|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
38-299 |
4.31e-159 |
|
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: 476.38 E-value: 4.31e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 38 HAEGFCMMCTMQAHITQALSNPGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKL---DRHTQ 114
Cdd:cd02661 40 CNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 115 ATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFT 194
Cdd:cd02661 120 ETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 195 IHRSSNVLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQ 274
Cdd:cd02661 200 IHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYN 279
|
250 260
....*....|....*....|....*
gi 1622919412 275 MNDSIVSTSDIRSVLSQQAYVLFYI 299
Cdd:cd02661 280 MDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
81-299 |
3.25e-64 |
|
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: 218.51 E-value: 3.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 81 FGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI----KAA 156
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 157 QSVNKALEQFVKPEQLDGENSYKCSKCKKmVPASKRFTIHRSSNVLTLSLKRFA---NFTGGKIAKDVKYPEYLDIRPYM 233
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622919412 234 SQP------NGEPIVYVLYAVLVHTGFNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVL-----SQQAYVLFYI 299
Cdd:cd02257 178 SEGekdsdsDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
44-298 |
1.13e-61 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 213.46 E-value: 1.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 44 MMCTMQAHITQALSN-PGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKAClngsnKLDRHTQATTLVCQI 122
Cdd:pfam00443 47 LLCALRDLFKALQKNsKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 123 FGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSV------NKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIH 196
Cdd:pfam00443 122 FRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKIS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 197 RSSNVLTLSLKRFA--NFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIV----YVLYAVLVHTGfNCHAGHYFCYIKA-SN 269
Cdd:pfam00443 202 RLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyEN 280
|
250 260 270
....*....|....*....|....*....|
gi 1622919412 270 GLWYQMNDSIVSTSD-IRSVLSQQAYVLFY 298
Cdd:pfam00443 281 NRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-299 |
8.86e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 194.13 E-value: 8.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 43 CMMCTMqAHITQALSNPGDVIK--PMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVC 120
Cdd:cd02660 46 CLSCAM-DEIFQEFYYSGDRSPygPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 121 QIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIK--------AAQSVNKA-------LEQFVKPEQLdGENSYKCSKCKK 185
Cdd:cd02660 125 QTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnkstpswaLGESGVSGtptlsdcLDRFTRPEKL-GDFAYKCSGCGS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 186 MVPASKRFTIHRSSNVLTLSLKRFANFTGG---KIAKDVKYPEYLDIRPYMSQPNGEP---------IVYVLYAVLVHTG 253
Cdd:cd02660 204 TQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKIDTYVQFPLELNMTPYTSSSIGDTqdsnsldpdYTYDLFAVVVHKG 283
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622919412 254 fNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 299
Cdd:cd02660 284 -TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-299 |
1.08e-48 |
|
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: 173.24 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 81 FGNQEDAHEFLQYTVDAMqkaclngsnkldrHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI------K 154
Cdd:cd02674 19 SADQQDAQEFLLFLLDGL-------------HS----IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 155 AAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFaNFTGG---KIAKDVKYP-EYLDIR 230
Cdd:cd02674 82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622919412 231 PY-MSQPNGEPIVYVLYAVLVHTG-FNChaGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 299
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYGsLNG--GHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
82-301 |
4.50e-45 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 166.28 E-value: 4.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 82 GNQEDAHEFLQYTVDAMQkaclNGSNKLDRHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNK 161
Cdd:cd02659 84 FEQHDVQEFFRVLFDKLE----EKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 162 ALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGGKIAKD---VKYPEYLDIRPYMSQPN 237
Cdd:cd02659 156 SLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDFETMMRIKIndrFEFPLELDMEPYTEKGL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 238 G-----------EPIVYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQ------------- 292
Cdd:cd02659 236 AkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfggeetqktydsg 314
|
250
....*....|....*...
gi 1622919412 293 ---------AYVLFYIRS 301
Cdd:cd02659 315 prafkrttnAYMLFYERK 332
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
61-298 |
7.09e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 157.93 E-value: 7.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 61 DVIKP----MFviNEMRRIARHFRFGNQEDAHEFLQYTVDAMQkaclngsnkldrhtqatTLVCQIFGGYLRSRVKCLNC 136
Cdd:cd02667 26 ELLSEtpkeLF--SQVCRKAPQFKGYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 137 KGVSDTFDPYLDITL----EIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKmvpASKRFTIHRSSNVLTLSLKRF--- 209
Cdd:cd02667 87 GTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 210 --ANFTggKIAKDVKYPEYLDIRPYMSQPN-----GEPIVYVLYAVLVHTGfNCHAGHYFCYIKASN------------- 269
Cdd:cd02667 164 rsANLR--KVSRHVSFPEILDLAPFCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskp 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622919412 270 ---------GLWYQMNDSIVSTSDIRSVLSQQAYVLFY 298
Cdd:cd02667 241 aadeagpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
61-298 |
1.08e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 143.60 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 61 DVIKPMFVINEMRRIARHFRFGNQEDAHEFLQY-------TVDAMQKACL---NGSNKLDRHTQaTTLVCQIFGGYLRSR 130
Cdd:cd02663 42 GVISPKKFITRLKRENELFDNYMHQDAHEFLNFllneiaeILDAERKAEKanrKLNNNNNAEPQ-PTWVHEIFQGILTNE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 131 VKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA 210
Cdd:cd02663 121 TRCLTCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 211 nFTGG-----KIAKDVKYPEYLdiRPYMSQPNGEP--IVYVLYAVLVHTGFNCHAGHYFCYIKaSNGLWYQMNDSIVSTS 283
Cdd:cd02663 201 -YDEQlnryiKLFYRVVFPLEL--RLFNTTDDAENpdRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKI 276
|
250 260
....*....|....*....|...
gi 1622919412 284 DIRSVL--------SQQAYVLFY 298
Cdd:cd02663 277 DENAVEeffgdspnQATAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-298 |
2.76e-34 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 134.47 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 46 CTMQAHITQALSNPGDVIKPMFVINEMRRIARHFRFGN-------------------QEDAHEFLQYTVDAMQkACLNGS 106
Cdd:cd02668 31 CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-AKLSKS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 107 NKLDrhtqATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKM 186
Cdd:cd02668 110 KNPD----LKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 187 VPASKRFTIHRSSNVLTLSLKRFAnF---TGG--KIAKDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHY 261
Cdd:cd02668 186 TDATRRIRLTTLPPTLNFQLLRFV-FdrkTGAkkKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHY 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622919412 262 FCYIK-ASNGLWYQMNDSIVSTSDIRSVL---------------------SQQAYVLFY 298
Cdd:cd02668 265 IAHIKdEQTGEWYKFNDEDVEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVY 323
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-298 |
4.28e-30 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 122.60 E-value: 4.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 79 FRFGNQEDAHEFLQYTVDamqkaclngsnKLDrhtqatTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLeikAAQS 158
Cdd:cd02664 76 FTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SFPS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 159 VNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGG---KIAKDVKYPEYLD--IRPY 232
Cdd:cd02664 136 VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSlpVRVE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 233 MS----------QPNGE-------PIVYVLYAVLVHTGFNCHAGHYFCYI---------------------KASNGLWYQ 274
Cdd:cd02664 216 SKssesplekkeEESGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYL 295
|
250 260 270
....*....|....*....|....*....|.
gi 1622919412 275 MNDSIVS---TSDIRSVLS----QQAYVLFY 298
Cdd:cd02664 296 FNDSRVTfssFESVQNVTSrfpkDTPYILFY 326
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
84-300 |
3.29e-23 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 107.26 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 84 QEDAHEFLQYTVDAMQKAClngsnkldRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKAL 163
Cdd:COG5077 273 QHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 164 EQFVKPEQLDGENSYKCSKcKKMVPASKRFTIHRSSNVLTLSLKRF-ANFTGG---KIAKDVKYPEYLDIRPYMS----Q 235
Cdd:COG5077 345 RRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFLDrdadK 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 236 PNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKAS-NGLWYQMNDSIVSTSDIRSVLSQ----------------------Q 292
Cdd:COG5077 424 SENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsgikrfmS 502
|
....*...
gi 1622919412 293 AYVLFYIR 300
Cdd:COG5077 503 AYMLVYLR 510
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
158-302 |
2.08e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 97.65 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 158 SVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYP-EYLDIRPYMS 234
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622919412 235 QPNGEPIVYVLYAVLVHTGFnCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYIRSH 302
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGG-LSGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-298 |
2.35e-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 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: 93.16 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 79 FRFGNQEDAHEFLQYTVDAMQKACLNgsnkldRHTQATTlvcQIFGGYLRSRVKCLNCKGVSDTFD---------PYLDI 149
Cdd:cd02658 95 FSTMRQQDALEFLLHLIDKLDRESFK------NLGLNPN---DLFKFMIEDRLECLSCKKVKYTSElseilslpvPKDEA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 150 T-----LEIKAAQSVNKALEQFVKPEQLDgensYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA---NFTGGKIAKDV 221
Cdd:cd02658 166 TekeegELVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQlleNWVPKKLDVPI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 222 KYPEYLDIRPYMsqpngepivyvLYAVLVHTGFNCHAGHYFCYIK---ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFY 298
Cdd:cd02658 242 DVPEELGPGKYE-----------LIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
65-298 |
6.90e-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 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: 92.26 E-value: 6.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 65 PMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKaclngsnkldrhtqattLVCQIFGGYLRSRVKCLNCKGVSDTFD 144
Cdd:cd02671 86 PRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERRE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 145 PYLDIT----------------------LEIKAAQsvnKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVL 202
Cdd:cd02671 149 DFQDISvpvqeselskseesseispdpkTEMKTLK---WAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 203 TLSLKRFA------NFTGG--KIAKDVKYPEYLDIRPYMSQPNGEpiVYVLYAVLVHTGFNCHAGHYFCYIKasnglWYQ 274
Cdd:cd02671 226 TIHLKCFAangsefDCYGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLL 298
|
250 260 270
....*....|....*....|....*....|...
gi 1622919412 275 MNDS---IVSTSDIRSVLSQQA------YVLFY 298
Cdd:cd02671 299 FDDSevkVTEEKDFLEALSPNTsststpYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
80-298 |
8.98e-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: 87.04 E-value: 8.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 80 RFGNQEDAHEFLQYTVDAMQKACLNgsnkldrhtqattlvcqIFGGYLRSRVKCLNCKGVS-DTFDPYLDITLEIKAAQS 158
Cdd:cd02662 30 EFLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQSS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 159 VNKA-----LEQFVKPEQLDGensYKCSKCK-KMVPASKRFTIH--RSS-NVLTLSLKRFANftggkiakdVKYPEYLdi 229
Cdd:cd02662 93 GSGTtlehcLDDFLSTEIIDD---YKCDRCQtVIVRLPQILCIHlsRSVfDGRGTSTKNSCK---------VSFPERL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 230 RPYMsqpngepivYVLYAVLVHTGFnCHAGHYFCY--------------------IKASNGL-WYQMNDSIVSTSDIRSV 288
Cdd:cd02662 159 PKVL---------YRLRAVVVHYGS-HSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHpWWRISDTTVKEVSESEV 228
|
250
....*....|.
gi 1622919412 289 LSQ-QAYVLFY 298
Cdd:cd02662 229 LEQkSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
74-300 |
8.13e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 82.16 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 74 RIARHFRFGNQEDAHEFLQYTVDAMqkaclngsnKLDRHTQATTLVCQIFGGYLRSrvkclnckgvsdTFDPYLDITLEI 153
Cdd:COG5533 69 KVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKT------------STGDWFDIIIEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 154 KAAQSVN--KALEQFVKP--EQLD-------GENSYKCSKCKKMVPASKRftihRSSNVLTLSLKRFANFTGG-KIAKDV 221
Cdd:COG5533 128 PDQTWVNnlKTLQEFIDNmeELVDdetgvkaKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 222 KYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKaSNGLWYQMNDSIVST---SDIRSVLSQQAYVLFY 298
Cdd:COG5533 204 DEKFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPvseEEAINEKAKNAYLYFY 281
|
..
gi 1622919412 299 IR 300
Cdd:COG5533 282 ER 283
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
54-298 |
5.49e-14 |
|
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: 74.29 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 54 QALSNPGDVIKPMFVINEMRRiarHF-RFGNQEDAHEFLQytvdamQKA--CLNG-----SNKLDRHTQATTLVCQIFGG 125
Cdd:cd02657 54 DTMDKKQEPVPPIEFLQLLRM---AFpQFAEKQNQGGYAQ------QDAeeCWSQllsvlSQKLPGAGSKGSFIDQLFGI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 126 YLRSRVKCL-NCKGVSDTFDP------YLDITLEIKAAQS-VNKALEQFVK--PEQLDGENSYkcskckkmvpaSKRFTI 195
Cdd:cd02657 125 ELETKMKCTeSPDEEEVSTESeyklqcHISITTEVNYLQDgLKKGLEEEIEkhSPTLGRDAIY-----------TKTSRI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 196 HRSSNVLTLSLKRF-----ANfTGGKIAKDVKYPEYLDIRPYMSqPNGepiVYVLYAVLVHTGFNCHAGHYFCYIKASN- 269
Cdd:cd02657 194 SRLPKYLTVQFVRFfwkrdIQ-KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNd 268
|
250 260 270
....*....|....*....|....*....|....*..
gi 1622919412 270 GLWYQMND---SIVSTSDIRSvLS-----QQAYVLFY 298
Cdd:cd02657 269 GKWIKFDDdkvSEVTEEDILK-LSgggdwHIAYILLY 304
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
113-280 |
1.58e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 57.67 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 113 TQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQ-----LDGENSYK--CSKCKK 185
Cdd:pfam13423 122 SPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYPRKPSSNNKKPPNQTFSSilkssLERETTTKawCEKCKR 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 186 MVPASKRFTIHRSSNVLTLSlkrfANFTGGKIAKDVKYPEYL--DIRPYMS---QPNGEPIVYVLYAVLVHTGFNCHAGH 260
Cdd:pfam13423 202 YQPLESRRTVRNLPPVLSLN----AALTNEEWRQLWKTPGWLppEIGLTLSddlQGDNEIVKYELRGVVVHIGDSGTSGH 277
|
170 180
....*....|....*....|....*...
gi 1622919412 261 YFCYIKASN--------GLWYQMNDSIV 280
Cdd:pfam13423 278 LVSFVKVADseledpteSQWYLFNDFLV 305
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
616-839 |
2.38e-08 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 58.46 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 616 KGSTDEMSAPGAERGP--PEDGDPEPQPGSPAAESLEEPDAAAASLSSTKKAPPPPDPGTPTTKEGAWEALAAAPEEPPP 693
Cdd:PRK07764 606 SGPPEEAARPAAPAAPaaPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 694 GAGQDIAGDTAPPDLCDPGSLTGDASPLSQDAkgmIAEGPRDSATAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHArda 773
Cdd:PRK07764 686 APAAPAAPAGAAPAQPAPAPAATPPAGQADDP---AAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP--- 759
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622919412 774 qdlPQSSGAPEATEGPPAPVLEAAPAGHLEGDAEPSPGErgEDAAAPKAPGPSPVREKIGSlRKVD 839
Cdd:PRK07764 760 ---PPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDD--EDRRDAEEVAMELLEEELGA-KKIE 819
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
630-830 |
2.63e-08 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 58.46 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 630 GPPEDGDPEPQPGSPAAESLEEPDAAAASlssTKKAPPPPDPGTPTTKEGAWEALAAAPEEPPPGAGQDIAGDTAPPDLC 709
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAP---AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 710 DPGSLTGDASPLSQDAKGMIAEGPRDSATAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAqdlPQSSGAPEATEgP 789
Cdd:PRK07764 667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASA---PSPAADDPVPL-P 742
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622919412 790 PAPVLEAAPAGHLEGDAEPSPGERGEDAAAPKAPGPSPVRE 830
Cdd:PRK07764 743 PEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
515-859 |
1.26e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.49 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 515 NGIGMIASSHSPGRDAEDEEAAPHELQEPMTLNGANSADSDSDPKENGLPP----------DGASCQGQPALHSENPFAK 584
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRaarptvgsltSLADPPPPPPTPEPAPHAL 2715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 585 ANGIPGKLMPAP----LPSLPEDKILETFKFSNKLKGSTDEMSAPGAERGPPEDGDPEPQPGSPAAESLEEPDA-AAASL 659
Cdd:PHA03247 2716 VSATPLPPGPAAarqaSPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAsLSESR 2795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 660 SSTKKAPPPPDPGTPTTKEGAWEALAAAPE--EPPPGAGQDIAGDTAPPDLCDPGSLTGDASPlsqdaKGMIAEGPRDSA 737
Cdd:PHA03247 2796 ESLPSPWDPADPPAAVLAPAAALPPAASPAgpLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP-----GGDVRRRPPSRS 2870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 738 TAEAPEGlSPAPPARSeepceqplLVHPSGDHARDAQDLPQSSGAPEATEGPPAPVLEAAPAGHLEGDAEPSPGERGEDA 817
Cdd:PHA03247 2871 PAAKPAA-PARPPVRR--------LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQP 2941
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622919412 818 AAPKAPGPSPVREKIGS-----LRKVDRGHYRSRRERSSSGEPARES 859
Cdd:PHA03247 2942 PLAPTTDPAGAGEPSGAvpqpwLGALVPGRVAVPRFRVPQPAPSREA 2988
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
624-819 |
2.57e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 55.24 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 624 APGAErGPPEDGDPEPQPGSPAAESLEEPDAAAASLSSTKKAPPPPDPGTPTTKEGAWEALA---AAPEEPPPGAGQDIA 700
Cdd:PRK07003 361 AVTGG-GAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATraeAPPAAPAPPATADRG 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 701 GDTAPPDLCDPGSLTGDASPLSQDAKgMIAEGPRDSATAEAPEGLSPAPPARSEEPCEqpllVHPSGDHARDAQDLPQSS 780
Cdd:PRK07003 440 DDAADGDAPVPAKANARASADSRCDE-RDAQPPADSGSASAPASDAPPDAAFEPAPRA----AAPSAATPAAVPDARAPA 514
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622919412 781 GAPEATEgpPAPVLEAAPAGHLEGDAEPSPGERGEDAAA 819
Cdd:PRK07003 515 AASREDA--PAAAAPPAPEARPPTPAAAAPAARAGGAAA 551
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
54-298 |
2.71e-07 |
|
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: 53.30 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 54 QALSNPGDVIKpmfvinemrriarHFRFGNQEDAHEFLQYTVDAMQKAC-LNGSNKLDRHTQATTL-VCQIFGGYLRSRV 131
Cdd:cd02673 16 QALSSIGKINT-------------EFDNDDQQDAHEFLLTLLEAIDDIMqVNRTNVPPSNIEIKRLnPLEAFKYTIESSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 132 KCLNCKGVSDTFDpyLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCK-KMVPASKRFTihRSSNVLTLSLKRFA 210
Cdd:cd02673 83 VCIGCSFEENVSD--VGNFLDVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKcESAISSERIM--TFPECLSINLKRYK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 211 NFTGgkIAKDVKypeylDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKAS--NGLWYQMNDSI---VSTSDI 285
Cdd:cd02673 159 LRIA--TSDYLK-----KNEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEirpVSKNDV 231
|
250
....*....|...
gi 1622919412 286 RSVLSQQAYVLFY 298
Cdd:cd02673 232 STNARSSGYLIFY 244
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
531-834 |
4.08e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.79 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 531 EDEEAAPHELQEPMTLNGANSADSDSDpkENGLPPDGASCQGQPALHSENPFAKANGIPGKlmPAPLPSLPEDkilETFK 610
Cdd:PHA03307 12 EAAAEGGEFFPRPPATPGDAADDLLSG--SQGQLVSDSAELAAVTVVAGAAACDRFEPPTG--PPPGPGTEAP---ANES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 611 FSNKLKGSTDEMSAPGAERGPPEDGDPEPQPGSPAAESLEEPDAAAASlsstkkappppdpgtpttkeGAWEALAAAPEE 690
Cdd:PHA03307 85 RSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAP--------------------DLSEMLRPVGSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 691 PPPGAGQDIAGDTAPPDLCD---PGSLTGDASPLSQDAKGMIAEGPRDSATAEAPEGLSPAPPARSEE-----PCEQPLL 762
Cdd:PHA03307 145 GPPPAASPPAAGASPAAVASdaaSSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPisasaSSPAPAP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 763 VHPSGDHARDAQDLPQSSGAPEATEGP--------PAPV-LEAAPAGHLEGDAEPSPGERGEDAAAPKAPGPSPVREKIG 833
Cdd:PHA03307 225 GRSAADDAGASSSDSSSSESSGCGWGPenecplprPAPItLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPG 304
|
.
gi 1622919412 834 S 834
Cdd:PHA03307 305 S 305
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
621-825 |
4.37e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 51.25 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 621 EMSAPGAERGPPEDGDPEPQPgSPAAESLEEP--DAAAASLSSTKKAPPPPDPGTPTTKEgAWEALAAAPEEPPPGAGQD 698
Cdd:PRK08691 376 ELQSPSAQTAEKETAAKKPQP-RPEAETAQTPvqTASAAAMPSEGKTAGPVSNQENNDVP-PWEDAPDEAQTAAGTAQTS 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 699 IAGDTAPPDLCDPgsltgdasPLSQDAKGMIAEGPRDSATAEAPEGlSPAPPARSEEPCEQPLLVHPSGDHARDAQDLPQ 778
Cdd:PRK08691 454 AKSIQTASEAETP--------PENQVSKNKAADNETDAPLSEVPSE-NPIQATPNDEAVETETFAHEAPAEPFYGYGFPD 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622919412 779 SSGAPE-ATEGPPAPVLEAAPAGHLEG--DAEPSPGERGEDaAAPKAPGP 825
Cdd:PRK08691 525 NDCPPEdGAEIPPPDWEHAAPADTAGGgaDEEAEAGGIGGN-NTPSAPPP 573
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
581-825 |
5.07e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 51.00 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 581 PFAKANGIPGKLMPAPLP-SLPEDKILETFKFSNKLKGSTDEMSAPGAERGPPEDGDPEPQPGSPAAESLEEPDAAAASL 659
Cdd:PRK07003 360 PAVTGGGAPGGGVPARVAgAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRG 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 660 SSTKKAPPPPDPGTPTTKEGAWEALAAAPEEPPPGAGQDIAGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSATA 739
Cdd:PRK07003 440 DDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASRE 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 740 EAPEGL-SPAPPARSEEPCEQPLLVHPSG-----------------DHARDAQDLPQSSGAPEATEGPPAP---VLEAAP 798
Cdd:PRK07003 520 DAPAAAaPPAPEARPPTPAAAAPAARAGGaaaaldvlrnagmrvssDRGARAAAAAKPAAAPAAAPKPAAPrvaVQVPTP 599
|
250 260
....*....|....*....|....*...
gi 1622919412 799 -AGHLEGDAEPSPGERGEDAAAPKAPGP 825
Cdd:PRK07003 600 rARAATGDAPPNGAARAEQAAESRGAPP 627
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
631-1028 |
5.80e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.94 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 631 PPEDGDPEPQPGSPAAESLEEPDAAAASLSSTKKAPPPPDPGTPTTKEGAWEALAAAPEEPPPGAGQDIAGDTAPPD-LC 709
Cdd:PHA03307 27 TPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREgSP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 710 DPGSLTGDASPlsqdakgmiaegprdSATAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDLPQSSGAPEATEGP 789
Cdd:PHA03307 107 TPPGPSSPDPP---------------PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 790 PAPVLEAAPAghlEGDAEPSPG-ERGEDAAAPKAPGPSPVREKIGSLRKVDRGhyrsrrersssGEPARESRSKTEGHRH 868
Cdd:PHA03307 172 AALPLSSPEE---TARAPSSPPaEPPPSTPPAAASPRPPRRSSPISASASSPA-----------PAPGRSAADDAGASSS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 869 RRRRTcprerdrQDRHAAEHHPGHGDRPSPGERRSLGRYSHHHSRHRSGAEPDWVRHHYTEGEhgwgrekfyaDRPRWDR 948
Cdd:PHA03307 238 DSSSS-------ESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRE----------RSPSPSP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 949 CRYyHDRYAPYAARDWKPFHGGREHERAGLHERPHKDHSRG-RRGCEPARERERHRPGSPRAGAPHALAPHPDRFSHDRT 1027
Cdd:PHA03307 301 SSP-GSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAvSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPA 379
|
.
gi 1622919412 1028 A 1028
Cdd:PHA03307 380 A 380
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
536-827 |
9.43e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.32 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 536 APHELQEPMTlNGANSADSDSDPKENGLPPDGASCQGQPALHSENPFAKANGIPgklMPAPLPSLPEDKiletfkfsnkl 615
Cdd:PHA03247 2591 APPQSARPRA-PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPP---PTVPPPERPRDD----------- 2655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 616 kgstdemSAPGAERGPPEDGDPEPQPGSPAAESLEEPDAAAASLSSTkkAPPPPDPGTPTTKEGAWEALAAAPEEPPPGA 695
Cdd:PHA03247 2656 -------PAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSL--TSLADPPPPPPTPEPAPHALVSATPLPPGPA 2726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 696 GQDIAGDTAPPDLCDPGSLTGDASPlsqdakGMIAEGPRDSATAEAPeglSPAPPARSEEPCEQPLLVHPSGDHARDAQD 775
Cdd:PHA03247 2727 AARQASPALPAAPAPPAVPAGPATP------GGPARPARPPTTAGPP---APAPPAAPAAGPPRRLTRPAVASLSESRES 2797
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622919412 776 LPqssgAPEATEGPPAPVLEAAPAghLEGDAEPSPGERGEDAAAPKAPGPSP 827
Cdd:PHA03247 2798 LP----SPWDPADPPAAVLAPAAA--LPPAASPAGPLPPPTSAQPTAPPPPP 2843
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
623-828 |
1.45e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 49.49 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 623 SAPGAERGPPEDGDPEPQPGSPAAESLEEPDAAAASLSSTKKAPPPpdpgtpttkegAWEALAAAPEEPPPGAGQDIAGD 702
Cdd:PRK12323 383 AQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSP-----------APEALAAARQASARGPGGAPAPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 703 TAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSATAEAP--------EGLSPAPPARSEEPCEQPLLVHPSGDHARDAQ 774
Cdd:PRK12323 452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPadddpppwEELPPEFASPAPAQPDAAPAGWVAESIPDPAT 531
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622919412 775 DLPQSSGAPEATEGPPAPVleAAPAGHLEGDAEPSPGERGEDAAAPKAPGPSPV 828
Cdd:PRK12323 532 ADPDDAFETLAPAPAAAPA--PRAAAATEPVVAPRPPRASASGLPDMFDGDWPA 583
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-277 |
1.91e-05 |
|
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: 48.47 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 72 MRRIARHFRFGNQEDAHEFLQYTVDAMqKACLNGSNKldrhtQATTLVCQIFGGYLR--------------SRVKCLNCK 137
Cdd:cd02669 195 SKVSKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 138 GVSDTFD-PYLDITLEIKAA---QSVNKA--LEQfVKPEQLdgENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRF-- 209
Cdd:cd02669 269 RVKKTSVsPFLLLTLDLPPPplfKDGNEEniIPQ-VPLKQL--LKKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFsk 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622919412 210 ANFTGGKIAKDVKYP-EYLDIRPYMSQP---NGEPIVYVLYAVLVHTGFNCHAGHYFCYI-KASNGLWYQMND 277
Cdd:cd02669 346 NNFFKEKNPTIVNFPiKNLDLSDYVHFDkpsLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQD 418
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
518-863 |
2.68e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 48.63 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 518 GMIASSHSPGRDAEDEEAAPHelQEPMTLNGANSADSDSDPKENGLPPDGASCQGQPALHSENPFAKANGIPGKLMPAPL 597
Cdd:PHA03307 98 ASPAREGSPTPPGPSSPDPPP--PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 598 PSLPEDkiletfkfsnklkgSTDEMSAPGAERGPpedgDPEPQPGSPAAESLEEPDAAAASLSSTKKAPPPPDPGTPTTK 677
Cdd:PHA03307 176 LSSPEE--------------TARAPSSPPAEPPP----STPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSS 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 678 EGAwealaaapeePPPGAGQDIAGDTAPPDlcdPGSLTGDASPLSQDAKGMIAEGPRDSATAEAPEGLSPAPPARSEEPC 757
Cdd:PHA03307 238 DSS----------SSESSGCGWGPENECPL---PRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 758 EQPllvHPSGDHARDAQDLPQSSGAPEATEGPPAPVLEAAPAGHLEGDAE-----------PSPGERGEDAAAPKAPGPS 826
Cdd:PHA03307 305 SGP---APSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPspsrppppadpSSPRKRPRPSRAPSSPAAS 381
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622919412 827 PVREKIGSLRKvDRGHYRSRRERSSSGEPARESRSKT 863
Cdd:PHA03307 382 AGRPTRRRARA-AVAGRARRRDATGRFPAGRPRPSPL 417
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
690-827 |
6.53e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 47.15 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 690 EPPPGAGQDIAGDTAP--------PDLCDPGSLTGDASPLSQDAKGMIAEGPRDSATAEAPEGLSPAPPARSEEPceqpl 761
Cdd:PRK07003 359 EPAVTGGGAPGGGVPArvagavpaPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPP----- 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622919412 762 lvhPSGDHARDAQDLPQSSGAPEATEGPPapvlEAAPAghlEGDAEPSPGERGEDAAAPKAPGPSP 827
Cdd:PRK07003 434 ---ATADRGDDAADGDAPVPAKANARASA----DSRCD---ERDAQPPADSGSASAPASDAPPDAA 489
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
624-828 |
9.48e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 624 APGAERGPPEDGDPEPQPGSPAA--------------------ESLEE----------PDAAAASLSSTKKAPPPPDPGT 673
Cdd:PHA03247 2495 APDPGGGGPPDPDAPPAPSRLAPailpdepvgepvhprmltwiRGLEElasddagdppPPLPPAAPPAAPDRSVPPPRPA 2574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 674 PTTKEGAWEALAAAPEEPP-------PGAGQDIAGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSATAEAPEGLS 746
Cdd:PHA03247 2575 PRPSEPAVTSRARRPDAPPqsarpraPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRD 2654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 747 PAPPARSEEPCEQPLLVHPSGDHA------RDAqdLPQSSGAPEATEGPPAPVLEAAPAGHLEGDAEPSP----GERGED 816
Cdd:PHA03247 2655 DPAPGRVSRPRRARRLGRAAQASSppqrprRRA--ARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPpgpaAARQAS 2732
|
250
....*....|..
gi 1622919412 817 AAAPKAPGPSPV 828
Cdd:PHA03247 2733 PALPAAPAPPAV 2744
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
623-829 |
1.46e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.02 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 623 SAPGAERGPPEDGDPEPQPGSPAAESLEEPDAAAASLSSTKKAPPPPDPGTPTTKEGAWEALAAAPEEPPPGAGQDIAGD 702
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 703 TAPPdlcdpgsltgdASPLSQDAKGMIAEGPRDSATAEAPEGLSPAPPARseepceqpllvhPSGDHARDAQDLPQSSGA 782
Cdd:PRK12323 452 PAPA-----------AAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPA------------PADDDPPPWEELPPEFAS 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622919412 783 PEATEGPPAPVLEAAPAGHLEGDAEPS---PGERGEDAAAPKAPGPSPVR 829
Cdd:PRK12323 509 PAPAQPDAAPAGWVAESIPDPATADPDdafETLAPAPAAAPAPRAAAATE 558
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
693-827 |
2.34e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 45.36 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 693 PGAGQDIAGDTAPPD-LCDPGSLTGDASPLSQDAKGMIAEGPRDSATAEAPEGLSPAPPAR--SEEPCEQPLLVHPSGDh 769
Cdd:PRK07764 365 PSASDDERGLLARLErLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPaaAPQPAPAPAPAPAPPS- 443
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622919412 770 ARDAQDLPQSSGAPEATEGPPAPVLEAAPAGHLEGDAEPSPGERGEDAAAPKAPGPSP 827
Cdd:PRK07764 444 PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPA 501
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
201-299 |
3.65e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 43.32 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 201 VLTLSLKRFA--NFTGGKIAKDVKYPEYLDIRPYMsqpngepivyvLYAVLVHTGfNCHAGHYFCYI-KASNGLWYQMND 277
Cdd:cd02665 131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYND 198
|
90 100 110
....*....|....*....|....*....|
gi 1622919412 278 SIVSTSDIRSVLSQ--------QAYVLFYI 299
Cdd:cd02665 199 ISVTESSWEEVERDsfgggrnpSAYCLMYI 228
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
632-838 |
6.10e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.10 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 632 PEDGDPEPQPGSPAAESLEEPDAAAASLSSTKKAppppdpgtpttkEGAWEALAAAPEEPPPGAGQDIAGDTAPPDLCDP 711
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPA------------PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 712 GSLTGDASPLSQDAKGMIAEGPRDS-ATAEAPEGLSPAPPARSEEPceQPLLVHPSGDHARDAQDLPQSSGAPEATEGPP 790
Cdd:PRK12323 433 LAAARQASARGPGGAPAPAPAPAAApAAAARPAAAGPRPVAAAAAA--APARAAPAAAPAPADDDPPPWEELPPEFASPA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622919412 791 APVLEAAPAGhLEGDAEPSPGERGEDAAAP---KAPGPSPVREKIGSLRKV 838
Cdd:PRK12323 511 PAQPDAAPAG-WVAESIPDPATADPDDAFEtlaPAPAAAPAPRAAAATEPV 560
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
734-950 |
7.78e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.74 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 734 RDSATAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDLPQSSGAPEATEGPPAPVLEAAP--AGHLEGDAEPSPG 811
Cdd:PRK12678 58 ARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPeaAQARERRERGEAA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 812 ERGEDAAAPKAPGPSPVREKIGSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRErDRQDRHAAEHHPG 891
Cdd:PRK12678 138 RRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDR-DRRDRREQGDRRE 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622919412 892 HGDRPSPGERRSLGRYSHHHSRHRSGAEPDWVRHHYTEGEHGWGRekfyadRPRWDRCR 950
Cdd:PRK12678 217 ERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGR------RGRRFRDR 269
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
678-826 |
8.21e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.82 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 678 EGAWEALAAAPEEPPPGAGqdIAGDTAPPDLCDPGSLTGDASPlSQDAKGMIAEGPRDSATAEAPEGLSPAPPARSEEPC 757
Cdd:PRK07764 368 SDDERGLLARLERLERRLG--VAGGAGAPAAAAPSAAAAAPAA-APAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSP 444
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622919412 758 EQPLLVHPSGDHARDAQDLPQSSGAPEATEgPPAPVLEAAPAGHLEGDAEPSPgergedAAAPKAPGPS 826
Cdd:PRK07764 445 AGNAPAGGAPSPPPAAAPSAQPAPAPAAAP-EPTAAPAPAPPAAPAPAAAPAA------PAAPAAPAGA 506
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
616-828 |
1.42e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 42.61 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 616 KGSTDEMSAPGAERGPPEDGDPEPQPGSP--AAESLEEPDAAAASLSSTKKAPPPPDPGTPTTKEG----AWEALAAAPE 689
Cdd:PLN03209 345 KPVTPEAPSPPIEEEPPQPKAVVPRPLSPytAYEDLKPPTSPIPTPPSSSPASSKSVDAVAKPAEPdvvpSPGSASNVPE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 690 EPPPGAGQDIAG---------DTAPPDLCDPGSLTGDASPLSQDAK-GMIAEGPRDSATAEAPEGLSPAPPARSEEPCEQ 759
Cdd:PLN03209 425 VEPAQVEAKKTRplspyaryeDLKPPTSPSPTAPTGVSPSVSSTSSvPAVPDTAPATAATDAAAPPPANMRPLSPYAVYD 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622919412 760 PLLVHPSGDHARDAQDLPQSSGAPEATEGPPAPVLEAAPAGH-LEGDAEP-SPGERGEDAAAPKAPGPSPV 828
Cdd:PLN03209 505 DLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHhAQPKPRPlSPYTMYEDLKPPTSPTPSPV 575
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
572-841 |
1.53e-03 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 42.74 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 572 GQPALHSENPFAKANGIPGKLMPAPLPSLPEDKILETFKFSNKLKGSTDEMSAPG----AERGPPEDGDPEPQPGSPAAE 647
Cdd:COG5180 205 EVKDEAQEEPPDLTGGADHPRPEAASSPKVDPPSTSEARSRPATVDAQPEMRPPAdakeRRRAAIGDTPAAEPPGLPVLE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 648 SLEEPDAAAASLSSTKKappppdpgtPTTKEGAWEALAAAPEEPPPGAGQdiagdtapPDLCDPGSLTGDASPLSQdAKG 727
Cdd:COG5180 285 AGSEPQSDAPEAETARP---------IDVKGVASAPPATRPVRPPGGARD--------PGTPRPGQPTERPAGVPE-AAS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 728 MIAEGPRDSATaeaPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDLPQSSGAPEATEGPPAPVleaapaghlegdae 807
Cdd:COG5180 347 DAGQPPSAYPP---AEEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGD-------------- 409
|
250 260 270
....*....|....*....|....*....|....
gi 1622919412 808 psPGERGEDAAAPKAPGPSPVREKIGSLRKVDRG 841
Cdd:COG5180 410 --LVQAALDGGGRETASLGGAAGGAGQGPKADFV 441
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
682-841 |
3.43e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 41.50 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 682 EALAAAPEEPPPG--AGQDIAGD---TAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSATAEAPEGLSPAPpaRSEEP 756
Cdd:PRK13108 289 EYVVDEALEREPAelAAAAVASAasaVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTP--AVEET 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 757 CEQPLLVHPSGDHARDAQDLPQSSGAPEATE-GPPAPVLEAAPAGHLEGDAEPSPGERG---EDAAAPKAPGPSPVR-EK 831
Cdd:PRK13108 367 SEADIEREQPGDLAGQAPAAHQVDAEAASAApEEPAALASEAHDETEPEVPEKAAPIPDpakPDELAVAGPGDDPAEpDG 446
|
170
....*....|
gi 1622919412 832 IGSLRKVDRG 841
Cdd:PRK13108 447 IRRQDDFSSR 456
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
563-782 |
3.80e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 563 LPPDGASCQGQPALHSENPFAKAngIPGKLMPAPLPSLPEDKILETFKFSNKLKGSTDEMSAPGAERGPPEDGDPEPQPG 642
Cdd:PRK12323 363 FRPGQSGGGAGPATAAAAPVAQP--APAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQAS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 643 SPAAESLEEPDAAAASLSSTKKAPPPPDPGTPTTKEGAWEALAAAPEEPPPGAGQDIAGDTAPPDLCDPGSLTGDASPLS 722
Cdd:PRK12323 441 ARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAG 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 723 QDAKGMIAEGPRDsATAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDLPQSSGA 782
Cdd:PRK12323 521 WVAESIPDPATAD-PDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDG 579
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
617-920 |
3.95e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 617 GSTDEMSAPGAERGPPEDGDPEPQPGSPAAESLEEPDAAA----ASLSSTKKAPPPPDPGTPTTKEGAWEALAAAPEEPP 692
Cdd:PRK07764 388 AGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAapqpAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPA 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 693 PGAGQDIAGDTAPPdlcdPGSLTGDASPLSQDAkGMIAEGPRDSATAEAPEGLSPA-----------------PPARSEE 755
Cdd:PRK07764 468 PAPAAAPEPTAAPA----PAPPAAPAPAAAPAA-PAAPAAPAGADDAATLRERWPEilaavpkrsrktwaillPEATVLG 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 756 PCEQPL-LVHPSGDHAR------DAQDLPQS-----------------SGAPEATEGPPAPVLEAAPAGHLEGDAEPSPG 811
Cdd:PRK07764 543 VRGDTLvLGFSTGGLARrfaspgNAEVLVTAlaeelggdwqveavvgpAPGAAGGEGPPAPASSGPPEEAARPAAPAAPA 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 812 ERGEDAAAPKAPGPSPVREKIGSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAAEHHPG 891
Cdd:PRK07764 623 APAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA 702
|
330 340
....*....|....*....|....*....
gi 1622919412 892 HGDRPSPGERRSLGRYSHHHSRHRSGAEP 920
Cdd:PRK07764 703 PAPAATPPAGQADDPAAQPPQAAQGASAP 731
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-281 |
4.21e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 40.94 E-value: 4.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1622919412 241 IVYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMNDSIVS 281
Cdd:cd02666 279 YGYRLHAVFIHRG-EASSGHYWVYIKdFEENVWRKYNDETVT 319
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
730-921 |
4.31e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.43 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 730 AEGPRDSATAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDLPQSSGAPEATEGPPAPVLEAAPAGHLEGDAEPS 809
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 810 PGERGEDAAAPKAPGPSPVREKIGSLRkvDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAAEHH 889
Cdd:PRK12678 147 EGGEQPATEARADAAERTEEEERDERR--RRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGG 224
|
170 180 190
....*....|....*....|....*....|..
gi 1622919412 890 PGHGDRPSPGERRSLGRYSHHHSRHRSGAEPD 921
Cdd:PRK12678 225 DRRGRRRRRDRRDARGDDNREDRGDRDGDDGE 256
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
626-829 |
4.49e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 41.35 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 626 GAERGPP-------EDGDPEPQPGSPAAESLEEPDAAAA---SLSSTKKAPPPPDPGTPTTKEGAWEALAAAPEEPPPGa 695
Cdd:PRK14086 75 SRELGRPiriaitvDPSAGEPAPPPPHARRTSEPELPRPgrrPYEGYGGPRADDRPPGLPRQDQLPTARPAYPAYQQRP- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 696 gqdiagdtappdlcDPGSLTGDASPLS--QDAKGMIAEGPRDSATAEAPEGLSPAPPARSEEPCEQPllVHPSGDHARDA 773
Cdd:PRK14086 154 --------------EPGAWPRAADDYGwqQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQ--RRRDYDHPRPD 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622919412 774 QDLPQSsgapEATEGP-PAPvleAAPAGHLEGDAEPSPGERGEDAAAPKAPGPSPVR 829
Cdd:PRK14086 218 WDRPRR----DRTDRPePPP---GAGHVHRGGPGPPERDDAPVVPIRPSAPGPLAAQ 267
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
677-828 |
9.67e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 40.43 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 677 KEGAWEALAAAP-----------EEPPPGAGQDIagDTAPpdlcDPGSLTGDASPLSQDAkgmiAEGPRDSATAEAPEGL 745
Cdd:PHA03379 398 TERAREALEKASeptygtprppvEKPRPEVPQSL--ETAT----SHGSAQVPEPPPVHDL----EPGPLHDQHSMAPCPV 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622919412 746 SPAPPArseepceqPLLVHPSGDhardaqdlpQSSGAPEATEGPPAPVleAAPAGHLEGDAEPSPGERGEDAAAPKAPGP 825
Cdd:PHA03379 468 AQLPPG--------PLQDLEPGD---------QLPGVVQDGRPACAPV--PAPAGPIVRPWEASLSQVPGVAFAPVMPQP 528
|
...
gi 1622919412 826 SPV 828
Cdd:PHA03379 529 MPV 531
|
|
| |
