|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
110-410 |
0e+00 |
|
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: 564.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 110 GAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQAHITQALSNPGDVIKPMFVINEMRRIARH 189
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 190 FRFGNQEDAHEFLQYTVDAMQKACLNGSNKL---DRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKA 266
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 267 AQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQ 346
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954668664 347 PNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 410
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
111-409 |
1.29e-78 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 261.99 E-value: 1.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 111 AGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFC--MMCTMQAHITQALSN-PGDVIKPMFVINEMRRIA 187
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNsKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 188 RHFRFGNQEDAHEFLQYTVDAMQKAClngsnKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAA 267
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 268 QSV------NKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYPEYLD 339
Cdd:pfam00443 156 SAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954668664 340 IRPYMSQPNGEPIV----YVLYAVLVHTGfNCHAGHYFCYIKA-SNGLWYQMNDSIVSTSD-IRSVLSQQAYVLFY 409
Cdd:pfam00443 236 LSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-410 |
1.28e-71 |
|
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: 242.66 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEG--FCMMCTMqAHITQALSNPGDVIK--PMFVINEMRRIA 187
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSpnSCLSCAM-DEIFQEFYYSGDRSPygPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 188 RHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIK-- 265
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 266 ------AAQSVNKA-------LEQFVKPEQLdGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGG---KIA 329
Cdd:cd02660 161 stpswaLGESGVSGtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 330 KDVKYPEYLDIRPYMSQPNGEP---------IVYVLYAVLVHTGfNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVL 400
Cdd:cd02660 240 TYVQFPLELNMTPYTSSSIGDTqdsnsldpdYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318
|
330
....*....|
gi 1954668664 401 SQQAYVLFYI 410
Cdd:cd02660 319 KSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
112-410 |
6.59e-69 |
|
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: 231.99 E-value: 6.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLtytpplanymlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvinemrriarhfr 191
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 192 FGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI----KAA 267
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 268 QSVNKALEQFVKPEQLDGENSYKCSKCKKmVPASKRFTIHRSSNVLTLSLKRFA---NFTGGKIAKDVKYPEYLDIRPYM 344
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954668664 345 SQP------NGEPIVYVLYAVLVHTGFNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVL-----SQQAYVLFYI 410
Cdd:cd02257 178 SEGekdsdsDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-410 |
1.57e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 187.11 E-value: 1.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLtytpplanymlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvinemrriarhfr 191
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 192 FGNQEDAHEFLQYTVDAMqkaclngsnkldrHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI------K 265
Cdd:cd02674 19 SADQQDAQEFLLFLLDGL-------------HS----IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdA 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 266 AAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFaNFTGG---KIAKDVKYP-EYLDIR 341
Cdd:cd02674 82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1954668664 342 PY-MSQPNGEPIVYVLYAVLVHTG-FNChaGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 410
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYGsLNG--GHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
7.98e-51 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 181.05 E-value: 7.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPPLANYMLShehsktchaegfcmmctmqahitqalsNPgdviKPMFviNEMRRIARHFR 191
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE---------------------------TP----KELF--SQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 192 FGNQEDAHEFLQYTVDAMQkaclngsnkldrhtqatTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITL----EIKAA 267
Cdd:cd02667 48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 268 QSVNKALEQFVKPEQLDGENSYKCSKCKKmvpASKRFTIHRSSNVLTLSLKRF-----ANFTggKIAKDVKYPEYLDIRP 342
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 343 YMSQPN-----GEPIVYVLYAVLVHTGfNCHAGHYFCYIKASN----------------------GLWYQMNDSIVSTSD 395
Cdd:cd02667 186 FCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 1954668664 396 IRSVLSQQAYVLFY 409
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-412 |
1.03e-50 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 182.84 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPPLAN--YMLSHEHSKTCHAEGFCMMcTMQAHITQALSNPGDVIKPMfvinemrriARH 189
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNavYSIPPTEDDDDNKSVPLAL-QRLFLFLQLSESPVKTTELT---------DKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 190 FRFG-------NQEDAHEFLQYTVDAMQkaclNGSNKLDRHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITL 262
Cdd:cd02659 74 RSFGwdslntfEQHDVQEFFRVLFDKLE----EKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 263 EIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGGKIAKD---VKYPEYL 338
Cdd:cd02659 146 AVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDFETMMRIKIndrFEFPLEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 339 DIRPYMSQPNG-----------EPIVYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQ--- 403
Cdd:cd02659 226 DMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfgg 304
|
330 340
....*....|....*....|....*...
gi 1954668664 404 -------------------AYVLFYIRS 412
Cdd:cd02659 305 eetqktydsgprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
6.16e-44 |
|
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: 162.09 E-value: 6.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYtpplaNYMLshehskTCHAEGFCMMctmqahITQALSnpGDVIKPMFVINEMRRIARHFR 191
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLL------TCLKDLFESI------SEQKKR--TGVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 192 FGNQEDAHEFLQY-------TVDAMQKACL---NGSNKLDRHTQaTTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDIT 261
Cdd:cd02663 62 NYMHQDAHEFLNFllneiaeILDAERKAEKanrKLNNNNNAEPQ-PTWVHEIFQGILTNETRCLTCETVSSRDETFLDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 262 LEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFAnFTGG-----KIAKDVKYPE 336
Cdd:cd02663 141 IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFK-YDEQlnryiKLFYRVVFPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 337 YLdiRPYMSQPNGEP--IVYVLYAVLVHTGFNCHAGHYFCYIKaSNGLWYQMNDSIVSTSDIRSVL--------SQQAYV 406
Cdd:cd02663 220 EL--RLFNTTDDAENpdRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEeffgdspnQATAYV 296
|
...
gi 1954668664 407 LFY 409
Cdd:cd02663 297 LFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
6.89e-41 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 154.12 E-value: 6.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPPLANYMLShehsktchaegfcmmCTMQAHITQALSNPGDVIKPMFVINEMRRIARHFR 191
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 192 FGN-------------------QEDAHEFLQYTVDAMQkACLNGSNKLDrhtqATTLVCQIFGGYLRSRVKCLNCKGVSD 252
Cdd:cd02668 66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-AKLSKSKNPD----LKNIVQDLFRGEYSYVTQCSKCGRESS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 253 TFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFAnF---TGG--K 327
Cdd:cd02668 141 LPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV-FdrkTGAkkK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 328 IAKDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVL------ 400
Cdd:cd02668 220 LNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMPGKPLKlgnsed 299
|
330 340
....*....|....*....|....
gi 1954668664 401 ---------------SQQAYVLFY 409
Cdd:cd02668 300 pakprkseikkgthsSRTAYMLVY 323
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
8.91e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 139.16 E-value: 8.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKT--CHAEGFCM-MCTMQAHITQALSNPgdviKPMFVINEMRriAR 188
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLgdSQSVMKKLqLLQAHLMHTQRRAEA----PPDYFLEASR--PP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 189 HFRFGNQEDAHEFLQYTVDamqkaclngsnKLDrhtqatTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLeikAAQ 268
Cdd:cd02664 75 WFTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SFP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 269 SVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGG---KIAKDVKYPEYLD--IRP 342
Cdd:cd02664 135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSlpVRV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 343 YMS----------QPNGE-------PIVYVLYAVLVHTGFNCHAGHYFCYI---------------------KASNGLWY 384
Cdd:cd02664 215 ESKssesplekkeEESGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWY 294
|
330 340 350
....*....|....*....|....*....|..
gi 1954668664 385 QMNDSIVS---TSDIRSVLS----QQAYVLFY 409
Cdd:cd02664 295 LFNDSRVTfssFESVQNVTSrfpkDTPYILFY 326
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
2.62e-27 |
|
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: 113.96 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEG--FCMMCTMqAHITQAL-----SNPGDV----------I 174
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQL-IKLADGLlsgrySKPASLksendpyqvgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 175 KP-MF--VI---NEMrriarhFRFGNQEDAHEFLQYTVDAMQKACLNgsnkldRHTQATTlvcQIFGGYLRSRVKCLNCK 248
Cdd:cd02658 80 KPsMFkaLIgkgHPE------FSTMRQQDALEFLLHLIDKLDRESFK------NLGLNPN---DLFKFMIEDRLECLSCK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 249 GVSDTFD---------PYLDIT-----LEIKAAQSVNKALEQFVKPEQLDgensYKCSKCKKMVPASKRFTIHRSSNVLT 314
Cdd:cd02658 145 KVKYTSElseilslpvPKDEATekeegELVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 315 LSLKRFA---NFTGGKIAKDVKYPEYLDIRPYMsqpngepivyvLYAVLVHTGFNCHAGHYFCYIK---ASNGLWYQMND 388
Cdd:cd02658 221 INMKRFQlleNWVPKKLDVPIDVPEELGPGKYE-----------LIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFND 289
|
330 340
....*....|....*....|.
gi 1954668664 389 SIVSTSDIRSVLSQQAYVLFY 409
Cdd:cd02658 290 EKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-409 |
6.83e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 110.37 E-value: 6.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 111 AGLQNLGNTCFANAALQCLTYTPPLAN---YMLSHEHSKTCHAEGFCMMCTM--QAHITQAlsnpgdvikPMFVINEMRR 185
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSFLLNPEKynDELANQA---------PRRLLNALRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 186 IARHFRFGNQEDAHEFLQYTVDAMQKaclngsnkldrhtqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDIT---- 261
Cdd:cd02671 96 VNPMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISvpvq 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 262 ------------------LEIKAAQsvnKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-- 321
Cdd:cd02671 159 eselskseesseispdpkTEMKTLK---WAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAan 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 322 ----NFTGG--KIAKDVKYPEYLDIRPYMSQPNGEpiVYVLYAVLVHTGFNCHAGHYFCYIKasnglWYQMNDS---IVS 392
Cdd:cd02671 236 gsefDCYGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSevkVTE 308
|
330 340
....*....|....*....|...
gi 1954668664 393 TSDIRSVLSQQA------YVLFY 409
Cdd:cd02671 309 EKDFLEALSPNTsststpYLLFY 331
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
112-411 |
3.28e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 113.81 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPPLAN--YMLSHEHSKTCHAEGFCMM-CTMQahiTQALSNPGDVIKpmFVINEMRRIAR 188
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSVALALQrLFYN---LQTGEEPVDTTE--LTRSFGWDSDD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 189 HFrfgNQEDAHEFLQYTVDAMQKAClngsnkldRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQ 268
Cdd:COG5077 270 SF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 269 SVNKALEQFVKPEQLDGENSYKCSKcKKMVPASKRFTIHRSSNVLTLSLKRF-ANFTGG---KIAKDVKYPEYLDIRPYM 344
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 345 S----QPNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKAS-NGLWYQMNDSIVSTSDIRSVLSQ----------------- 402
Cdd:COG5077 418 DrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsg 496
|
330
....*....|....
gi 1954668664 403 -----QAYVLFYIR 411
Cdd:COG5077 497 ikrfmSAYMLVYLR 510
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
112-411 |
1.53e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 102.19 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLT-YTPPLANYM---------LSHEHSKTCHAEGFCMMctmqahiTQALSNpgdvikpmFVIN 181
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRKPEPDLNQEEA-------LKLFTA--------LWSS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 182 EMRRIARHFRFGNQEDAHEFLQYTVDAMqkaclngsnKLDRHTQATTLVCQIFGGYLRSrvkclnckgvsdTFDPYLDIT 261
Cdd:COG5533 66 KEHKVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKT------------STGDWFDII 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 262 LEIKAAQSVN--KALEQFVKP--EQLD-------GENSYKCSKCKKMVPASKRftihRSSNVLTLSLKRFANFTGG-KIA 329
Cdd:COG5533 125 IELPDQTWVNnlKTLQEFIDNmeELVDdetgvkaKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKID 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 330 KDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKaSNGLWYQMNDSIVST---SDIRSVLSQQAYV 406
Cdd:COG5533 201 TEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPvseEEAINEKAKNAYL 278
|
....*
gi 1954668664 407 LFYIR 411
Cdd:COG5533 279 YFYER 283
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
1.85e-23 |
|
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: 102.41 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPP----LANYMLSHEHSktchaegfcmmctMQAHIT---------QALSNPGDVIKPMF 178
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPElrdaLKNYNPARRGA-------------NQSSDNltnalrdlfDTMDKKQEPVPPIE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 179 VINEMRriaRHF-RFGNQEDAHEFLQytvdamQKA--CLNG-----SNKLDRHTQATTLVCQIFGGYLRSRVKCL-NCKG 249
Cdd:cd02657 68 FLQLLR---MAFpQFAEKQNQGGYAQ------QDAeeCWSQllsvlSQKLPGAGSKGSFIDQLFGIELETKMKCTeSPDE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 250 VSDTFDP------YLDITLEIKAAQS-VNKALEQFVK--PEQLDGENSYkcskckkmvpaSKRFTIHRSSNVLTLSLKRF 320
Cdd:cd02657 139 EEVSTESeyklqcHISITTEVNYLQDgLKKGLEEEIEkhSPTLGRDAIY-----------TKTSRISRLPKYLTVQFVRF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 321 -----ANfTGGKIAKDVKYPEYLDIRPYMSqPNGepiVYVLYAVLVHTGFNCHAGHYFCYIKASN-GLWYQMND---SIV 391
Cdd:cd02657 208 fwkrdIQ-KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDdkvSEV 282
|
330 340
....*....|....*....|...
gi 1954668664 392 STSDIRSvLS-----QQAYVLFY 409
Cdd:cd02657 283 TEEDILK-LSgggdwHIAYILLY 304
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
3.36e-22 |
|
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: 97.05 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPPLANYmlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvINemrriarhfR 191
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-----------------------------------------LE---------E 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 192 FGNQEDAHEFLQYTVDAMQKACLNgsnkldrhtqattlvcqIFGGYLRSRVKCLNCKGVS-DTFDPYLDITLEIKAAQSV 270
Cdd:cd02662 31 FLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQSSG 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 271 NKA-----LEQFVKPEQLDGensYKCSKCK-KMVPASKRFTIH--RSS-NVLTLSLKRFANftggkiakdVKYPEYLdiR 341
Cdd:cd02662 94 SGTtlehcLDDFLSTEIIDD---YKCDRCQtVIVRLPQILCIHlsRSVfDGRGTSTKNSCK---------VSFPERL--P 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 342 PYMsqpngepivYVLYAVLVHTGFnCHAGHYFCY--------------------IKASNGL-WYQMNDSIVSTSDIRSVL 400
Cdd:cd02662 160 KVL---------YRLRAVVVHYGS-HSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHpWWRISDTTVKEVSESEVL 229
|
330
....*....|
gi 1954668664 401 SQ-QAYVLFY 409
Cdd:cd02662 230 EQkSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
269-413 |
2.37e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 97.65 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 269 SVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYP-EYLDIRPYMS 345
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1954668664 346 QPNGEPIVYVLYAVLVHTGFnCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYIRSH 413
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGG-LSGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
112-264 |
1.25e-14 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 79.16 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGfcmMCTMQAHITQALSnpgDVIKPMFVINEMRRIARHFR 191
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEN---PLGMHGSVASAYA---DLIKQLYDGNLHAFTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 192 F----------GN-QEDAHEFLQYTVDAMQKAcLN------------------------GSNKLDRHTQAT-TLVCQIFG 235
Cdd:COG5560 341 KtigsfneefsGYdQQDSQEFIAFLLDGLHED-LNriikkpytskpdlspgddvvvkkkAKECWWEHLKRNdSIITDLFQ 419
|
170 180
....*....|....*....|....*....
gi 1954668664 236 GYLRSRVKCLNCKGVSDTFDPYLDITLEI 264
Cdd:COG5560 420 GMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
111-391 |
6.13e-14 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 74.23 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 111 AGLQNLGNTCFANAALQCLTYTPPLANYMLSH-------EHS-----------------KTCHAEGFCmmctmqahitQA 166
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHlateclkEHCllcelgflfdmlekakgKNCQASNFL----------RA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 167 LSNPGDViKPMFVINEMRRIARHFRFGNQEDA-HEFLqytvdaMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCL 245
Cdd:pfam13423 71 LSSIPEA-SALGLLDEDRETNSAISLSSLIQSfNRFL------LDQLSSEENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 246 NCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQ-----LDGENSYK--CSKCKKMVPASKRFTIHRSSNVLTLSlk 318
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYPRKPSSNNKKPPNQTFSSilkssLERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLN-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 319 rfANFTGGKIAKDVKYPEYL--DIRPYMS---QPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASN--------GLWYQ 385
Cdd:pfam13423 222 --AALTNEEWRQLWKTPGWLppEIGLTLSddlQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYL 299
|
....*.
gi 1954668664 386 MNDSIV 391
Cdd:pfam13423 300 FNDFLV 305
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
735-940 |
9.42e-12 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 69.63 E-value: 9.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 735 APGAERGPPEDRDAEPQPGSPAAESleEPDAaaglsSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTA 814
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAA--RPAA-----PAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 815 PPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPE 894
Cdd:PRK07764 662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPL 741
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1954668664 895 aaerPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKE 940
Cdd:PRK07764 742 ----PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-388 |
1.27e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 68.50 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMqAHITQALSNPGD---VIKPMFVINE-MRRIA 187
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRL-SELIRKIWNPRNfkgHVSPHELLQAvSKVSK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 188 RHFRFGNQEDAHEFLQYTVDAMqKACLNGSNKldrhtQATTLVCQIFGGYLR--------------SRVKCLNCKGVSDT 253
Cdd:cd02669 200 KKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 254 FD-PYLDITLEIKAA---QSVNKA--LEQfVKPEQLdgENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRF--ANFTG 325
Cdd:cd02669 274 SVsPFLLLTLDLPPPplfKDGNEEniIPQ-VPLKQL--LKKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFskNNFFK 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954668664 326 GKIAKDVKYP-EYLDIRPYMSQP---NGEPIVYVLYAVLVHTGFNCHAGHYFCYI-KASNGLWYQMND 388
Cdd:cd02669 351 EKNPTIVNFPiKNLDLSDYVHFDkpsLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQD 418
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
735-929 |
2.65e-09 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 61.79 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 735 APGAERGPPEDRDAePQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPP----PSAGEDIV 810
Cdd:PRK07003 361 AVTGGGAPGGGVPA-RVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPaapaPPATADRG 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 811 GDTAPPDLCDPGSLTGDASPLSQDAKgMIAEGPRDSALAEAPEGLSPAPPARSEEPceqpllvhPSGDHARDAQDPSQSL 890
Cdd:PRK07003 440 DDAADGDAPVPAKANARASADSRCDE-RDAQPPADSGSASAPASDAPPDAAFEPAP--------RAAAPSAATPAAVPDA 510
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1954668664 891 GAPEAAERP--PAPVLDMAPAGHPEGDAEPSPGERVEDAAA 929
Cdd:PRK07003 511 RAPAAASREdaPAAAAPPAPEARPPTPAAAAPAARAGGAAA 551
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
734-935 |
3.14e-09 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 61.54 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 734 SAPGAERGPPEDR--DAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVG 811
Cdd:PRK07764 601 PAPASSGPPEEAArpAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 812 DTAPPDLCDPGSLTGDASPLSQDAkgmiAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLG 891
Cdd:PRK07764 681 PPPAPAPAAPAAPAGAAPAQPAPA----PAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA 756
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1954668664 892 APEAAERPPAPVldmAPAGHPEGDAEPSPGERVEDAAAPKAPGP 935
Cdd:PRK07764 757 QPPPPPAPAPAA---APAAAPPPSPPSEEEEMAEDDAPSMDDED 797
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
734-939 |
1.01e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 60.34 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 734 SAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAP-PPRDPGTPATkegaweamAVAPEEPPPSAGEDIVGD 812
Cdd:PHA03247 2727 AARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPaPPAAPAAGPP--------RRLTRPAVASLSESRESL 2798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 813 TAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQpllVHPSGDHARDAqdPSQSLGA 892
Cdd:PHA03247 2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGS---VAPGGDVRRRP--PSRSPAA 2873
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1954668664 893 -PEAAERPPA-----------------PVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAK 939
Cdd:PHA03247 2874 kPAAPARPPVrrlarpavsrstesfalPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
735-941 |
3.66e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 57.94 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 735 APGAERGPPEDRDAEPQPGSPAAESLEE--PDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAV-------APEEPPPSA 805
Cdd:PRK07003 382 APGARAAAAVGASAVPAVTAVTGAAGAAlaPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGdapvpakANARASADS 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 806 GEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPceqpllvhpsgdhARDAQD 885
Cdd:PRK07003 462 RCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAP-------------AAAAPP 528
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1954668664 886 PSQSLGAPEAAERPPAPVLDMAPAghpeGDAEPSPGERVED------AAAPKAPGPSPAKEK 941
Cdd:PRK07003 529 APEARPPTPAAAAPAARAGGAAAA----LDVLRNAGMRVSSdrgaraAAAAKPAAAPAAAPK 586
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
728-938 |
4.23e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 57.58 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 728 GSTDEMSAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGE 807
Cdd:PRK12323 367 QSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 808 DIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAP----PARSEEPCEQPLLVHPSGDHARDA 883
Cdd:PRK12323 447 APAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPweelPPEFASPAPAQPDAAPAGWVAESI 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1954668664 884 QDPSQSLGAPEAAERPPAPVldMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPA 938
Cdd:PRK12323 527 PDPATADPDDAFETLAPAPA--AAPAPRAAAATEPVVAPRPPRASASGLPDMFDG 579
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
735-938 |
7.68e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.26 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 735 APGAERGPPEDRDAEPQPGSPAAESLeePDAAAG----------------LSSTKKAPPPrdPGTPATKEGAWEAMAVAP 798
Cdd:PHA03247 2495 APDPGGGGPPDPDAPPAPSRLAPAIL--PDEPVGepvhprmltwirgleeLASDDAGDPP--PPLPPAAPPAAPDRSVPP 2570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 799 EEPPPSAGEDIVGD-----TAPPDLCDPGSLTGDasplSQDAKGMIAEGPRDSAlAEAPEGLSPAPPARSEEPCEQPLLV 873
Cdd:PHA03247 2571 PRPAPRPSEPAVTSrarrpDAPPQSARPRAPVDD----RGDPRGPAPPSPLPPD-THAPDPPPPSPSPAANEPDPHPPPT 2645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1954668664 874 HPSGDHARDAQDPSQsLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPA 938
Cdd:PHA03247 2646 VPPPERPRDDPAPGR-VSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPE 2709
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
113-409 |
1.43e-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: 54.07 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 113 LQNLGNTCFANAALQcltytpplanymlshehsktchaegfcmmctmqahitqALSNPGDVIKpmfvinemrriarHFRF 192
Cdd:cd02673 2 LVNTGNSCYFNSTMQ--------------------------------------ALSSIGKINT-------------EFDN 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 193 GNQEDAHEFLQYTVDAMQKAC-LNGSNKLDRHTQATTL-VCQIFGGYLRSRVKCLNCKGVSDTFDpyLDITLEIKAAQSV 270
Cdd:cd02673 31 DDQQDAHEFLLTLLEAIDDIMqVNRTNVPPSNIEIKRLnPLEAFKYTIESSYVCIGCSFEENVSD--VGNFLDVSMIDNK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 271 NKALEQFVKPEQLDGENSYKCSKCK-KMVPASKRFTihRSSNVLTLSLKRFANFTGgkIAKDVKypeylDIRPYMSQPNG 349
Cdd:cd02673 109 LDIDELLISNFKTWSPIEKDCSSCKcESAISSERIM--TFPECLSINLKRYKLRIA--TSDYLK-----KNEEIMKKYCG 179
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1954668664 350 EPIVYVLYAVLVHTGFNCHAGHYFCYIKAS--NGLWYQMNDSI---VSTSDIRSVLSQQAYVLFY 409
Cdd:cd02673 180 TDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEirpVSKNDVSTNARSSGYLIFY 244
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
727-929 |
2.41e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 55.38 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 727 KGSTDEMSAPGAERGP--PEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMA--VAPEEPP 802
Cdd:PRK07764 606 SGPPEEAARPAAPAAPaaPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAapAAPPPAP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 803 PSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPceQPLLVHPSGDHARD 882
Cdd:PRK07764 686 APAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP--DPAGAPAQPPPPPA 763
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1954668664 883 AQDPSQSLGAPEAAERPPAPVLDMapaghpegDAEPSPGERVEDAAA 929
Cdd:PRK07764 764 PAPAAAPAAAPPPSPPSEEEEMAE--------DDAPSMDDEDRRDAE 802
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
705-949 |
3.47e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 55.18 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 705 PAPLLSLPEDKILETFRLSNKLKGSTDEMSAPGAE-RGPPEDRDAEPQPGSPAaesleePDAAAGLSSTKK---APPPRD 780
Cdd:PHA03307 75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPgPSSPDPPPPTPPPASPP------PSPAPDLSEMLRpvgSPGPPP 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 781 PG-----------TPATKEGAWEA-----MAVAPEEPPPSAGEDIVGDTAPPDLCDPGSLTGdaSPLSQDAKGMIAEGPR 844
Cdd:PHA03307 149 AAsppaagaspaaVASDAASSRQAalplsSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS--SPISASASSPAPAPGR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 845 DSAlAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPvldmaPAGHPEGDAEPSPGERV 924
Cdd:PHA03307 227 SAA-DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPG-----PASSSSSPRERSPSPSP 300
|
250 260
....*....|....*....|....*
gi 1954668664 925 EDAAAPKAPGPSPAKEKIGSLRKVD 949
Cdd:PHA03307 301 SSPGSGPAPSSPRASSSSSSSRESS 325
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
735-941 |
3.56e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 735 APGAERGPPEDRDAEPQPGSPAAESLEEPDAA---------AGLSSTKKAPPPRDPGTPAT----KEGAWEAMAVA---- 797
Cdd:PHA03247 262 GEGADRAPETARGATGPPPPPEAAAPNGAAAPpdgvwgaalAGAPLALPAPPDPPPPAPAGdaeeEDDEDGAMEVVsplp 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 798 ---------------PEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPlsqDAKGMIAEGPrdsalaeapeGLSPAPPAR 862
Cdd:PHA03247 342 rprqhyplgfpkrrrPTWTPPSSLEDLSAGRHHPKRASLPTRKRRSAR---HAATPFARGP----------GGDDQTRPA 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1954668664 863 SEEPCEQPLLVHPsgdhardaqdpsqslGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEK 941
Cdd:PHA03247 409 APVPASVPTPAPT---------------PVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPDDPDDATRK 472
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
762-951 |
6.86e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 54.09 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 762 EPDAAAGlSSTKKAPPPRDPG---TPATKEGAWEAMAVAPEEPPPSAGediVGDTAPPDLCDPGSLTGDASPLSQDAKGM 838
Cdd:PRK07003 359 EPAVTGG-GAPGGGVPARVAGavpAPGARAAAAVGASAVPAVTAVTGA---AGAALAPKAAAAAAATRAEAPPAAPAPPA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 839 IAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEgDAEP 918
Cdd:PRK07003 435 TADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPD-ARAP 513
|
170 180 190
....*....|....*....|....*....|...
gi 1954668664 919 SPGERVEDAAAPKAPGPSPAKEKIGSLRKVDRG 951
Cdd:PRK07003 514 AAASREDAPAAAAPPAPEARPPTPAAAAPAARA 546
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
730-940 |
2.08e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 52.48 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 730 TDEMSAPGAERGPPEDR-DAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPR--DPGTPATKEG--AWEAMAVAPEEPPPS 804
Cdd:PHA03307 69 TGPPPGPGTEAPANESRsTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPtpPPASPPPSPApdLSEMLRPVGSPGPPP 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 805 AGEDI---VGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPAR-SEEPCEQPLLVHPSGDHA 880
Cdd:PHA03307 149 AASPPaagASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRsSPISASASSPAPAPGRSA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 881 RDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPgERVEDAAAPKAPGPSPAKE 940
Cdd:PHA03307 229 ADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR-IWEASGWNGPSSRPGPASS 287
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
628-938 |
2.57e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 628 IGTIVSSHSPGQDAEDEEATPHelqepmtLNGANSADSDSDPKENGLAPDGASCQGQPAlhseNPFAKANGLPGKlMPAP 707
Cdd:PHA03247 2578 SEPAVTSRARRPDAPPQSARPR-------APVDDRGDPRGPAPPSPLPPDTHAPDPPPP----SPSPAANEPDPH-PPPT 2645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 708 LLSLPEDKILETFRLSNKLKGSTDEMSAPGAErGPPEdrdaepQPGSPAAesleePDAAAGLSSTKKAPPPrdPGTPATK 787
Cdd:PHA03247 2646 VPPPERPRDDPAPGRVSRPRRARRLGRAAQAS-SPPQ------RPRRRAA-----RPTVGSLTSLADPPPP--PPTPEPA 2711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 788 EGAWEAmavAPEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPlsqdakGMIAEGPRDSALAEAPeglSPAPPARSEEPc 867
Cdd:PHA03247 2712 PHALVS---ATPLPPGPAAARQASPALPAAPAPPAVPAGPATP------GGPARPARPPTTAGPP---APAPPAAPAAG- 2778
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954668664 868 EQPLLVHPSGDHARDAqdpSQSLGAPEAAERPPAPVLDMAPAGHPEgdAEPSPGERVEDAAAPKAPGPSPA 938
Cdd:PHA03247 2779 PPRRLTRPAVASLSES---RESLPSPWDPADPPAAVLAPAAALPPA--ASPAGPLPPPTSAQPTAPPPPPG 2844
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
735-1055 |
2.67e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 51.91 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 735 APGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTA 814
Cdd:PRK07764 413 AAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAA 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 815 PPdlcdpgsltGDASPLSQDAKGMIAEGPRDS--ALAEAPEGLSPA------PPARSEEPCEQPL-LVHPSGDHAR--DA 883
Cdd:PRK07764 493 AP---------AAPAAPAAPAGADDAATLRERwpEILAAVPKRSRKtwaillPEATVLGVRGDTLvLGFSTGGLARrfAS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 884 QDPSQSL---------------------GAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEKI 942
Cdd:PRK07764 564 PGNAEVLvtalaeelggdwqveavvgpaPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAP 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 943 GSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDRLSPGERRSLGRCSH--- 1019
Cdd:PRK07764 644 APGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQppq 723
|
330 340 350
....*....|....*....|....*....|....*...
gi 1954668664 1020 --HHSRHRSGVELDWVRHHYTEGERGWGREKFYPDRPR 1055
Cdd:PRK07764 724 aaQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPP 761
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-392 |
2.78e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 50.95 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 111 AGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGfcmMCTMQAHITQALSNpGDVIKPMFVINEMRRIARHF 190
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASD---YPTERRIGGREVSR-SELQRSNQFVYELRSLFNDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 191 RFGN----------------QEDAHEFLQYTVDAMQKACLNGSN-----KLDRHTQATTLVCQIF-GGYLRSRVKCLNCK 248
Cdd:cd02666 78 IHSNtrsvtpskelaylalrQQDVTECIDNVLFQLEVALEPISNafagpDTEDDKEQSDLIKRLFsGKTKQQLVPESMGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 249 GVSD---------TFDPYLDITLEIKA---AQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASK------RFTIHRSS 310
Cdd:cd02666 158 QPSVrtkterflsLLVDVGKKGREIVVllePKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRelismdRYELPSSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 311 NVlTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGE-PIVYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMND 388
Cdd:cd02666 238 DD-IDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLkSYGYRLHAVFIHRG-EASSGHYWVYIKdFEENVWRKYND 315
|
....
gi 1954668664 389 SIVS 392
Cdd:cd02666 316 ETVT 319
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
735-951 |
2.78e-06 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 51.52 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 735 APGAERGPP--EDRDAEPQPgspaAESleepdAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGD 812
Cdd:PRK13108 281 APGALRGSEyvVDEALEREP----AEL-----AAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQ 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 813 TAPPDlcdpgsltGDASPLSQDAKGMIAEGPRDSALA----EAPEGLSPAPPARSEEPCEQPllvhpsgdhardAQDPSQ 888
Cdd:PRK13108 352 VADRD--------GESTPAVEETSEADIEREQPGDLAgqapAAHQVDAEAASAAPEEPAALA------------SEAHDE 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954668664 889 SlgAPEAAERppapvldmapaghpegdAEPSPGERVEDAAAPKAPGPSPAK-EKIGSLRKVDRG 951
Cdd:PRK13108 412 T--EPEVPEK-----------------AAPIPDPAKPDELAVAGPGDDPAEpDGIRRQDDFSSR 456
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
629-973 |
7.32e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.55 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 629 GTIVSSHSPGQDAEDEEATPHelQEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPFAKANGLPGKLMPAPL 708
Cdd:PHA03307 98 ASPAREGSPTPPGPSSPDPPP--PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 709 LSLPEDkiletfrlsnklkgSTDEMSAPGAERGPPEDR----DAEPQPGSPAAESLEEPDAAAGLSStkKAPPPRDPGTP 784
Cdd:PHA03307 176 LSSPEE--------------TARAPSSPPAEPPPSTPPaaasPRPPRRSSPISASASSPAPAPGRSA--ADDAGASSSDS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 785 ATKEGAWEAMAVAPEEPPPSAGEDIVgdtapPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSE 864
Cdd:PHA03307 240 SSSESSGCGWGPENECPLPRPAPITL-----PTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 865 EPCEQPllVHPSGDHARDAQDPSQSlgaPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEKIGS 944
Cdd:PHA03307 315 SSSSSS--SRESSSSSTSSSSESSR---GAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRR 389
|
330 340
....*....|....*....|....*....
gi 1954668664 945 LRKvDRGHYRSRRERSSSGEPARESRSKT 973
Cdd:PHA03307 390 ARA-AVAGRARRRDATGRFPAGRPRPSPL 417
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
733-1138 |
3.29e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 48.63 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 733 MSAPGAERGPPED--RDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAP-------EEPPP 803
Cdd:PHA03307 22 PRPPATPGDAADDllSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTwslstlaPASPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 804 SAGEDIVGDTAPPDlcDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEepceqpllvhPSGDHARDA 883
Cdd:PHA03307 102 REGSPTPPGPSSPD--PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPA----------AVASDAASS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 884 QDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKA-PGPSPAKE-KIGSLRKVDRGHYRSRRERSS 961
Cdd:PHA03307 170 RQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASsPAPAPGRSaADDAGASSSDSSSSESSGCGW 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 962 SGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDRLSPGERRSLGRCSHHHSRHRSGVELDwvrhhytege 1041
Cdd:PHA03307 250 GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSS---------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 1042 rgwgrekfypdrprwdrcryyhdryalyaardwkpfhGGREHERAGLHERPHKDHNRG-RRGCEPARERERHRPSSPRAG 1120
Cdd:PHA03307 320 -------------------------------------SSRESSSSSTSSSSESSRGAAvSPGPSPSRSPSPSRPPPPADP 362
|
410
....*....|....*...
gi 1954668664 1121 APHALAPHPDRFSHDRTA 1138
Cdd:PHA03307 363 SSPRKRPRPSRAPSSPAA 380
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
734-908 |
3.58e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 48.31 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 734 SAPGAERGPPEDRDAEPQ---------PGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEamAVAPEEPPPS 804
Cdd:PRK07003 454 NARASADSRCDERDAQPPadsgsasapASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDA--PAAAAPPAPE 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 805 AGEdivgdTAPPDLCDPGSLTGDASPLS--QDAkGMIAEGPRDSALAEAPEglSPAPPARSEEPCEQPLLVH---PSGDH 879
Cdd:PRK07003 532 ARP-----PTPAAAAPAARAGGAAAALDvlRNA-GMRVSSDRGARAAAAAK--PAAAPAAAPKPAAPRVAVQvptPRARA 603
|
170 180 190
....*....|....*....|....*....|.
gi 1954668664 880 ARDAQDPSQSLGAPEAAE--RPPAPVLDMAP 908
Cdd:PRK07003 604 ATGDAPPNGAARAEQAAEsrGAPPPWEDIPP 634
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
737-939 |
2.49e-04 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 45.59 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 737 GAERGPP-------EDRDAEPQPGSPAAESLEEPDaaagLSSTKKAPPPRDPGTPATKEG-AWEAMAVAPEEPPpsaged 808
Cdd:PRK14086 75 SRELGRPiriaitvDPSAGEPAPPPPHARRTSEPE----LPRPGRRPYEGYGGPRADDRPpGLPRQDQLPTARP------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 809 ivgdtAPPDLCD---PGSLTGDASPLS--QDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPllVHPSGDH-ARD 882
Cdd:PRK14086 145 -----AYPAYQQrpePGAWPRAADDYGwqQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQ--RRRDYDHpRPD 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 883 AQDPSQslgapEAAERP-PAPvldmaPAGHPEGDAEPSPG--ERVEDAAAPKAPGPSPAK 939
Cdd:PRK14086 218 WDRPRR-----DRTDRPePPP-----GAGHVHRGGPGPPErdDAPVVPIRPSAPGPLAAQ 267
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
846-1113 |
3.47e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.89 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 846 SALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVE 925
Cdd:PRK12678 53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 926 DAAAPKAPGPSPAKEKIGSLRKVDRGHyrsrRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDR 1005
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARAD----AAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 1006 LSPGERRslgrcSHHHSRHRsgveldwvrhhytEGERGWGRekfypDRPRWDRCRYYHDRYALYAARDWKPFHGGReher 1085
Cdd:PRK12678 209 REQGDRR-----EERGRRDG-------------GDRRGRRR-----RRDRRDARGDDNREDRGDRDGDDGEGRGGR---- 261
|
250 260
....*....|....*....|....*...
gi 1954668664 1086 aglherphkdhnRGRRGcepaRERERHR 1113
Cdd:PRK12678 262 ------------RGRRF----RDRDRRG 273
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
748-878 |
3.82e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 44.71 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 748 AEPQPGSPAAESLEEPDAAAglSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTAPPDLCDPG--SLT 825
Cdd:PRK14951 369 AAEAAAPAEKKTPARPEAAA--PAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAApaAVA 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1954668664 826 GDASPLSQDAKGMIAEGPRdsalAEAPEGLSPAPPARSEEPCEQPLLVHPSGD 878
Cdd:PRK14951 447 LAPAPPAQAAPETVAIPVR----VAPEPAVASAAPAPAAAPAAARLTPTEEGD 495
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
312-410 |
3.92e-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: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 312 VLTLSLKRFA--NFTGGKIAKDVKYPEYLDIRPYMsqpngepivyvLYAVLVHTGfNCHAGHYFCYI-KASNGLWYQMND 388
Cdd:cd02665 131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYND 198
|
90 100 110
....*....|....*....|....*....|
gi 1954668664 389 SIVSTSDIRSVLSQ--------QAYVLFYI 410
Cdd:cd02665 199 ISVTESSWEEVERDsfgggrnpSAYCLMYI 228
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
727-939 |
4.92e-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: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 727 KGSTDEMSAPGAERGPPEDRDAEPQPGSP--AAESLEEPDAAAGLSSTKKAPPPRD------PGTPATKEGAWEAMAVAP 798
Cdd:PLN03209 345 KPVTPEAPSPPIEEEPPQPKAVVPRPLSPytAYEDLKPPTSPIPTPPSSSPASSKSvdavakPAEPDVVPSPGSASNVPE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 799 EEPPPSAGED--------IVGDTAPPDLCDPGSLTGDASPLSQDAK-GMIAEGPRDSALAEA-------PEGLSPAPPAR 862
Cdd:PLN03209 425 VEPAQVEAKKtrplspyaRYEDLKPPTSPSPTAPTGVSPSVSSTSSvPAVPDTAPATAATDAaapppanMRPLSPYAVYD 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954668664 863 SEEPCEQPLLVHPSGDHArdaqdPSQSLGAPEAAERPPaPVLDMAPAGHPEGDAEP-SPGERVEDAAAPKAPGPSPAK 939
Cdd:PLN03209 505 DLKPPTSPSPAAPVGKVA-----PSSTNEVVKVGNSAP-PTALADEQHHAQPKPRPlSPYTMYEDLKPPTSPTPSPVL 576
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
422-938 |
4.95e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 422 THPTHSPGQSSPRPVISQRVVTNKQAAPGFIGPQLPSHMIKNP---PHLNGTGPLKDTPSSSMSSPNGNSSVNRASPVNA 498
Cdd:PHA03247 2587 RRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPspsPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR 2666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 499 SASVQNWSvnRSSVIPEHPKKQKITISIHnklPVRQCQSQPnlhsnSLENPTKPVPSSTITNSAVQSTSNASTMSVSSKV 578
Cdd:PHA03247 2667 ARRLGRAA--QASSPPQRPRRRAARPTVG---SLTSLADPP-----PPPPTPEPAPHALVSATPLPPGPAAARQASPALP 2736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 579 TKPIPRSeSCSQPVMNGKSKLNSSVLVPYGAESSEDSDEESKGLGKEngiGTIVSSHSPGQDAEDEEATPHELQEPMTLN 658
Cdd:PHA03247 2737 AAPAPPA-VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR---LTRPAVASLSESRESLPSPWDPADPPAAVL 2812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 659 GANSADSDSDPKENGLAPDGASCQGQPALHSEnPFAKANGLPGKLMPAPLLSlpedkiletfrlsnKLKGSTDEMSAPGA 738
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPG-PPPPSLPLGGSVAPGGDVR--------------RRPPSRSPAAKPAA 2877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 739 ERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTAPPDL 818
Cdd:PHA03247 2878 PARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 819 CDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPeglSPAPPARSEEP----CEQPLLVHPSGDHArdAQDPSQSLGAPE 894
Cdd:PHA03247 2958 AVPQPWLGALVPGRVAVPRFRVPQPAPSREAPAS---STPPLTGHSLSrvssWASSLALHEETDPP--PVSLKQTLWPPD 3032
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1954668664 895 AAERPPAPVLDMAPAGHPEGDA-EPSPGERVEDAAAPKAPGPSPA 938
Cdd:PHA03247 3033 DTEDSDADSLFDSDSERSDLEAlDPLPPEPHDPFAHEPDPATPEA 3077
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
772-941 |
5.51e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.48 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 772 TKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEdiVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEA 851
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPA--AAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 852 PeglSPAPPARSEEPCEQPLlvhPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDA---- 927
Cdd:PRK12323 454 P---AAAPAAAARPAAAGPR---PVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAesip 527
|
170
....*....|....*...
gi 1954668664 928 ----AAPKAPGPSPAKEK 941
Cdd:PRK12323 528 dpatADPDDAFETLAPAP 545
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
840-938 |
5.56e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 840 AEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDhARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPS 919
Cdd:PRK07764 405 APAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPS-PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPA 483
|
90
....*....|....*....
gi 1954668664 920 PGERVEDAAAPKAPGPSPA 938
Cdd:PRK07764 484 PPAAPAPAAAPAAPAAPAA 502
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
732-939 |
6.16e-04 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 43.90 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 732 EMSAPG----AERGPPEDRDAEPQPGSPAAESLEEPDAAA------------GLSSTKKAPPP-------RDPGTPATKE 788
Cdd:COG5180 254 EMRPPAdakeRRRAAIGDTPAAEPPGLPVLEAGSEPQSDApeaetarpidvkGVASAPPATRPvrppggaRDPGTPRPGQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 789 GAWEAMAV----APEEPPPS----AGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAP-------- 852
Cdd:COG5180 334 PTERPAGVpeaaSDAGQPPSayppAEEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMgagdlvqa 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 853 EGLSPAPPARSEEPCEQPLLVHPSGDH-ARDAQDPSQSLGAPEAAERPPAPVldMAPAGHPEGDAePSPGERVEDAAAPK 931
Cdd:COG5180 414 ALDGGGRETASLGGAAGGAGQGPKADFvPGDAESVSGPAGLADQAGAAASTA--MADFVAPVTDA-TPVDVADVLGVRPD 490
|
....*...
gi 1954668664 932 APGPSPAK 939
Cdd:COG5180 491 AILGGNVA 498
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
728-996 |
6.99e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 728 GSTDEMSAPGAERGPPEDRDAEPQPGS-PAAESLEEPDAAAGLSSTKKAPPPRDPGtpATKEGAW-EAMAVAPEEPPPSA 805
Cdd:PRK07764 454 PSPPPAAAPSAQPAPAPAAAPEPTAAPaPAPPAAPAPAAAPAAPAAPAAPAGADDA--ATLRERWpEILAAVPKRSRKTW 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 806 GedIVGDTAPPDLCDPGSLT-GDASPLsqdAKGMIAEGPRDSALAEA-----------------------PEGLSPAPPA 861
Cdd:PRK07764 532 A--ILLPEATVLGVRGDTLVlGFSTGG---LARRFASPGNAEVLVTAlaeelggdwqveavvgpapgaagGEGPPAPASS 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 862 RSEEPCEQPllvhPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEK 941
Cdd:PRK07764 607 GPPEEAARP----AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPP 682
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1954668664 942 IGSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAP 996
Cdd:PRK07764 683 PAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADD 737
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
555-778 |
7.40e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 43.93 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 555 SSTITNSAVQSTSnASTMSVSSKVTKPIPRSESCSQpvmngksklNSSVLVPYGAESSEDSDEESKGLGKENGIGtivss 634
Cdd:PRK08691 369 NAVIENTELQSPS-AQTAEKETAAKKPQPRPEAETA---------QTPVQTASAAAMPSEGKTAGPVSNQENNDV----- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 635 hSPGQDAEDEEATPhELQEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPfakanglpgklMPAPLLSLPED 714
Cdd:PRK08691 434 -PPWEDAPDEAQTA-AGTAQTSAKSIQTASEAETPPENQVSKNKAADNETDAPLSEVP-----------SENPIQATPND 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954668664 715 KILETFRLSNKLKGST---------DEMSAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPP 778
Cdd:PRK08691 501 EAVETETFAHEAPAEPfygygfpdnDCPPEDGAEIPPPDWEHAAPADTAGGGADEEAEAGGIGGNNTPSAPPP 573
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-409 |
8.76e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 42.88 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 111 AGLQNLGNTCFANAALQCLTYTPPLANYMLsheHSKTCHAEGFCMMC-------TMQAHITQALSN--PGDVIKPMFVIN 181
Cdd:cd02672 16 AGLENHITNSYCNSLLQLLYFIPPFRNFTA---IILVACPKESCLLCelgylfsTLIQNFTRFLLEtiSQDQLGTPFSCG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 182 EMRR-------IARHFRFGNQEDAHEFLQytvdamqkaCLNGSNKLDRHTQATTLVCQifggYLRSRVKCLNCKGVSDTF 254
Cdd:cd02672 93 TSRNsvsllytLSLPLGSTKTSKESTFLQ---------LLKRSLDLEKVTKAWCDTCC----KYQPLEQTTSIRHLPDIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 255 DPYLDITLEiKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKmvpaskrftihrssnvltlslkrfanftggkiAKDVKY 334
Cdd:cd02672 160 LLVLVINLS-VTNGEFDDINVVLPSGKVMQNKVSPKAIDHDK--------------------------------LVKNRG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 335 PEYLDirpymsqpngepiVYVLYAVLVHTGFNCHAGHYFCYIKASN-----GLWYQMNDSIVSTsdirsvLSQQAYVLFY 409
Cdd:cd02672 207 QESIY-------------KYELVGYVCEINDSSRGQHNVVFVIKVNeesthGRWYLFNDFLVTP------VSELAYILLY 267
|
|
| PRK14949 |
PRK14949 |
DNA polymerase III subunits gamma and tau; Provisional |
501-936 |
9.78e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237863 [Multi-domain] Cd Length: 944 Bit Score: 43.56 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 501 SVQNWSVNRSSVIpEHPKKQKITISIHNKLPVRQCQSQPNLHSNSlENPTKPVPSSTiTNSAVQsTSNASTMSVSSKVTK 580
Cdd:PRK14949 362 PVKRWQVDDPAEI-SLPEGQTPSALAAAVQAPHANEPQFVNAAPA-EKKTALTEQTT-AQQQVQ-AANAEAVAEADASAE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 581 PIPRSESCSQPVMNGKSKLNSSVlvpygaessedsdeeskglgkengigTIVSSHSPGQDAEDEEATPHELQEPMTLNGA 660
Cdd:PRK14949 438 PADTVEQALDDESELLAALNAEQ--------------------------AVILSQAQSQGFEASSSLDADNSAVPEQIDS 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 661 NSADSDSDPK-ENGLAPD--GASCQGQPALHSENPFAKANGLPGKLMP-------APLLSLPEDKILETFRLSNKLKGST 730
Cdd:PRK14949 492 TAEQSVVNPSvTDTQVDDtsASNNSAADNTVDDNYSAEDTLESNGLDEgdyaqdsAPLDAYQDDYVAFSSESYNALSDDE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 731 DEMSAPGAERGPPEDRDAEPQPGSP-----AAESLEEPD------AA-----AGL-------SSTKKAPPPRDPGTPatk 787
Cdd:PRK14949 572 QHSANVQSAQSAAEAQPSSQSLSPIsavttAAASLADDDildavlAArdsllSDLdalspkeGDGKKSSADRKPKTP--- 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 788 egaweamavaPEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAkgmIAEGPRDSALAEAPeGLSPAPPARS--EE 865
Cdd:PRK14949 649 ----------PSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQS---VPEAALASGSAPAP-PPVPDPYDRPpwEE 714
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954668664 866 PCEQPLLVHPSGDHARDAQDPSQslgapEAAERPPAPVLDMAPAGHPEGDAEPSPgerveDAAAPKAPGPS 936
Cdd:PRK14949 715 APEVASANDGPNNAAEGNLSESV-----EDASNSELQAVEQQATHQPQVQAEAQS-----PASTTALTQTS 775
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
736-924 |
1.21e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 736 PGAERGPPEDRDAEPQPGSPAAESL---------EEPDAAAGLSSTKKAPPPRDPgtPATKEGAWEAMAVAPEEPPPSAg 806
Cdd:PHA03307 284 PASSSSSPRERSPSPSPSSPGSGPApssprasssSSSSRESSSSSTSSSSESSRG--AAVSPGPSPSRSPSPSRPPPPA- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 807 edivgDTAPPdlcdPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARseePCEQPllvhpsgdhardaqdP 886
Cdd:PHA03307 361 -----DPSSP----RKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRF---PAGRP---------------R 413
|
170 180 190
....*....|....*....|....*....|....*...
gi 1954668664 887 SQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERV 924
Cdd:PHA03307 414 PSPLDAGAASGAFYARYPLLTPSGEPWPGSPPPPPGRV 451
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
734-929 |
1.24e-03 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 43.02 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 734 SAPGAERGPPEDR--DAEPQPGSPAAESLEEPDAAAglsstkKAPPPRDPGTPATKegaWEAMAVAPEEPPP--SAGEDI 809
Cdd:PHA03321 452 STPACARRARAQRarDAGPEYVDPLGALRRLPAGAA------PPPEPAAAPSPATY---YTRMGGGPPRLPPrnRATETL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 810 VGDTAPP------DLCDPGSLTGDASPLSQDAKGMIAEgpRDSALAEAPEGLSPAPPAR-SEEPCEQPL-----LVHPSG 877
Cdd:PHA03321 523 RPDWGPPaaappeQMEDPYLEPDDDRFDRRDGAAAAAT--SHPREAPAPDDDPIYEGVSdSEEPVYEEIptprvYQNPLP 600
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954668664 878 DHARDAQDP---------------------SQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAA 929
Cdd:PHA03321 601 RPMEGAGEPpdldaptspwveeenpiygwgDSPLFSPPPAARFPPPDPALSPEPPALPAHRPRPGALAPDGPA 673
|
|
| KLF14_N |
cd21576 |
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ... |
761-939 |
1.64e-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: 41.34 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 761 EEPDAAAGLSSTKKAPPPRDPGtPATKEGAWEAMAVAPEEPPPSAGedivgDTAPPDLCdpgsltgdASPLSqDAKGMIA 840
Cdd:cd21576 32 EGAGGAAGSEVGAAPPESALPG-PGPPGPAWVPPLLQVPAPSPGAG-----GAAPHLLA--------ASVLA-DLRGGAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 841 EGPRDSALaEAPEGLSPAP-PARSEEPCEQPLLVHPSGDHArdAQDPSQSLGAPEAAERPPAPvldmapaghpegdaePS 919
Cdd:cd21576 97 EGSREDSG-EAPRASSGSSdPARGSSPTLGSEPAPASGEDA--VSGPESSFGAPAIPSAPAAP---------------GA 158
|
170 180
....*....|....*....|
gi 1954668664 920 PGERVEDAAAPKAPGPSPAK 939
Cdd:cd21576 159 PAVSGEVPGGAPGAGPAPAA 178
|
|
| PHA01929 |
PHA01929 |
putative scaffolding protein |
858-951 |
2.29e-03 |
|
putative scaffolding protein
Pssm-ID: 177328 Cd Length: 306 Bit Score: 41.58 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 858 APPARSEEPCEQPLLVHPSGDHARDAQDPSQSlgAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKA---PG 934
Cdd:PHA01929 19 VPPAAAPTPQPNPVIQPQAPVQPGQPGAPQQL--AIPTQQPQPVPTSAMTPHVVQQAPAQPAPAAPPAAGAALPEaleVP 96
|
90
....*....|....*..
gi 1954668664 935 PSPAKEKIGSLRKVDRG 951
Cdd:PHA01929 97 PPPAFTPNGEIVGTLAG 113
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
724-970 |
3.10e-03 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 41.97 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 724 NKLKGSTDEMSAPGAERGPPEDRDAEP--QPGSPAAESLEEPDAAAGLSStkKAPPPRDPGTPATKEGAWEAMAVAPEEP 801
Cdd:COG5180 70 GKPQLPSVAEPEAYLDPAPPKSSPDTPeeQLGAPAGDLLVLPAAKTPELA--AGALPAPAAAAALPKAKVTREATSASAG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 802 PPSAGEDIvGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDsALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHAR 881
Cdd:COG5180 148 VALAAALL-QRSDPILAKDPDGDSASTLPPPAEKLDKVLTEPRD-ALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHPR 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 882 DAQDPSQSLGAPEAAE--------------RPPAPVLDMAPAGHPEGDAEPSPGERVedaaAPKAPGPSPAKEKIGSLRK 947
Cdd:COG5180 226 PEAASSPKVDPPSTSEarsrpatvdaqpemRPPADAKERRRAAIGDTPAAEPPGLPV----LEAGSEPQSDAPEAETARP 301
|
250 260
....*....|....*....|...
gi 1954668664 948 VDRGHYRSRRERSSSGEPARESR 970
Cdd:COG5180 302 IDVKGVASAPPATRPVRPPGGAR 324
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
756-939 |
3.35e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 41.97 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 756 AAESLEEPDAAAGLSSTKKAPPPRdPGTPATKEGAWEAMAVAPEEPPPsagediVGDTAPPDLCDPGSLT------GDAS 829
Cdd:PHA03379 401 AREALEKASEPTYGTPRPPVEKPR-PEVPQSLETATSHGSAQVPEPPP------VHDLEPGPLHDQHSMApcpvaqLPPG 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 830 PLSQDAKGMIAEGP-RDSALAEAPeglSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAP 908
Cdd:PHA03379 474 PLQDLEPGDQLPGVvQDGRPACAP---VPAPAGPIVRPWEASLSQVPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPP 550
|
170 180 190
....*....|....*....|....*....|.
gi 1954668664 909 AGHPEGDAEPSPGERVEDAAAPKAPGPSPAK 939
Cdd:PHA03379 551 LIAMQGPGETSGIVRVRERWRPAPWTPNPPR 581
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
762-1008 |
3.44e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 41.84 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 762 EPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDivgDTAPPDLCDPGSLTG-DASPLSQDAKGMIA 840
Cdd:PLN03209 332 ESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYE---DLKPPTSPIPTPPSSsPASSKSVDAVAKPA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 841 EgPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSlgaPEAAERPPApvldmapaghPEGDAEPSP 920
Cdd:PLN03209 409 E-PDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPT---APTGVSPSV----------SSTSSVPAV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 921 GERVEDAAAPKAPGPSPAKEKIGSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHP 1000
Cdd:PLN03209 475 PDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRP 554
|
....*...
gi 1954668664 1001 ghgdrLSP 1008
Cdd:PLN03209 555 -----LSP 557
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
843-940 |
3.85e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 41.33 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 843 PRDSALAEAPEGLSPAP----PARSEEPCEQPLLVHPSGDHARDAQDPSqslgapeaaerPPAPVLDMAPAGHPEGDAEP 918
Cdd:PRK14950 362 PVPAPQPAKPTAAAPSPvrptPAPSTRPKAAAAANIPPKEPVRETATPP-----------PVPPRPVAPPVPHTPESAPK 430
|
90 100
....*....|....*....|..
gi 1954668664 919 SPGERVEDAAAPKAPGPSPAKE 940
Cdd:PRK14950 431 LTRAAIPVDEKPKYTPPAPPKE 452
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
734-898 |
4.05e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 41.62 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 734 SAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIvgdt 813
Cdd:PRK14951 372 AAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVAL---- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 814 aPPDLCDPGSLTGDASPLsqdakgMIAEGPRDSALAEAPEGLSPAPPARSEEPCE------------------------Q 869
Cdd:PRK14951 448 -APAPPAQAAPETVAIPV------RVAPEPAVASAAPAPAAAPAAARLTPTEEGDvwhatvqqlaaaeaitalarelalQ 520
|
170 180
....*....|....*....|....*....
gi 1954668664 870 PLLVHPSGDHArDAQDPSQSLGAPEAAER 898
Cdd:PRK14951 521 SELVARDGDQW-LLRVERESLNQPGARER 548
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
795-942 |
4.48e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 795 AVAPEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPlSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVH 874
Cdd:PRK07764 373 GLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAA-APAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAG 451
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954668664 875 PSGDHARDAQDPSQSLGAPEAAERPPApvldmAPAghPEGDAEPSPGERVEDAAAPKAPGPSPAKEKI 942
Cdd:PRK07764 452 GAPSPPPAAAPSAQPAPAPAAAPEPTA-----APA--PAPPAAPAPAAAPAAPAAPAAPAGADDAATL 512
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
821-938 |
5.96e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.01 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 821 PGSLTGDASPLSQDAKGMIAEGPRDSAL-----AEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDP---SQSLGA 892
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAAPaaaapAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAarqASARGP 444
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1954668664 893 PEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPA 938
Cdd:PRK12323 445 GGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPA 490
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
652-807 |
6.57e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 40.73 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 652 QEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPFAKANGLPGKlMPAPLLSLPEDKILETfrlsnklKGSTD 731
Cdd:PRK13108 293 DEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDE-VAAESVVQVADRDGES-------TPAVE 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1954668664 732 EMSAPGAERGPPEDRDAEP--QPGSPAAESLEEPDAAAGL-SSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGE 807
Cdd:PRK13108 365 ETSEADIEREQPGDLAGQApaAHQVDAEAASAAPEEPAALaSEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAE 443
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
803-938 |
6.58e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 40.85 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 803 PSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPceqpllvhpsgdhard 882
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAP---------------- 429
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1954668664 883 AQDPSQSLGAPEAAERPPAPVLDMAPAghPEGDAEP---SPGERVEDAAAPKAPGPSPA 938
Cdd:PRK14951 430 AAAAPAAAPAAAPAAVALAPAPPAQAA--PETVAIPvrvAPEPAVASAAPAPAAAPAAA 486
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
708-806 |
6.83e-03 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 40.75 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 708 LLSLPEDKILETFRLSNKLKGSTDEMSAPGAERGPPedrdAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATK 787
Cdd:COG5373 12 VLALLVGLLGRVARLRRRVEELEAELAEAAEAASAP----AEPEPEAAAAATAAAPEAAPAPVPEAPAAPPAAAEAPAPA 87
|
90
....*....|....*....
gi 1954668664 788 EGAwEAMAVAPEEPPPSAG 806
Cdd:COG5373 88 AAA-PPAEAEPAAAPAAAS 105
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
740-896 |
7.14e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 740 RGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPgtPATKEgawEAMAVAPEEPPPSAGEDIVGDTAPPDlc 819
Cdd:PRK07764 384 RLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAP--AAAPQ---PAPAPAPAPAPPSPAGNAPAGGAPSP-- 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1954668664 820 dpgsltgdasplsqdakgmiaegPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAA 896
Cdd:PRK07764 457 -----------------------PPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAA 510
|
|
| |
