|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-256 |
3.96e-156 |
|
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: 467.52 E-value: 3.96e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 1 MMCTMQAHITQALSNPGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKL---DRHTQATTLVC 77
Cdd:cd02661 46 MMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 78 QIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSN 157
Cdd:cd02661 126 QIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 158 VLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIV 237
Cdd:cd02661 206 VLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKV 285
|
250
....*....|....*....
gi 2462616534 238 STSDIRSVLSQQAYVLFYI 256
Cdd:cd02661 286 SPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
38-256 |
2.95e-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: 2.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 38 FGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI----KAA 113
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 114 QSVNKALEQFVKPEQLDGENSYKCSKCKKmVPASKRFTIHRSSNVLTLSLKRFA---NFTGGKIAKDVKYPEYLDIRPYM 190
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616534 191 SQP------NGEPIVYVLYAVLVHTGFNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVL-----SQQAYVLFYI 256
Cdd:cd02257 178 SEGekdsdsDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1-255 |
1.04e-61 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 213.46 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 1 MMCTMQAHITQALSN-PGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKAClngsnKLDRHTQATTLVCQI 79
Cdd:pfam00443 47 LLCALRDLFKALQKNsKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 80 FGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSV------NKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIH 153
Cdd:pfam00443 122 FRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKIS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 154 RSSNVLTLSLKRFA--NFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIV----YVLYAVLVHTGfNCHAGHYFCYIKA-SN 226
Cdd:pfam00443 202 RLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyEN 280
|
250 260 270
....*....|....*....|....*....|
gi 2462616534 227 GLWYQMNDSIVSTSD-IRSVLSQQAYVLFY 255
Cdd:pfam00443 281 NRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
31-256 |
1.00e-53 |
|
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: 191.05 E-value: 1.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 31 RIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI 110
Cdd:cd02660 78 KHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 111 K--------AAQSVNKA-------LEQFVKPEQLdGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGG--- 172
Cdd:cd02660 158 PnkstpswaLGESGVSGtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsr 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 173 KIAKDVKYPEYLDIRPYMSQPNGEP---------IVYVLYAVLVHTGfNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIR 243
Cdd:cd02660 237 KIDTYVQFPLELNMTPYTSSSIGDTqdsnsldpdYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEE 315
|
250
....*....|...
gi 2462616534 244 SVLSQQAYVLFYI 256
Cdd:cd02660 316 EVLKSQAYLLFYH 328
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
38-256 |
1.03e-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: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 38 FGNQEDAHEFLQYTVDAMqkaclngsnkldrHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI------K 111
Cdd:cd02674 19 SADQQDAQEFLLFLLDGL-------------HS----IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 112 AAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFaNFTGG---KIAKDVKYP-EYLDIR 187
Cdd:cd02674 82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616534 188 PY-MSQPNGEPIVYVLYAVLVHTG-FNChaGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 256
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYGsLNG--GHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
39-258 |
4.31e-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: 4.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 39 GNQEDAHEFLQYTVDAMQkaclNGSNKLDRHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNK 118
Cdd:cd02659 84 FEQHDVQEFFRVLFDKLE----EKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 119 ALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGGKIAKD---VKYPEYLDIRPYMSQPN 194
Cdd:cd02659 156 SLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDFETMMRIKIndrFEFPLELDMEPYTEKGL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 195 G-----------EPIVYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQ------------- 249
Cdd:cd02659 236 AkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfggeetqktydsg 314
|
250
....*....|....*...
gi 2462616534 250 ---------AYVLFYIRS 258
Cdd:cd02659 315 prafkrttnAYMLFYERK 332
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
18-255 |
6.80e-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: 6.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 18 DVIKP----MFviNEMRRIARHFRFGNQEDAHEFLQYTVDAMQkaclngsnkldrhtqatTLVCQIFGGYLRSRVKCLNC 93
Cdd:cd02667 26 ELLSEtpkeLF--SQVCRKAPQFKGYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 94 KGVSDTFDPYLDITL----EIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKmvpASKRFTIHRSSNVLTLSLKRF--- 166
Cdd:cd02667 87 GTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 167 --ANFTggKIAKDVKYPEYLDIRPYMSQPN-----GEPIVYVLYAVLVHTGfNCHAGHYFCYIKASN------------- 226
Cdd:cd02667 164 rsANLR--KVSRHVSFPEILDLAPFCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskp 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462616534 227 ---------GLWYQMNDSIVSTSDIRSVLSQQAYVLFY 255
Cdd:cd02667 241 aadeagpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
18-255 |
1.04e-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: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 18 DVIKPMFVINEMRRIARHFRFGNQEDAHEFLQY-------TVDAMQKACL---NGSNKLDRHTQaTTLVCQIFGGYLRSR 87
Cdd:cd02663 42 GVISPKKFITRLKRENELFDNYMHQDAHEFLNFllneiaeILDAERKAEKanrKLNNNNNAEPQ-PTWVHEIFQGILTNE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 88 VKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA 167
Cdd:cd02663 121 TRCLTCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 168 nFTGG-----KIAKDVKYPEYLdiRPYMSQPNGEP--IVYVLYAVLVHTGFNCHAGHYFCYIKaSNGLWYQMNDSIVSTS 240
Cdd:cd02663 201 -YDEQlnryiKLFYRVVFPLEL--RLFNTTDDAENpdRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKI 276
|
250 260
....*....|....*....|...
gi 2462616534 241 DIRSVL--------SQQAYVLFY 255
Cdd:cd02663 277 DENAVEeffgdspnQATAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
3-255 |
2.64e-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: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 3 CTMQAHITQALSNPGDVIKPMFVINEMRRIARHFRFGN-------------------QEDAHEFLQYTVDAMQkACLNGS 63
Cdd:cd02668 31 CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-AKLSKS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 64 NKLDrhtqATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKM 143
Cdd:cd02668 110 KNPD----LKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 144 VPASKRFTIHRSSNVLTLSLKRFAnF---TGG--KIAKDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHY 218
Cdd:cd02668 186 TDATRRIRLTTLPPTLNFQLLRFV-FdrkTGAkkKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHY 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616534 219 FCYIK-ASNGLWYQMNDSIVSTSDIRSVL---------------------SQQAYVLFY 255
Cdd:cd02668 265 IAHIKdEQTGEWYKFNDEDVEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVY 323
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-255 |
4.10e-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: 4.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 36 FRFGNQEDAHEFLQYTVDamqkaclngsnKLDrhtqatTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLeikAAQS 115
Cdd:cd02664 76 FTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SFPS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 116 VNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGG---KIAKDVKYPEYLD--IRPY 189
Cdd:cd02664 136 VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSlpVRVE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 190 MS----------QPNGE-------PIVYVLYAVLVHTGFNCHAGHYFCYI---------------------KASNGLWYQ 231
Cdd:cd02664 216 SKssesplekkeEESGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYL 295
|
250 260 270
....*....|....*....|....*....|.
gi 2462616534 232 MNDSIVS---TSDIRSVLS----QQAYVLFY 255
Cdd:cd02664 296 FNDSRVTfssFESVQNVTSrfpkDTPYILFY 326
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
41-257 |
3.11e-23 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 107.26 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 41 QEDAHEFLQYTVDAMQKAClngsnkldRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKAL 120
Cdd:COG5077 273 QHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 121 EQFVKPEQLDGENSYKCSKcKKMVPASKRFTIHRSSNVLTLSLKRF-ANFTGG---KIAKDVKYPEYLDIRPYMS----Q 192
Cdd:COG5077 345 RRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFLDrdadK 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 193 PNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKAS-NGLWYQMNDSIVSTSDIRSVLSQ----------------------Q 249
Cdd:COG5077 424 SENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsgikrfmS 502
|
....*...
gi 2462616534 250 AYVLFYIR 257
Cdd:COG5077 503 AYMLVYLR 510
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
115-259 |
1.98e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 97.65 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 115 SVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYP-EYLDIRPYMS 191
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616534 192 QPNGEPIVYVLYAVLVHTGFnCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYIRSH 259
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGG-LSGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-255 |
2.25e-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: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 36 FRFGNQEDAHEFLQYTVDAMQKACLNgsnkldRHTQATTlvcQIFGGYLRSRVKCLNCKGVSDTFD---------PYLDI 106
Cdd:cd02658 95 FSTMRQQDALEFLLHLIDKLDRESFK------NLGLNPN---DLFKFMIEDRLECLSCKKVKYTSElseilslpvPKDEA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 107 T-----LEIKAAQSVNKALEQFVKPEQLDgensYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA---NFTGGKIAKDV 178
Cdd:cd02658 166 TekeegELVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQlleNWVPKKLDVPI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 179 KYPEYLDIRPYMsqpngepivyvLYAVLVHTGFNCHAGHYFCYIK---ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFY 255
Cdd:cd02658 242 DVPEELGPGKYE-----------LIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
22-255 |
9.76e-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: 91.88 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 22 PMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKaclngsnkldrhtqattLVCQIFGGYLRSRVKCLNCKGVSDTFD 101
Cdd:cd02671 86 PRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERRE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 102 PYLDIT----------------------LEIKAAQsvnKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVL 159
Cdd:cd02671 149 DFQDISvpvqeselskseesseispdpkTEMKTLK---WAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 160 TLSLKRFA------NFTGG--KIAKDVKYPEYLDIRPYMSQPNGEpiVYVLYAVLVHTGFNCHAGHYFCYIKasnglWYQ 231
Cdd:cd02671 226 TIHLKCFAangsefDCYGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLL 298
|
250 260 270
....*....|....*....|....*....|...
gi 2462616534 232 MNDS---IVSTSDIRSVLSQQA------YVLFY 255
Cdd:cd02671 299 FDDSevkVTEEKDFLEALSPNTsststpYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
37-255 |
8.63e-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: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 37 RFGNQEDAHEFLQYTVDAMQKACLNgsnkldrhtqattlvcqIFGGYLRSRVKCLNCKGVS-DTFDPYLDITLEIKAAQS 115
Cdd:cd02662 30 EFLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQSS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 116 VNKA-----LEQFVKPEQLDGensYKCSKCK-KMVPASKRFTIH--RSS-NVLTLSLKRFANftggkiakdVKYPEYLdi 186
Cdd:cd02662 93 GSGTtlehcLDDFLSTEIIDD---YKCDRCQtVIVRLPQILCIHlsRSVfDGRGTSTKNSCK---------VSFPERL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 187 RPYMsqpngepivYVLYAVLVHTGFnCHAGHYFCY--------------------IKASNGL-WYQMNDSIVSTSDIRSV 245
Cdd:cd02662 159 PKVL---------YRLRAVVVHYGS-HSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHpWWRISDTTVKEVSESEV 228
|
250
....*....|.
gi 2462616534 246 LSQ-QAYVLFY 255
Cdd:cd02662 229 LEQkSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
31-257 |
7.80e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 82.16 E-value: 7.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 31 RIARHFRFGNQEDAHEFLQYTVDAMqkaclngsnKLDRHTQATTLVCQIFGGYLRSrvkclnckgvsdTFDPYLDITLEI 110
Cdd:COG5533 69 KVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKT------------STGDWFDIIIEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 111 KAAQSVN--KALEQFVKP--EQLD-------GENSYKCSKCKKMVPASKRftihRSSNVLTLSLKRFANFTGG-KIAKDV 178
Cdd:COG5533 128 PDQTWVNnlKTLQEFIDNmeELVDdetgvkaKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 179 KYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKaSNGLWYQMNDSIVST---SDIRSVLSQQAYVLFY 255
Cdd:COG5533 204 DEKFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPvseEEAINEKAKNAYLYFY 281
|
..
gi 2462616534 256 IR 257
Cdd:COG5533 282 ER 283
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
11-255 |
5.26e-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: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 11 QALSNPGDVIKPMFVINEMRRiarHF-RFGNQEDAHEFLQytvdamQKA--CLNG-----SNKLDRHTQATTLVCQIFGG 82
Cdd:cd02657 54 DTMDKKQEPVPPIEFLQLLRM---AFpQFAEKQNQGGYAQ------QDAeeCWSQllsvlSQKLPGAGSKGSFIDQLFGI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 83 YLRSRVKCL-NCKGVSDTFDP------YLDITLEIKAAQS-VNKALEQFVK--PEQLDGENSYkcskckkmvpaSKRFTI 152
Cdd:cd02657 125 ELETKMKCTeSPDEEEVSTESeyklqcHISITTEVNYLQDgLKKGLEEEIEkhSPTLGRDAIY-----------TKTSRI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 153 HRSSNVLTLSLKRF-----ANfTGGKIAKDVKYPEYLDIRPYMSqPNGepiVYVLYAVLVHTGFNCHAGHYFCYIKASN- 226
Cdd:cd02657 194 SRLPKYLTVQFVRFfwkrdIQ-KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNd 268
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462616534 227 GLWYQMND---SIVSTSDIRSvLS-----QQAYVLFY 255
Cdd:cd02657 269 GKWIKFDDdkvSEVTEEDILK-LSgggdwHIAYILLY 304
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
581-786 |
1.10e-11 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 69.24 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 581 APGAERGPPEDRDAEPQPGSPAAESleEPDAaaglsSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTA 660
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAA--RPAA-----PAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 661 PPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPE 740
Cdd:PRK07764 662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPL 741
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462616534 741 aaerPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKE 786
Cdd:PRK07764 742 ----PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
581-775 |
2.67e-09 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 61.40 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 581 APGAERGPPEDRDAePQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPP----PSAGEDIV 656
Cdd:PRK07003 361 AVTGGGAPGGGVPA-RVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPaapaPPATADRG 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 657 GDTAPPDLCDPGSLTGDASPLSQDAKgMIAEGPRDSALAEAPEGLSPAPPARSEEPceqpllvhPSGDHARDAQDPSQSL 736
Cdd:PRK07003 440 DDAADGDAPVPAKANARASADSRCDE-RDAQPPADSGSASAPASDAPPDAAFEPAP--------RAAAPSAATPAAVPDA 510
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462616534 737 GAPEAAERP--PAPVLDMAPAGHPEGDAEPSPGERVEDAAA 775
Cdd:PRK07003 511 RAPAAASREdaPAAAAPPAPEARPPTPAAAAPAARAGGAAA 551
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
580-781 |
3.95e-09 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 61.16 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 580 SAPGAERGPPEDR--DAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVG 657
Cdd:PRK07764 601 PAPASSGPPEEAArpAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 658 DTAPPDLCDPGSLTGDASPLSQDAkgmiAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLG 737
Cdd:PRK07764 681 PPPAPAPAAPAAPAGAAPAQPAPA----PAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA 756
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462616534 738 APEAAERPPAPVldmAPAGHPEGDAEPSPGERVEDAAAPKAPGP 781
Cdd:PRK07764 757 QPPPPPAPAPAA---APAAAPPPSPPSEEEEMAEDDAPSMDDED 797
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
580-785 |
1.34e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.57 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 580 SAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAP-PPRDPGTPATkegaweamAVAPEEPPPSAGEDIVGD 658
Cdd:PHA03247 2727 AARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPaPPAAPAAGPP--------RRLTRPAVASLSESRESL 2798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 659 TAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQpllVHPSGDHARDAqdPSQSLGA 738
Cdd:PHA03247 2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGS---VAPGGDVRRRP--PSRSPAA 2873
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616534 739 -PEAAERPPA-----------------PVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAK 785
Cdd:PHA03247 2874 kPAAPARPPVrrlarpavsrstesfalPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
70-237 |
1.52e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 57.67 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 70 TQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQ-----LDGENSYK--CSKCKK 142
Cdd:pfam13423 122 SPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYPRKPSSNNKKPPNQTFSSilkssLERETTTKawCEKCKR 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 143 MVPASKRFTIHRSSNVLTLSlkrfANFTGGKIAKDVKYPEYL--DIRPYMS---QPNGEPIVYVLYAVLVHTGFNCHAGH 217
Cdd:pfam13423 202 YQPLESRRTVRNLPPVLSLN----AALTNEEWRQLWKTPGWLppEIGLTLSddlQGDNEIVKYELRGVVVHIGDSGTSGH 277
|
170 180
....*....|....*....|....*...
gi 2462616534 218 YFCYIKASN--------GLWYQMNDSIV 237
Cdd:pfam13423 278 LVSFVKVADseledpteSQWYLFNDFLV 305
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
581-787 |
3.67e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 57.94 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 581 APGAERGPPEDRDAEPQPGSPAAESLEE--PDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAV-------APEEPPPSA 651
Cdd:PRK07003 382 APGARAAAAVGASAVPAVTAVTGAAGAAlaPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGdapvpakANARASADS 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 652 GEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPceqpllvhpsgdhARDAQD 731
Cdd:PRK07003 462 RCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAP-------------AAAAPP 528
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616534 732 PSQSLGAPEAAERPPAPVLDMAPAghpeGDAEPSPGERVED------AAAPKAPGPSPAKEK 787
Cdd:PRK07003 529 APEARPPTPAAAAPAARAGGAAAA----LDVLRNAGMRVSSdrgaraAAAAKPAAAPAAAPK 586
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
574-784 |
3.83e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 57.58 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 574 GSTDEMSAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGE 653
Cdd:PRK12323 367 QSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 654 DIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAP----PARSEEPCEQPLLVHPSGDHARDA 729
Cdd:PRK12323 447 APAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPweelPPEFASPAPAQPDAAPAGWVAESI 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462616534 730 QDPSQSLGAPEAAERPPAPVldMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPA 784
Cdd:PRK12323 527 PDPATADPDDAFETLAPAPA--AAPAPRAAAATEPVVAPRPPRASASGLPDMFDG 579
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
581-784 |
1.04e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.87 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 581 APGAERGPPEDRDAEPQPGSPAAESLeePDAAAG----------------LSSTKKAPPPrdPGTPATKEGAWEAMAVAP 644
Cdd:PHA03247 2495 APDPGGGGPPDPDAPPAPSRLAPAIL--PDEPVGepvhprmltwirgleeLASDDAGDPP--PPLPPAAPPAAPDRSVPP 2570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 645 EEPPPSAGEDIVGD-----TAPPDLCDPGSLTGDasplSQDAKGMIAEGPRDSAlAEAPEGLSPAPPARSEEPCEQPLLV 719
Cdd:PHA03247 2571 PRPAPRPSEPAVTSrarrpDAPPQSARPRAPVDD----RGDPRGPAPPSPLPPD-THAPDPPPPSPSPAANEPDPHPPPT 2645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616534 720 HPSGDHARDAQDPSQsLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPA 784
Cdd:PHA03247 2646 VPPPERPRDDPAPGR-VSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPE 2709
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
11-255 |
2.61e-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: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 11 QALSNPGDVIKpmfvinemrriarHFRFGNQEDAHEFLQYTVDAMQKAC-LNGSNKLDRHTQATTL-VCQIFGGYLRSRV 88
Cdd:cd02673 16 QALSSIGKINT-------------EFDNDDQQDAHEFLLTLLEAIDDIMqVNRTNVPPSNIEIKRLnPLEAFKYTIESSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 89 KCLNCKGVSDTFDpyLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCK-KMVPASKRFTihRSSNVLTLSLKRFA 167
Cdd:cd02673 83 VCIGCSFEENVSD--VGNFLDVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKcESAISSERIM--TFPECLSINLKRYK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 168 NFTGgkIAKDVKypeylDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKAS--NGLWYQMNDSI---VSTSDI 242
Cdd:cd02673 159 LRIA--TSDYLK-----KNEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEirpVSKNDV 231
|
250
....*....|...
gi 2462616534 243 RSVLSQQAYVLFY 255
Cdd:cd02673 232 STNARSSGYLIFY 244
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
573-775 |
2.97e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 54.99 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 573 KGSTDEMSAPGAERGP--PEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMA--VAPEEPP 648
Cdd:PRK07764 606 SGPPEEAARPAAPAAPaaPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAapAAPPPAP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 649 PSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPceQPLLVHPSGDHARD 728
Cdd:PRK07764 686 APAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP--DPAGAPAQPPPPPA 763
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462616534 729 AQDPSQSLGAPEAAERPPAPVLDMapaghpegDAEPSPGERVEDAAA 775
Cdd:PRK07764 764 PAPAAAPAAAPPPSPPSEEEEMAE--------DDAPSMDDEDRRDAE 802
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
581-787 |
4.58e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.56 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 581 APGAERGPPEDRDAEPQPGSPAAESLEEPDAA---------AGLSSTKKAPPPRDPGTPAT----KEGAWEAMAVA---- 643
Cdd:PHA03247 262 GEGADRAPETARGATGPPPPPEAAAPNGAAAPpdgvwgaalAGAPLALPAPPDPPPPAPAGdaeeEDDEDGAMEVVsplp 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 644 ---------------PEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPlsqDAKGMIAEGPrdsalaeapeGLSPAPPAR 708
Cdd:PHA03247 342 rprqhyplgfpkrrrPTWTPPSSLEDLSAGRHHPKRASLPTRKRRSAR---HAATPFARGP----------GGDDQTRPA 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616534 709 SEEPCEQPLLVHPsgdhardaqdpsqslGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEK 787
Cdd:PHA03247 409 APVPASVPTPAPT---------------PVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPDDPDDATRK 472
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
608-797 |
6.27e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 53.70 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 608 EPDAAAGlSSTKKAPPPRDPG---TPATKEGAWEAMAVAPEEPPPSAGediVGDTAPPDLCDPGSLTGDASPLSQDAKGM 684
Cdd:PRK07003 359 EPAVTGG-GAPGGGVPARVAGavpAPGARAAAAVGASAVPAVTAVTGA---AGAALAPKAAAAAAATRAEAPPAAPAPPA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 685 IAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEgDAEP 764
Cdd:PRK07003 435 TADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPD-ARAP 513
|
170 180 190
....*....|....*....|....*....|...
gi 2462616534 765 SPGERVEDAAAPKAPGPSPAKEKIGSLRKVDRG 797
Cdd:PRK07003 514 AAASREDAPAAAAPPAPEARPPTPAAAAPAARA 546
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
551-795 |
1.21e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 53.25 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 551 PAPLLSLPEDKILETFRLSNKLKGSTDEMSAPGaergpPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPG-- 628
Cdd:PHA03307 75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPT-----PPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpa 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 629 ------------TPATKEGAWEA-----MAVAPEEPPPSAGEDIVGDTAPPDLCDPGSLTGdaSPLSQDAKGMIAEGPRD 691
Cdd:PHA03307 150 asppaagaspaaVASDAASSRQAalplsSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS--SPISASASSPAPAPGRS 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 692 SAlAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPvldmaPAGHPEGDAEPSPGERVE 771
Cdd:PHA03307 228 AA-DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPG-----PASSSSSPRERSPSPSPS 301
|
250 260
....*....|....*....|....
gi 2462616534 772 DAAAPKAPGPSPAKEKIGSLRKVD 795
Cdd:PHA03307 302 SPGSGPAPSSPRASSSSSSSRESS 325
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
581-797 |
2.71e-06 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 51.52 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 581 APGAERGPP--EDRDAEPQPgspaAESleepdAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGD 658
Cdd:PRK13108 281 APGALRGSEyvVDEALEREP----AEL-----AAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQ 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 659 TAPPDlcdpgsltGDASPLSQDAKGMIAEGPRDSALA----EAPEGLSPAPPARSEEPCEQPllvhpsgdhardAQDPSQ 734
Cdd:PRK13108 352 VADRD--------GESTPAVEETSEADIEREQPGDLAgqapAAHQVDAEAASAAPEEPAALA------------SEAHDE 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616534 735 SlgAPEAAERppapvldmapaghpegdAEPSPGERVEDAAAPKAPGPSPAK-EKIGSLRKVDRG 797
Cdd:PRK13108 412 T--EPEVPEK-----------------AAPIPDPAKPDELAVAGPGDDPAEpDGIRRQDDFSSR 456
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
581-901 |
3.26e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 51.53 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 581 APGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTA 660
Cdd:PRK07764 413 AAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAA 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 661 PPdlcdpgsltGDASPLSQDAKGMIAEGPRDS--ALAEAPEGLSPA------PPARSEEPCEQPL-LVHPSGDHAR--DA 729
Cdd:PRK07764 493 AP---------AAPAAPAAPAGADDAATLRERwpEILAAVPKRSRKtwaillPEATVLGVRGDTLvLGFSTGGLARrfAS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 730 QDPSQSL---------------------GAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEKI 788
Cdd:PRK07764 564 PGNAEVLvtalaeelggdwqveavvgpaPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAP 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 789 GSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDRLSPGERRSLGRCSH--- 865
Cdd:PRK07764 644 APGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQppq 723
|
330 340 350
....*....|....*....|....*....|....*...
gi 2462616534 866 --HHSRHRSGVELDWVRHHYTEGERGWGREKFYPDRPR 901
Cdd:PRK07764 724 aaQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPP 761
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
505-784 |
4.46e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.48 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 505 GANSADSDSDPKENGLAPDGASCQGQPAlhseNPFAKANGLPGKlMPAPLLSLPEDKILETFRLSNKLKGSTDEMSAPGA 584
Cdd:PHA03247 2602 VDDRGDPRGPAPPSPLPPDTHAPDPPPP----SPSPAANEPDPH-PPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQA 2676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 585 ErGPPEdrdaepQPGSPAAesleePDAAAGLSSTKKAPPPrdPGTPATKEGAWEAmavAPEEPPPSAGEDIVGDTAPPDL 664
Cdd:PHA03247 2677 S-SPPQ------RPRRRAA-----RPTVGSLTSLADPPPP--PPTPEPAPHALVS---ATPLPPGPAAARQASPALPAAP 2739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 665 CDPGSLTGDASPlsqdakGMIAEGPRDSALAEAPeglSPAPPARSEEPcEQPLLVHPSGDHARDAqdpSQSLGAPEAAER 744
Cdd:PHA03247 2740 APPAVPAGPATP------GGPARPARPPTTAGPP---APAPPAAPAAG-PPRRLTRPAVASLSES---RESLPSPWDPAD 2806
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462616534 745 PPAPVLDMAPAGHPEgdAEPSPGERVEDAAAPKAPGPSPA 784
Cdd:PHA03247 2807 PPAAVLAPAAALPPA--ASPAGPLPPPTSAQPTAPPPPPG 2844
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-234 |
1.83e-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: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 29 MRRIARHFRFGNQEDAHEFLQYTVDAMqKACLNGSNKldrhtQATTLVCQIFGGYLR--------------SRVKCLNCK 94
Cdd:cd02669 195 SKVSKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 95 GVSDTFD-PYLDITLEIKAA---QSVNKA--LEQfVKPEQLdgENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRF-- 166
Cdd:cd02669 269 RVKKTSVsPFLLLTLDLPPPplfKDGNEEniIPQ-VPLKQL--LKKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFsk 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616534 167 ANFTGGKIAKDVKYP-EYLDIRPYMSQP---NGEPIVYVLYAVLVHTGFNCHAGHYFCYI-KASNGLWYQMND 234
Cdd:cd02669 346 NNFFKEKNPTIVNFPiKNLDLSDYVHFDkpsLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQD 418
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
475-819 |
2.89e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 48.63 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 475 GTIVSSHSPGQEAEDEEATPHelQEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPFAKANGLPGKLMPAPL 554
Cdd:PHA03307 98 ASPAREGSPTPPGPSSPDPPP--PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 555 LSLPEDkiletfrlsnklkgSTDEMSAPGAERGPPEDR----DAEPQPGSPAAESLEEPDAAAGLSStkKAPPPRDPGTP 630
Cdd:PHA03307 176 LSSPEE--------------TARAPSSPPAEPPPSTPPaaasPRPPRRSSPISASASSPAPAPGRSA--ADDAGASSSDS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 631 ATKEGAWEAMAVAPEEPPPSAGEDIVgdtapPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSE 710
Cdd:PHA03307 240 SSSESSGCGWGPENECPLPRPAPITL-----PTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 711 EPCEQPllVHPSGDHARDAQDPSQSlgaPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEKIGS 790
Cdd:PHA03307 315 SSSSSS--SRESSSSSTSSSSESSR---GAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRR 389
|
330 340
....*....|....*....|....*....
gi 2462616534 791 LRKvDRGHYRSRRERSSSGEPARESRSKT 819
Cdd:PHA03307 390 ARA-AVAGRARRRDATGRFPAGRPRPSPL 417
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
580-754 |
3.43e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 48.31 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 580 SAPGAERGPPEDRDAEPQ---------PGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEamAVAPEEPPPS 650
Cdd:PRK07003 454 NARASADSRCDERDAQPPadsgsasapASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDA--PAAAAPPAPE 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 651 AGEdivgdTAPPDLCDPGSLTGDASPLS--QDAkGMIAEGPRDSALAEAPEglSPAPPARSEEPCEQPLLVH---PSGDH 725
Cdd:PRK07003 532 ARP-----PTPAAAAPAARAGGAAAALDvlRNA-GMRVSSDRGARAAAAAK--PAAAPAAAPKPAAPRVAVQvptPRARA 603
|
170 180 190
....*....|....*....|....*....|.
gi 2462616534 726 ARDAQDPSQSLGAPEAAE--RPPAPVLDMAP 754
Cdd:PRK07003 604 ATGDAPPNGAARAEQAAEsrGAPPPWEDIPP 634
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
579-984 |
5.55e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.47 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 579 MSAPGAERGPPED--RDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAP-------EEPPP 649
Cdd:PHA03307 22 PRPPATPGDAADDllSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTwslstlaPASPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 650 SAGEDIVGDTAPPDlcDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEepceqpllvhPSGDHARDA 729
Cdd:PHA03307 102 REGSPTPPGPSSPD--PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPA----------AVASDAASS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 730 QDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKA-PGPSPAKE-KIGSLRKVDRGHYRSRRERSS 807
Cdd:PHA03307 170 RQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASsPAPAPGRSaADDAGASSSDSSSSESSGCGW 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 808 SGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDRLSPGERRSLGRCSHHHSRHRSGVELDwvrhhytege 887
Cdd:PHA03307 250 GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSS---------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 888 rgwgrekfypdrprwdrcryyhdryalyaardwkpfhGGREHERAGLHERPHKDHNRG-RRGCEPARERERHRPSSPRAG 966
Cdd:PHA03307 320 -------------------------------------SSRESSSSSTSSSSESSRGAAvSPGPSPSRSPSPSRPPPPADP 362
|
410
....*....|....*...
gi 2462616534 967 APHALAPHPDRFSHDRTA 984
Cdd:PHA03307 363 SSPRKRPRPSRAPSSPAA 380
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
594-724 |
3.46e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 44.71 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 594 AEPQPGSPAAESLEEPDAAAglSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTAPPDLCDPG--SLT 671
Cdd:PRK14951 369 AAEAAAPAEKKTPARPEAAA--PAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAApaAVA 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462616534 672 GDASPLSQDAKGMIAEGPRdsalAEAPEGLSPAPPARSEEPCEQPLLVHPSGD 724
Cdd:PRK14951 447 LAPAPPAQAAPETVAIPVR----VAPEPAVASAAPAPAAAPAAARLTPTEEGD 495
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
158-256 |
3.48e-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: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 158 VLTLSLKRFA--NFTGGKIAKDVKYPEYLDIRPYMsqpngepivyvLYAVLVHTGfNCHAGHYFCYI-KASNGLWYQMND 234
Cdd:cd02665 131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYND 198
|
90 100 110
....*....|....*....|....*....|
gi 2462616534 235 SIVSTSDIRSVLSQ--------QAYVLFYI 256
Cdd:cd02665 199 ISVTESSWEEVERDsfgggrnpSAYCLMYI 228
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
692-959 |
4.19e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.51 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 692 SALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVE 771
Cdd:PRK12678 53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 772 DAAAPKAPGPSPAKEKIGSLRKVDRGHyrsrRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDR 851
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARAD----AAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 852 LSPGERRslgrcSHHHSRHRsgveldwvrhhytEGERGWGRekfypDRPRWDRCRYYHDRYALYAARDWKPFHGGReher 931
Cdd:PRK12678 209 REQGDRR-----EERGRRDG-------------GDRRGRRR-----RRDRRDARGDDNREDRGDRDGDDGEGRGGR---- 261
|
250 260
....*....|....*....|....*...
gi 2462616534 932 aglherphkdhnRGRRGcepaRERERHR 959
Cdd:PRK12678 262 ------------RGRRF----RDRDRRG 273
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
583-785 |
4.39e-04 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 44.43 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 583 GAERGPP-------EDRDAEPQPGSPAAESLEEPDaaagLSSTKKAPPPRDPGTPATKEG-AWEAMAVAPEEPPpsaged 654
Cdd:PRK14086 75 SRELGRPiriaitvDPSAGEPAPPPPHARRTSEPE----LPRPGRRPYEGYGGPRADDRPpGLPRQDQLPTARP------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 655 ivgdtAPPDLCD---PGSLTGDASPLSQDAKgmiaegprDSALAEAPEGLSPAPPARSEEPCEQPL-LVHPSGDHARDAQ 730
Cdd:PRK14086 145 -----AYPAYQQrpePGAWPRAADDYGWQQQ--------RLGFPPRAPYASPASYAPEQERDREPYdAGRPEYDQRRRDY 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616534 731 DPSQSLGAPEAAERPPAPvlDMAP-AGHPEGDAEPSPG--ERVEDAAAPKAPGPSPAK 785
Cdd:PRK14086 212 DHPRPDWDRPRRDRTDRP--EPPPgAGHVHRGGPGPPErdDAPVVPIRPSAPGPLAAQ 267
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
573-785 |
4.45e-04 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 44.53 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 573 KGSTDEMSAPGAERGPPEDRDAEPQPGSP--AAESLEEPDAAAGLSSTKKAPPPRD------PGTPATKEGAWEAMAVAP 644
Cdd:PLN03209 345 KPVTPEAPSPPIEEEPPQPKAVVPRPLSPytAYEDLKPPTSPIPTPPSSSPASSKSvdavakPAEPDVVPSPGSASNVPE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 645 EEPPPSAGED--------IVGDTAPPDLCDPGSLTGDASPLSQDAK-GMIAEGPRDSALAEA-------PEGLSPAPPAR 708
Cdd:PLN03209 425 VEPAQVEAKKtrplspyaRYEDLKPPTSPSPTAPTGVSPSVSSTSSvPAVPDTAPATAATDAaapppanMRPLSPYAVYD 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616534 709 SEEPCEQPLLVHPSGDHArdaqdPSQSLGAPEAAERPPaPVLDMAPAGHPEGDAEP-SPGERVEDAAAPKAPGPSPAK 785
Cdd:PLN03209 505 DLKPPTSPSPAAPVGKVA-----PSSTNEVVKVGNSAP-PTALADEQHHAQPKPRPlSPYTMYEDLKPPTSPTPSPVL 576
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
618-787 |
5.03e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.10 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 618 TKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEdiVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEA 697
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPA--AAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 698 PeglSPAPPARSEEPCEQPLlvhPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDA---- 773
Cdd:PRK12323 454 P---AAAPAAAARPAAAGPR---PVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAesip 527
|
170
....*....|....*...
gi 2462616534 774 ----AAPKAPGPSPAKEK 787
Cdd:PRK12323 528 dpatADPDDAFETLAPAP 545
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
686-784 |
5.91e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 686 AEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDhARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPS 765
Cdd:PRK07764 405 APAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPS-PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPA 483
|
90
....*....|....*....
gi 2462616534 766 PGERVEDAAAPKAPGPSPA 784
Cdd:PRK07764 484 PPAAPAPAAAPAAPAAPAA 502
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
268-784 |
6.00e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 268 THPTHSPGQSSPRPVISQRVVTNKQAAPGFIGPQLPSHMIKNP---PHLNGTGPLKDTPSSSMSSPNGNSSVNRASPVNA 344
Cdd:PHA03247 2587 RRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPspsPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR 2666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 345 SASVQNWSvnRSSVIPEHPKKQKITISIHnklPVRQCQSQPnlhsnSLENPTKPVPSSTITNSAVQSTSNASTMSVSSKV 424
Cdd:PHA03247 2667 ARRLGRAA--QASSPPQRPRRRAARPTVG---SLTSLADPP-----PPPPTPEPAPHALVSATPLPPGPAAARQASPALP 2736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 425 TKPIPRSeSCSQPVMNGKSKLNSSVLVPYGAESSEDSDEESKGLGKEngiGTIVSSHSPGQEAEDEEATPHELQEPMTLN 504
Cdd:PHA03247 2737 AAPAPPA-VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR---LTRPAVASLSESRESLPSPWDPADPPAAVL 2812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 505 GANSADSDSDPKENGLAPDGASCQGQPALHSEnPFAKANGLPGKLMPAPLLSlpedkiletfrlsnKLKGSTDEMSAPGA 584
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPG-PPPPSLPLGGSVAPGGDVR--------------RRPPSRSPAAKPAA 2877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 585 ERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTAPPDL 664
Cdd:PHA03247 2878 PARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 665 CDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPeglSPAPPARSEEPC----EQPLLVHPSGDHArdAQDPSQSLGAPE 740
Cdd:PHA03247 2958 AVPQPWLGALVPGRVAVPRFRVPQPAPSREAPAS---STPPLTGHSLSRvsswASSLALHEETDPP--PVSLKQTLWPPD 3032
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2462616534 741 AAERPPAPVLDMAPAGHPEGDA-EPSPGERVEDAAAPKAPGPSPA 784
Cdd:PHA03247 3033 DTEDSDADSLFDSDSERSDLEAlDPLPPEPHDPFAHEPDPATPEA 3077
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
574-842 |
8.23e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.82 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 574 GSTDEMSAPGAERGPPEDRDAEPQPGS-PAAESLEEPDAAAGLSSTKKAPPPRDPGtpATKEGAW-EAMAVAPEEPPPSA 651
Cdd:PRK07764 454 PSPPPAAAPSAQPAPAPAAAPEPTAAPaPAPPAAPAPAAAPAAPAAPAAPAGADDA--ATLRERWpEILAAVPKRSRKTW 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 652 GedIVGDTAPPDLCDPGSLT-GDASPLsqdAKGMIAEGPRDSALAEA-----------------------PEGLSPAPPA 707
Cdd:PRK07764 532 A--ILLPEATVLGVRGDTLVlGFSTGG---LARRFASPGNAEVLVTAlaeelggdwqveavvgpapgaagGEGPPAPASS 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 708 RSEEPCEQPllvhPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEK 787
Cdd:PRK07764 607 GPPEEAARP----AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPP 682
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462616534 788 IGSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAP 842
Cdd:PRK07764 683 PAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADD 737
|
|
| PRK14949 |
PRK14949 |
DNA polymerase III subunits gamma and tau; Provisional |
347-782 |
8.85e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237863 [Multi-domain] Cd Length: 944 Bit Score: 43.56 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 347 SVQNWSVNRSSVIpEHPKKQKITISIHNKLPVRQCQSQPNLHSNSlENPTKPVPSSTiTNSAVQsTSNASTMSVSSKVTK 426
Cdd:PRK14949 362 PVKRWQVDDPAEI-SLPEGQTPSALAAAVQAPHANEPQFVNAAPA-EKKTALTEQTT-AQQQVQ-AANAEAVAEADASAE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 427 PIPRSESCSQPVMNGKSKLNSSVlvpygaessedsdeeskglgkengigTIVSSHSPGQEAEDEEATPHELQEPMTLNGA 506
Cdd:PRK14949 438 PADTVEQALDDESELLAALNAEQ--------------------------AVILSQAQSQGFEASSSLDADNSAVPEQIDS 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 507 NSADSDSDPK-ENGLAPD--GASCQGQPALHSENPFAKANGLPGKLMP-------APLLSLPEDKILETFRLSNKLKGST 576
Cdd:PRK14949 492 TAEQSVVNPSvTDTQVDDtsASNNSAADNTVDDNYSAEDTLESNGLDEgdyaqdsAPLDAYQDDYVAFSSESYNALSDDE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 577 DEMSAPGAERGPPEDRDAEPQPGSP-----AAESLEEPD------AA-----AGL-------SSTKKAPPPRDPGTPatk 633
Cdd:PRK14949 572 QHSANVQSAQSAAEAQPSSQSLSPIsavttAAASLADDDildavlAArdsllSDLdalspkeGDGKKSSADRKPKTP--- 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 634 egaweamavaPEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAkgmIAEGPRDSALAEAPeGLSPAPPARS--EE 711
Cdd:PRK14949 649 ----------PSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQS---VPEAALASGSAPAP-PPVPDPYDRPpwEE 714
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616534 712 PCEQPLLVHPSGDHARDAQDPSQslgapEAAERPPAPVLDMAPAGHPEGDAEPSPgerveDAAAPKAPGPS 782
Cdd:PRK14949 715 APEVASANDGPNNAAEGNLSESV-----EDASNSELQAVEQQATHQPQVQAEAQS-----PASTTALTQTS 775
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
578-785 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 578 EMSAPG----AERGPPEDRDAEPQPGSPAAESLEEPDAAA------------GLSSTKKAPPP-------RDPGTPATKE 634
Cdd:COG5180 254 EMRPPAdakeRRRAAIGDTPAAEPPGLPVLEAGSEPQSDApeaetarpidvkGVASAPPATRPvrppggaRDPGTPRPGQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 635 GAWEAMAV----APEEPPPS----AGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPP 706
Cdd:COG5180 334 PTERPAGVpeaaSDAGQPPSayppAEEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 707 AR--------SEEPCEQPLLVHPSGDH-ARDAQDPSQSLGAPEAAERPPAPVldMAPAGHPEGDAePSPGERVEDAAAPK 777
Cdd:COG5180 414 ALdgggretaSLGGAAGGAGQGPKADFvPGDAESVSGPAGLADQAGAAASTA--MADFVAPVTDA-TPVDVADVLGVRPD 490
|
....*...
gi 2462616534 778 APGPSPAK 785
Cdd:COG5180 491 AILGGNVA 498
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
582-770 |
1.49e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 582 PGAERGPPEDRDAEPQPGSPAAESL---------EEPDAAAGLSSTKKAPPPRDPgtPATKEGAWEAMAVAPEEPPPSAg 652
Cdd:PHA03307 284 PASSSSSPRERSPSPSPSSPGSGPApssprasssSSSSRESSSSSTSSSSESSRG--AAVSPGPSPSRSPSPSRPPPPA- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 653 edivgDTAPPdlcdPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARseePCEQPllvhpsgdhardaqdP 732
Cdd:PHA03307 361 -----DPSSP----RKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRF---PAGRP---------------R 413
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462616534 733 SQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERV 770
Cdd:PHA03307 414 PSPLDAGAASGAFYARYPLLTPSGEPWPGSPPPPPGRV 451
|
|
| KLF14_N |
cd21576 |
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ... |
607-785 |
1.55e-03 |
|
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.
Pssm-ID: 409238 [Multi-domain] Cd Length: 195 Bit Score: 40.96 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 607 EEPDAAAGLSSTKKAPPPRDPGtPATKEGAWEAMAVAPEEPPPSAGedivgDTAPPDLCdpgsltgdASPLSqDAKGMIA 686
Cdd:cd21576 32 EGAGGAAGSEVGAAPPESALPG-PGPPGPAWVPPLLQVPAPSPGAG-----GAAPHLLA--------ASVLA-DLRGGAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 687 EGPRDSALaEAPEGLSPAP-PARSEEPCEQPLLVHPSGDHArdAQDPSQSLGAPEAAERPPAPvldmapaghpegdaePS 765
Cdd:cd21576 97 EGSREDSG-EAPRASSGSSdPARGSSPTLGSEPAPASGEDA--VSGPESSFGAPAIPSAPAAP---------------GA 158
|
170 180
....*....|....*....|
gi 2462616534 766 PGERVEDAAAPKAPGPSPAK 785
Cdd:cd21576 159 PAVSGEVPGGAPGAGPAPAA 178
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
580-775 |
1.74e-03 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 42.64 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 580 SAPGAERGPPEDR--DAEPQPGSPAAESLEEPDAAAglsstkKAPPPRDPGTPATKegaWEAMAVAPEEPPP--SAGEDI 655
Cdd:PHA03321 452 STPACARRARAQRarDAGPEYVDPLGALRRLPAGAA------PPPEPAAAPSPATY---YTRMGGGPPRLPPrnRATETL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 656 VGDTAPP------DLCDPGSLTGDASPLSQDAKGMIAEgpRDSALAEAPEGLSPAPPAR-SEEPCEQPL-----LVHPSG 723
Cdd:PHA03321 523 RPDWGPPaaappeQMEDPYLEPDDDRFDRRDGAAAAAT--SHPREAPAPDDDPIYEGVSdSEEPVYEEIptprvYQNPLP 600
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616534 724 DHARDAQDP---------------------SQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAA 775
Cdd:PHA03321 601 RPMEGAGEPpdldaptspwveeenpiygwgDSPLFSPPPAARFPPPDPALSPEPPALPAHRPRPGALAPDGPA 673
|
|
| PHA01929 |
PHA01929 |
putative scaffolding protein |
704-797 |
2.03e-03 |
|
putative scaffolding protein
Pssm-ID: 177328 Cd Length: 306 Bit Score: 41.58 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 704 APPARSEEPCEQPLLVHPSGDHARDAQDPSQSlgAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKA---PG 780
Cdd:PHA01929 19 VPPAAAPTPQPNPVIQPQAPVQPGQPGAPQQL--AIPTQQPQPVPTSAMTPHVVQQAPAQPAPAAPPAAGAALPEaleVP 96
|
90
....*....|....*..
gi 2462616534 781 PSPAKEKIGSLRKVDRG 797
Cdd:PHA01929 97 PPPAFTPNGEIVGTLAG 113
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
401-624 |
2.71e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 42.00 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 401 SSTITNSAVQSTSnASTMSVSSKVTKPIPRSESCSQpvmngksklNSSVLVPYGAESSEDSDEESKGLGKENGIGtivss 480
Cdd:PRK08691 369 NAVIENTELQSPS-AQTAEKETAAKKPQPRPEAETA---------QTPVQTASAAAMPSEGKTAGPVSNQENNDV----- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 481 hSPGQEAEDEEATPhELQEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPfakanglpgklMPAPLLSLPED 560
Cdd:PRK08691 434 -PPWEDAPDEAQTA-AGTAQTSAKSIQTASEAETPPENQVSKNKAADNETDAPLSEVP-----------SENPIQATPND 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616534 561 KILETFRLSNKLKGST---------DEMSAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPP 624
Cdd:PRK08691 501 EAVETETFAHEAPAEPfygygfpdnDCPPEDGAEIPPPDWEHAAPADTAGGGADEEAEAGGIGGNNTPSAPPP 573
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
608-854 |
3.20e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 41.45 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 608 EPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDivgDTAPPDLCDPGSLTG-DASPLSQDAKGMIA 686
Cdd:PLN03209 332 ESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYE---DLKPPTSPIPTPPSSsPASSKSVDAVAKPA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 687 EgPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSlgaPEAAERPPApvldmapaghPEGDAEPSP 766
Cdd:PLN03209 409 E-PDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPT---APTGVSPSV----------SSTSSVPAV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 767 GERVEDAAAPKAPGPSPAKEKIGSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHP 846
Cdd:PLN03209 475 PDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRP 554
|
....*...
gi 2462616534 847 ghgdrLSP 854
Cdd:PLN03209 555 -----LSP 557
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
602-785 |
3.92e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 41.58 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 602 AAESLEEPDAAAGLSSTKKAPPPRdPGTPATKEGAWEAMAVAPEEPPPsagediVGDTAPPDLCDPGSLT------GDAS 675
Cdd:PHA03379 401 AREALEKASEPTYGTPRPPVEKPR-PEVPQSLETATSHGSAQVPEPPP------VHDLEPGPLHDQHSMApcpvaqLPPG 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 676 PLSQDAKGMIAEGP-RDSALAEAPeglSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAP 754
Cdd:PHA03379 474 PLQDLEPGDQLPGVvQDGRPACAP---VPAPAGPIVRPWEASLSQVPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPP 550
|
170 180 190
....*....|....*....|....*....|.
gi 2462616534 755 AGHPEGDAEPSPGERVEDAAAPKAPGPSPAK 785
Cdd:PHA03379 551 LIAMQGPGETSGIVRVRERWRPAPWTPNPPR 581
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
580-714 |
3.97e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 41.24 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 580 SAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIvgdt 659
Cdd:PRK14951 372 AAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVAL---- 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462616534 660 aPPDLCDPGSLTGDASPLsqdakgMIAEGPRDSALAEAPEGLSPAPPARSEEPCE 714
Cdd:PRK14951 448 -APAPPAQAAPETVAIPV------RVAPEPAVASAAPAPAAAPAAARLTPTEEGD 495
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-238 |
4.05e-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: 4.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2462616534 198 IVYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMNDSIVS 238
Cdd:cd02666 279 YGYRLHAVFIHRG-EASSGHYWVYIKdFEENVWRKYNDETVT 319
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
689-786 |
4.07e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 41.33 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 689 PRDSALAEAPEGLSPAP----PARSEEPCEQPLLVHPSGDHARDAQDPSqslgapeaaerPPAPVLDMAPAGHPEGDAEP 764
Cdd:PRK14950 362 PVPAPQPAKPTAAAPSPvrptPAPSTRPKAAAAANIPPKEPVRETATPP-----------PVPPRPVAPPVPHTPESAPK 430
|
90 100
....*....|....*....|..
gi 2462616534 765 SPGERVEDAAAPKAPGPSPAKE 786
Cdd:PRK14950 431 LTRAAIPVDEKPKYTPPAPPKE 452
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
641-788 |
4.65e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.12 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 641 AVAPEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPlSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVH 720
Cdd:PRK07764 373 GLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAA-APAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAG 451
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616534 721 PSGDHARDAQDPSQSLGAPEAAERPPApvldmAPAghPEGDAEPSPGERVEDAAAPKAPGPSPAKEKI 788
Cdd:PRK07764 452 GAPSPPPAAAPSAQPAPAPAAAPEPTA-----APA--PAPPAAPAPAAAPAAPAAPAAPAGADDAATL 512
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
570-816 |
5.42e-03 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 40.82 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 570 NKLKGSTDEMSAPGAERGPPEDRDAEP--QPGSPAAESLEEPDAAAGLSStkKAPPPRDPGTPATKEGAWEAMAVAPEEP 647
Cdd:COG5180 70 GKPQLPSVAEPEAYLDPAPPKSSPDTPeeQLGAPAGDLLVLPAAKTPELA--AGALPAPAAAAALPKAKVTREATSASAG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 648 PPSAGEDIvGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDsALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHAR 727
Cdd:COG5180 148 VALAAALL-QRSDPILAKDPDGDSASTLPPPAEKLDKVLTEPRD-ALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHPR 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 728 DAQDPSQSLGAPEAAE--------------RPPAPVLDMAPAGHPEGDAEPSPGERVedaaAPKAPGPSPAKEKIGSLRK 793
Cdd:COG5180 226 PEAASSPKVDPPSTSEarsrpatvdaqpemRPPADAKERRRAAIGDTPAAEPPGLPV----LEAGSEPQSDAPEAETARP 301
|
250 260
....*....|....*....|...
gi 2462616534 794 VDRGHYRSRRERSSSGEPARESR 816
Cdd:COG5180 302 IDVKGVASAPPATRPVRPPGGAR 324
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
667-785 |
5.54e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.01 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 667 PGSLTGDASPLSQDAKGMIAEGPRDSA--LAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAER 744
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAApaAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP 444
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462616534 745 PPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAK 785
Cdd:PRK12323 445 GGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAP 485
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
554-652 |
5.94e-03 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 40.75 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 554 LLSLPEDKILETFRLSNKLKGSTDEMSAPGAERGPPedrdAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATK 633
Cdd:COG5373 12 VLALLVGLLGRVARLRRRVEELEAELAEAAEAASAP----AEPEPEAAAAATAAAPEAAPAPVPEAPAAPPAAAEAPAPA 87
|
90
....*....|....*....
gi 2462616534 634 EGAwEAMAVAPEEPPPSAG 652
Cdd:COG5373 88 AAA-PPAEAEPAAAPAAAS 105
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
649-784 |
6.02e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 40.85 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 649 PSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPceqpllvhpsgdhard 728
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAP---------------- 429
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616534 729 AQDPSQSLGAPEAAERPPAPVLDMAPAghPEGDAEP---SPGERVEDAAAPKAPGPSPA 784
Cdd:PRK14951 430 AAAAPAAAPAAAPAAVALAPAPPAQAA--PETVAIPvrvAPEPAVASAAPAPAAAPAAA 486
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
498-653 |
6.12e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 40.35 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 498 QEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPFAKANGLPGKlMPAPLLSLPEDKILETfrlsnklKGSTD 577
Cdd:PRK13108 293 DEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDE-VAAESVVQVADRDGES-------TPAVE 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616534 578 EMSAPGAERGPPEDRDAEP--QPGSPAAESLEEPDAAAGL-SSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGE 653
Cdd:PRK13108 365 ETSEADIEREQPGDLAGQApaAHQVDAEAASAAPEEPAALaSEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAE 443
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
586-742 |
7.74e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616534 586 RGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPgtPATKEgawEAMAVAPEEPPPSAGEDIVGDTAPPDlc 665
Cdd:PRK07764 384 RLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAP--AAAPQ---PAPAPAPAPAPPSPAGNAPAGGAPSP-- 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616534 666 dpgsltgdasplsqdakgmiaegPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAA 742
Cdd:PRK07764 457 -----------------------PPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAA 510
|
|
| |
