:COG5560 681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083256 391 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLR 451
Cdd:COG5560 761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-442 |
3.33e-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: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGGFcmlclmqnHMVQAFA-------NSgNAIK----PVSFI 220
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKS--------ELVKRLSelirkiwNP-RNFKghvsPHELL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 221 RDLKKI-ARHFRFGNQEDAHEFLRYTIDAMqKACLNGYAKldrqtQATTLVHQIFGGYLR-----------------SRV 282
Cdd:cd02669 192 QAVSKVsKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegskdKFF 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 283 KCSVCKSVSDTydPYLDIALEIRQAA--------NIVRALELFvksDVLSGENAYMCAKCKKKVpasKRFTIHRTSNVLT 354
Cdd:cd02669 266 KDSRVKKTSVS--PFLLLTLDLPPPPlfkdgneeNIIPQVPLK---QLLKKYDGKTETELKDSL---KRYLISRLPKYLI 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 355 LSLKRF--ANFSGGKITKDVGYP-EFLNIRPYMSQ---SSGDPVMYGLYAVLVHSGYSCHAGHYYCYV-KASNGQWYQMN 427
Cdd:cd02669 338 FHIKRFskNNFFKEKNPTIVNFPiKNLDLSDYVHFdkpSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQ 417
|
330
....*....|....*
gi 1907083256 428 DslvhsSNVKVVLNQ 442
Cdd:cd02669 418 D-----LNVKEVLPQ 427
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
153-449 |
5.99e-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: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 153 LHNLGNTCFLNSTIQCLTytpplanyllskeharschqggfcmlclmqnhmvqafansgnaikpvsfirDLKKIARHFRF 232
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS---------------------------------------------------SIGKINTEFDN 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 233 GNQEDAHEFLRYTI----DAMQKACLNGYAKLDRQTQATTLvhQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQaa 308
Cdd:cd02673 31 DDQQDAHEFLLTLLeaidDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMID-- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 309 NIVRALELFVKSDVLSGENAYMCAKCKKKVpASKRFTIHRTSNVLTLSLKRF-ANFSGGKITKDVgypeflniRPYMSQS 387
Cdd:cd02673 107 NKLDIDELLISNFKTWSPIEKDCSSCKCES-AISSERIMTFPECLSINLKRYkLRIATSDYLKKN--------EEIMKKY 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083256 388 SGDPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSLVH---SSNVKVVLNQQAYVLFY 449
Cdd:cd02673 178 CGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRpvsKNDVSTNARSSGYLIFY 244
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
508-1018 |
4.26e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.11 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 508 PAPEEVGVPVSRNGSLPGLKLQNGCAPAKT----PAGSPSPRLTPTPTHMPTILDEPGKKVKKSAPLQSLTTSPTTSQGS 583
Cdd:PHA03247 2593 PQSARPRAPVDDRGDPRGPAPPSPLPPDTHapdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGR 2672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 584 PGTGESRSQRPGSWASRDTIFSTSPklLAR----AITNGHRLKGEGSGVDLEKGDSSSSSPEHSASSDPAkAPQTAESRA 659
Cdd:PHA03247 2673 AAQASSPPQRPRRRAARPTVGSLTS--LADppppPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPA-PPAVPAGPA 2749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 660 AHACDSQGTNCPT---AGHPKALLNGVDAKMVKLKSPALSSTTTEPTSLMSPP-PAKKLALSAKKASTLRRATGNDIGSP 735
Cdd:PHA03247 2750 TPGGPARPARPPTtagPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLP 2829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 736 SPSAFCDlTSPMKATHPV---------VASTGPVSK---TRTAAPAPRPSTHPHSASLSSSSAKPlgTSEPQSCRPSAWT 803
Cdd:PHA03247 2830 PPTSAQP-TAPPPPPGPPppslplggsVAPGGDVRRrppSRSPAAKPAAPARPPVRRLARPAVSR--STESFALPPDQPE 2906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 804 PLPQvnghftshlHQLPEASEALHSPSKKRKKTPNGDPQRLGIDTLLPQclrGAPAAARRKRKKRCSEGEGATAPKQEGQ 883
Cdd:PHA03247 2907 RPPQ---------PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT---TDPAGAGEPSGAVPQPWLGALVPGRVAV 2974
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 884 FQDQSWSSGSQKE--EGTQPQVNGHQVSHIldsyhvssrkrRKRKRSEGLSQEATPSQDLIQHSCSPVDHSEPEARTELQ 961
Cdd:PHA03247 2975 PRFRVPQPAPSREapASSTPPLTGHSLSRV-----------SSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLF 3043
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083256 962 KKKKKKRRKRKPEPQqdeeskhPGDQRSPrPSVTPVPALSVNGHLPSDCLGLGQAPL 1018
Cdd:PHA03247 3044 DSDSERSDLEALDPL-------PPEPHDP-FAHEPDPATPEAGARESPSSQFGPPPL 3092
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-450 |
1.86e-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: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 152 GLHNLGNTCFLNSTIQCLTytpplanyllskeharSCHQGGFCMLCLMQNHMVQAFANSGNAIKPVsfirdlKKIarhfr 231
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLF----------------SQQQDVSEFTHLLLDWLEDAFQAAAEAISPG------EKS----- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 232 fgnqedaheflrytidamqkacLNGYAKLDRQTQATTLVHqiFGGYLRsrvKCSVCKSVSDTYDPY--LDIALEirqAAN 309
Cdd:cd02665 54 ----------------------KNPMVQLFYGTFLTEGVL--EGKPFC---NCETFGQYPLQVNGYgnLHECLE---AAM 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 310 IVRALELF--VKSDVLSGENAYMcakckkKVPAskrftihrtsnVLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMs 385
Cdd:cd02665 104 FEGEVELLpsDHSVKSGQERWFT------ELPP-----------VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE- 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083256 386 qssgdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMND-SLVHSSNVKVV-------LNQQAYVLFYL 450
Cdd:cd02665 166 ----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDiSVTESSWEEVErdsfgggRNPSAYCLMYI 228
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
671-836 |
8.20e-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: 46.83 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 671 PTAGHPKALLNGVDAKMVKLKSPALSSTTTEPTSlMSPPPAKKLALSAKKASTLRRATGND-IGSPSPSAFCD---LTSP 746
Cdd:pfam05109 487 PVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNA-TSPTPAVTTPTPNATSPTLGKTSPTSaVTTPTPNATSPtpaVTTP 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 747 M-KATHPVVASTGPVSKTRTAAP----------APRPSTHPHSASLSSSSakPLGTSEPQSCRPSAWTPLPQVNGHFTSH 815
Cdd:pfam05109 566 TpNATIPTLGKTSPTSAVTTPTPnatsptvgetSPQANTTNHTLGGTSST--PVVTSPPKNATSAVTTGQHNITSSSTSS 643
|
170 180
....*....|....*....|.
gi 1907083256 816 LHQLPEASEALHSPSKKRKKT 836
Cdd:pfam05109 644 MSLRPSSISETLSPSTSDNST 664
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
151-431 |
1.60e-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: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 151 AGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSchqggfcmlcLMQNHMVQAFANSGNAIKPVS------FIRDLK 224
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKA----------ELASDYPTERRIGGREVSRSElqrsnqFVYELR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 225 KIARHFRFGN----------------QEDAHEFLRYTIDAMQKA-----CLNGYAKLDRQTQATTLVHQIF-GGYLRSRV 282
Cdd:cd02666 72 SLFNDLIHSNtrsvtpskelaylalrQQDVTECIDNVLFQLEVAlepisNAFAGPDTEDDKEQSDLIKRLFsGKTKQQLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 283 KCS--VCKSVSDTYDPYLDIALEIRQAANIVR----------ALELFVKSDVL------SGENAYMCAKCKKKVPASKRF 344
Cdd:cd02666 152 PESmgNQPSVRTKTERFLSLLVDVGKKGREIVvllepkdlydALDRYFDYDSLtklpqrSQVQAQLAQPLQRELISMDRY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 345 TIHRTSNVlTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQSSG-DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQ 422
Cdd:cd02666 232 ELPSSIDD-IDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDlKSYGYRLHAVFIHRG-EASSGHYWVYIKdFEENV 309
|
....*....
gi 1907083256 423 WYQMNDSLV 431
Cdd:cd02666 310 WRKYNDETV 318
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
453-802 |
2.03e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 453 PGSKKSPEGPVSRVGATLPSRPkvvPEHSKKSPGNGVVPSPLMAKRQDSVMMRKLPaPEEVGVPVSRNGSLPGLKLQNGC 532
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPP---PERPRDDPAPGRVSRPRRARRLGRAAQASSP-PQRPRRRAARPTVGSLTSLADPP 2702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 533 APAKTPAGSPSPRLTPTPThmpTILDEPGKKVKKSAPLQSLTTSPTTSQGSPGTGESRSQR-----PGSWASRDTIFSTS 607
Cdd:PHA03247 2703 PPPPTPEPAPHALVSATPL---PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPpttagPPAPAPPAAPAAGP 2779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 608 PKLLARAITNGHRLKGEGSGVDLEKGDSSSSSPEHSASSDPAKAPQTAESRAAHACDSQGTNCPTAGHPKALLNG--VDA 685
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsvAPG 2859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 686 KMVKLKSPALSSTTTEPTSlmSPPPAKKLALSAKKASTLRRATGNDIGSPSPSafcdltsPMKATHPVVASTGPVSktrt 765
Cdd:PHA03247 2860 GDVRRRPPSRSPAAKPAAP--ARPPVRRLARPAVSRSTESFALPPDQPERPPQ-------PQAPPPPQPQPQPPPP---- 2926
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907083256 766 AAPAPRPSTHPHSASLSSSSAKPLGTSEPQSCRPSAW 802
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
508-806 |
3.14e-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: 41.48 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 508 PAPEEVGVPVSRNGSLPGLKLQNGCAPAKTPAGSPSPRLTPTPTHMPTILDEPGKKVKKSAPLQSLTTSPTTSQGSPGTG 587
Cdd:pfam17823 92 PHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 588 esrSQRPGSWASRDTIFSTSPKLLARAITnghrlkgegsgvdlekGDSSSSSPEHSASSDPAKAPQTAESRAAHACDSQG 667
Cdd:pfam17823 172 ---SPAPRTAASSTTAASSTTAASSAPTT----------------AASSAPATLTPARGISTAATATGHPAAGTALAAVG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083256 668 TNCPTAGHPKALLNGVD-AKMVKLKSPALSSTTTEPTSLMSPPPAKKLALSakkastlrRATGNDIGSPSPSAfcdltsP 746
Cdd:pfam17823 233 NSSPAAGTVTAAVGTVTpAALATLAAAAGTVASAAGTINMGDPHARRLSPA--------KHMPSDTMARNPAA------P 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083256 747 MKAThpvvaSTGPVSKTRTAAP----APRPSTHPHSASLSSSSAKPLG--------TSEPQSCRPSAwTPLP 806
Cdd:pfam17823 299 MGAQ-----AQGPIIQVSTDQPvhntAGEPTPSPSNTTLEPNTPKSVAstnlavvtTTKAQAKEPSA-SPVP 364
|
|
| |
