|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02534 |
PLN02534 |
UDP-glycosyltransferase |
1-487 |
0e+00 |
|
UDP-glycosyltransferase
Pssm-ID: 215293 [Multi-domain] Cd Length: 491 Bit Score: 723.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1 MASTLSNQLelqpHFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNATRLESFFARAKQSSLSISLLEIPFPCLQ 80
Cdd:PLN02534 1 KAVSKAKQL----HFVLIPLMAQGHMIPMIDMARLLAERGVIVSLVTTPQNASRFAKTIDRARESGLPIRLVQIPFPCKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 81 VGLPLGCENLDTLPSRSLLRNFYKALSLLQQPLEQFLSRHHLNPTCIISDKYLYWTAQTAHKFKCPRVVFHGTGCFSLLS 160
Cdd:PLN02534 77 VGLPIGCENLDTLPSRDLLRKFYDAVDKLQQPLERFLEQAKPPPSCIISDKCLSWTSKTAQRFNIPRIVFHGMCCFSLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 161 SHNLQLYSPHTSIDSNSQPFLVPGLPHKIEITKSQLPGSLIKSPDFDDFRDKITKAEQEAYGVVVNSFSELENGYYQNYE 240
Cdd:PLN02534 157 SHNIRLHNAHLSVSSDSEPFVVPGMPQSIEITRAQLPGAFVSLPDLDDVRNKMREAESTAFGVVVNSFNELEHGCAEAYE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 241 RAISKKLWCIGPVSLCNENSIEKYNRGNKASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTRPFI 320
Cdd:PLN02534 237 KAIKKKVWCVGPVSLCNKRNLDKFERGNKASIDETQCLEWLDSMKPRSVIYACLGSLCRLVPSQLIELGLGLEASKKPFI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 321 WVIKNrDENCSELEKWLSEEEFERKTKGRGLIIRGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQF 400
Cdd:PLN02534 317 WVIKT-GEKHSELEEWLVKENFEERIKGRGLLIKGWAPQVLILSHPAIGGFLTHCGWNSTIEGICSGVPMITWPLFAEQF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 401 LNEKLVVEILKIGVRVGVEGAVRWGEEERVGVMAKKEEIEKAIEMVMDG-GEEGEERRRRVGDLSKMAPKAMENGGSSYV 479
Cdd:PLN02534 396 LNEKLIVEVLRIGVRVGVEVPVRWGDEERVGVLVKKDEVEKAVKTLMDDgGEEGERRRRRAQELGVMARKAMELGGSSHI 475
|
....*...
gi 1731019548 480 NLSLFIED 487
Cdd:PLN02534 476 NLSILIQD 483
|
|
| RT_LTR |
cd01647 |
RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long ... |
1416-1592 |
2.07e-94 |
|
RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long terminal repeats (LTRs) in their DNA copies but not in their RNA template. RT catalyzes DNA replication from an RNA template, and is responsible for the replication of retroelements. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs are present in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and Caulimoviruses.
Pssm-ID: 238825 Cd Length: 177 Bit Score: 302.98 E-value: 2.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1416 GFIRPSVSPWGAPVLFVKKKDGSMRLCIDYRELNKVTVKNRYPLPRIDDLFDQLQGATVFSKIDLRSGYHQLRIRDGDIP 1495
Cdd:cd01647 1 GIIEPSSSPYASPVVVVKKKDGKLRLCVDYRKLNKVTIKDRYPLPTIDELLEELAGAKVFSKLDLRSGYHQIPLAEESRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1496 KTAFRSRYGHYEFVVMSFGLTNAPAVFMDLMNRVFKEFLDSFVIVFIDDILIYSKTEAEHEEHLHQVLETLRANKLYAKF 1575
Cdd:cd01647 81 KTAFRTPFGLYEYTRMPFGLKNAPATFQRLMNKILGDLLGDFVEVYLDDILVYSKTEEEHLEHLREVLERLREAGLKLNP 160
|
170
....*....|....*..
gi 1731019548 1576 SKCEFWLRKVTFLGHVV 1592
Cdd:cd01647 161 EKCEFGVPEVEFLGHIV 177
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
13-448 |
5.51e-67 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 233.21 E-value: 5.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 13 PHFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNatrLESFFARAKQSSLSISLLEIPFPCLQVglplgcENLDT 92
Cdd:cd03784 1 MRILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFN---FADLVEAAGLTFVPVGDDPDELELDSE------TNLGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 93 LPSRSLLRNFYKALSLLQQPLEQFLsRHHLNPTCIISDKYLYWTAQTAHKFKCPRVVFHgtgcfsllsshnlqlysphts 172
Cdd:cd03784 72 DSLLELLRRLLKAADELLDDLLAAL-RSSWKPDLVIADPFAYAGPLVAEELGIPSVRLF--------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 173 idsnSQPFLVPGLPHKIEITKSQLPGSLIKSPDFDDFRDKITKAEQEAYGVVVNSFSelengyyqNYERAISKKLWCIGP 252
Cdd:cd03784 130 ----TGPATLLSAYLHPFGVLNLLLSSLLEPELFLDPLLEVLDRLRERLGLPPFSLV--------LLLLRLVPPLYVIGP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 253 VSLCNE-------NSIEKYNRGNKASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLG-QCLESSTRPFIWVIK 324
Cdd:cd03784 198 TFPSLPpdrprlpSVLGGLRIVPKNGPLPDELWEWLDKQPPRSVVYVSFGSMVRDLPEELLELIaEALASLGQRFLWVVG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 325 NrdencselekwlSEEEFERKTKGRGLIIRgWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNeK 404
Cdd:cd03784 278 P------------DPLGGLERLPDNVLVVK-WVPQDELLAHPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNN-A 343
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1731019548 405 LVVEILKIGVRVGVEgavrwgeeervgvMAKKEEIEKAIEMVMD 448
Cdd:cd03784 344 ARVEELGAGVELDKD-------------ELTAEELAKAVREVLE 374
|
|
| RNase_HI_RT_Ty3 |
cd09274 |
Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) ... |
1686-1801 |
1.30e-57 |
|
Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Ty3/Gypsy family widely distributed among the genomes of plants, fungi and animals. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.
Pssm-ID: 260006 [Multi-domain] Cd Length: 121 Bit Score: 195.02 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1686 VIYSDASKKGLGCVLMQ-----QGKVVAYASRQLKIHEQNYPTHDLELAAVVFALKIWRHYLYGEKIQIYTDHKSLKYFF 1760
Cdd:cd09274 1 ILETDASDYGIGAVLSQedddgKERPIAFFSRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRPFTVYTDHKALKYLL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1731019548 1761 TQKELNMRQRRWLELVKDYDCEILYHPGKANVVADALSRKV 1801
Cdd:cd09274 81 TQKDLNGRLARWLLLLSEFDFEIEYRPGKENVVADALSRLP 121
|
|
| RT_RNaseH |
pfam17917 |
RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) ... |
1685-1775 |
2.42e-41 |
|
RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) activities allow reverse transcriptases to convert the single-stranded retroviral RNA genome into double-stranded DNA, which is integrated into the host chromosome during infection. This entry represents the RNase H like domain.
Pssm-ID: 465565 Cd Length: 104 Bit Score: 148.04 E-value: 2.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1685 FVIYSDASKKGLGCVLMQQG-----KVVAYASRQLKIHEQNYPTHDLELAAVVFALKIWRHYLYGEKIQIYTDHKSLKYF 1759
Cdd:pfam17917 6 FILETDASDYGIGAVLSQKDedgkeRPIAYASRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRKFTVYTDHKPLKYL 85
|
90
....*....|....*.
gi 1731019548 1760 FTQKELNMRQRRWLEL 1775
Cdd:pfam17917 86 FTPKELNGRLARWALF 101
|
|
| RVT_1 |
pfam00078 |
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ... |
1432-1592 |
6.27e-38 |
|
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. Reverse transcriptases occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses.
Pssm-ID: 395031 [Multi-domain] Cd Length: 189 Bit Score: 141.67 E-value: 6.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1432 VKKKD-GSMRLC----IDYRELNKVTVK-------NRYPLPRIDDLFDQLQGATVFSKIDLRSGYHQLRIRDGDIPKTAF 1499
Cdd:pfam00078 1 IPKKGkGKYRPIsllsIDYKALNKIIVKrlkpenlDSPPQPGFRPGLAKLKKAKWFLKLDLKKAFDQVPLDELDRKLTAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1500 R-----------SRYGHYEFVVMSFGLTNAPAVFMDLMNRVFKEFL---DSFVIVFIDDILIYSKTEAEHEEHLHQVLET 1565
Cdd:pfam00078 81 TtppininwngeLSGGRYEWKGLPQGLVLSPALFQLFMNELLRPLRkraGLTLVRYADDILIFSKSEEEHQEALEEVLEW 160
|
170 180
....*....|....*....|....*....
gi 1731019548 1566 LRANKLYAKFSKCEFWL--RKVTFLGHVV 1592
Cdd:pfam00078 161 LKESGLKINPEKTQFFLksKEVKYLGVTL 189
|
|
| RVP_2 |
pfam08284 |
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ... |
1173-1304 |
3.97e-32 |
|
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases.
Pssm-ID: 400537 Cd Length: 134 Bit Score: 122.92 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1173 QGRVFATTRQEAERAGTVVTGTLPILGHYAFVLFDSGSSHSFISSVFVQHVGLEVEPLGSVLSVSTPSGEVLLSKEQIKA 1252
Cdd:pfam08284 2 QGRVNHLSAEEAEASPDVIQGTFLVNSIPATVLFDSGATHSFISHAFVGKLKLPVESLSNPLCIETPTGGSVTTNLICPS 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1731019548 1253 CRVEIANRMLDVTLLVLDMQDFDVILGMDWLSANHANIDCYGKEVVFNPPSE 1304
Cdd:pfam08284 82 CPIEIQGISFLADLILLDMKDLDVILGMDWLSKNKANIDCARRTVTLTKERE 133
|
|
| Retrotrans_gag |
pfam03732 |
Retrotransposon gag protein; Gag or Capsid-like proteins from LTR retrotransposons. There is a ... |
943-1038 |
4.67e-20 |
|
Retrotransposon gag protein; Gag or Capsid-like proteins from LTR retrotransposons. There is a central motif QGXXEXXXXXFXXLXXH that is common to Retroviridae gag-proteins, but is poorly conserved.
Pssm-ID: 367628 Cd Length: 97 Bit Score: 87.00 E-value: 4.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 943 AVFFLEDRGTAWWETAERmlGGDVSKITWEQFKENFYAKFFSANVKHAKLQEFLNLEQGDMTVEQYDAEFDMLSRFAPDM 1022
Cdd:pfam03732 3 AVHSLRGAALTWWKSLVA--RSIDAFDSWDELKDAFLKRFFPSIRKDLLRNELRSLRQGTESVREYVERFKRLARQLPHH 80
|
90
....*....|....*.
gi 1731019548 1023 VRDEAARTEKFVRGLR 1038
Cdd:pfam03732 81 GRDEEALISAFLRGLR 96
|
|
| Integrase_H2C2 |
pfam17921 |
Integrase zinc binding domain; This zinc binding domain is found in a wide variety of ... |
1891-1949 |
5.79e-16 |
|
Integrase zinc binding domain; This zinc binding domain is found in a wide variety of integrase proteins.
Pssm-ID: 465569 [Multi-domain] Cd Length: 58 Bit Score: 73.82 E-value: 5.79e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1731019548 1891 DSAVKTELLTEAHSSpfTMHPGSTKMYQDLRSVYWWRGMKRDVADFVSRCLVCQQVKAP 1949
Cdd:pfam17921 2 PKSLRKEILKEAHDS--GGHLGIEKTLARLRRRYWWPGMRKDVKKYVKSCETCQRRKPS 58
|
|
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
289-448 |
7.84e-12 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 70.13 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 289 VLYICLGSLCRMLPSQ-LIQLGQCLESSTRPFIWviknrdencselekwlSEEEFERKTKGRGLIIRGWAPQLLILSHWS 367
Cdd:pfam00201 277 VVVFSLGSMVSNIPEEkANAIASALAQIPQKVLW----------------RFDGTKPSTLGNNTRLVKWLPQNDLLGHPK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 368 TGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKLVVEilkigvrVGVEGAVRWGEeervgvMAkKEEIEKAIEMVM 447
Cdd:pfam00201 341 TRAFITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEA-------KGAAVTLNVLT------MT-SEDLLNALKEVI 406
|
.
gi 1731019548 448 D 448
Cdd:pfam00201 407 N 407
|
|
| retropepsin_like |
cd00303 |
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ... |
1219-1283 |
9.35e-10 |
|
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.
Pssm-ID: 133136 Cd Length: 92 Bit Score: 57.35 E-value: 9.35e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731019548 1219 FVQHVGLEVEPLGSVLSVSTPSGEVLLSKEQIKACRVEIANRMLDVTLLVLDMQDFDVILGMDWL 1283
Cdd:cd00303 27 LAKKLGLPPRLLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDLLSYDVILGRPWL 91
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
352-409 |
6.59e-09 |
|
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) subfamily of the UDP-glucuronosyltransferase family. Members include a number of glucosyl transferases for macrolide antibiotic inactivation, but also include transferases of glucose-related sugars for macrolide antibiotic production. [Cellular processes, Toxin production and resistance]
Pssm-ID: 273616 [Multi-domain] Cd Length: 392 Bit Score: 60.47 E-value: 6.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1731019548 352 IIRGWAPQLLILSHwsTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKLVVEI 409
Cdd:TIGR01426 278 EVRQWVPQLEILKK--ADAFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAEL 333
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
351-416 |
8.15e-09 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 59.10 E-value: 8.15e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731019548 351 LIIRGWAPQLLILSHwsTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKLVVEiLKIGVRV 416
Cdd:COG1819 171 VRVVDYVPQDALLPR--ADAVVHHGGAGTTAEALRAGVPQVVVPFGGDQPLNAARVER-LGAGLAL 233
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
497-672 |
4.35e-07 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 55.46 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 497 AQPSRNRNRAVAELPAAPGESSKPICAAE--RPSEQPSLARRsrveaasaRPQPTRQPAEsrrfdPTQAQPKRQSVAVAE 574
Cdd:PHA03378 674 YQPSPTGANTMLPIQWAPGTMQPPPRAPTpmRPPAAPPGRAQ--------RPAAATGRAR-----PPAAAPGRARPPAAA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 575 RSRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREIP--VPSRAASAQAEPV-LSSSSRAARTKLAP 651
Cdd:PHA03378 741 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPrgAPTPQPPPQAGPTsMQLMPRAAPGQQGP 820
|
170 180
....*....|....*....|.
gi 1731019548 652 STYILRGISSVGARALQPPSR 672
Cdd:PHA03378 821 TKQILRQLLTGGVKRGRPSLK 841
|
|
| transpos_IS481 |
NF033577 |
IS481 family transposase; null |
1950-2078 |
3.65e-05 |
|
IS481 family transposase; null
Pssm-ID: 468094 [Multi-domain] Cd Length: 283 Bit Score: 47.97 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1950 RQHPAGLLQplsvpgwkwesvsMDfITGLPKTL-RGYTVIWVVVDRLTKSAH--FVPGKSTYTASKwgqlYMTEIVRLHG 2026
Cdd:NF033577 124 RAHPGELWH-------------ID-IKKLGRIPdVGRLYLHTAIDDHSRFAYaeLYPDETAETAAD----FLRRAFAEHG 185
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1731019548 2027 VPV-SIISDRDARFTSKFwKGLQLAL---GTRLDFSTAFHPQTDGQTERLNQILED 2078
Cdd:NF033577 186 IPIrRVLTDNGSEFRSRA-HGFELALaelGIEHRRTRPYHPQTNGKVERFHRTLKD 240
|
|
| rve |
pfam00665 |
Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into ... |
1963-2063 |
4.41e-05 |
|
Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain pfam02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain pfam00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyzes the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.
Pssm-ID: 459897 [Multi-domain] Cd Length: 98 Bit Score: 44.23 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1963 PGWKWEsvsMDFITGLPKTLRGYTVIWVVVDRLTK--SAHFVPGKSTYTAskWGQLYMTEIVRLHGVPVSIISDRDARFT 2040
Cdd:pfam00665 1 PNQLWQ---GDFTYIRIPGGGGKLYLLVIVDDFSReiLAWALSSEMDAEL--VLDALERAIAFRGGVPLIIHSDNGSEYT 75
|
90 100
....*....|....*....|...
gi 1731019548 2041 SKFWKGLQLALGTRLDFSTAFHP 2063
Cdd:pfam00665 76 SKAFREFLKDLGIKPSFSRPGNP 98
|
|
| RnhA |
COG0328 |
Ribonuclease HI [Replication, recombination and repair]; |
1686-1800 |
4.79e-05 |
|
Ribonuclease HI [Replication, recombination and repair];
Pssm-ID: 440097 [Multi-domain] Cd Length: 136 Bit Score: 45.22 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1686 VIYSDAS------KKGLGCVLMQQGKVvayasRQLKIHEQNYPTHDLELAAVVFALKIWRHyLYGEKIQIYTDHKSLKYF 1759
Cdd:COG0328 4 EIYTDGAcrgnpgPGGWGAVIRYGGEE-----KELSGGLGDTTNNRAELTALIAALEALKE-LGPCEVEIYTDSQYVVNQ 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1731019548 1760 FTQKELNMRQRRW------------LELVKDYDCEILYHPGKA----NVVADALSRK 1800
Cdd:COG0328 78 ITGWIHGWKKNGWkpvknpdlwqrlDELLARHKVTFEWVKGHAghpgNERADALANK 134
|
|
| CD_POL_like |
cd18979 |
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins ... |
2268-2315 |
3.58e-03 |
|
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins (Z195D10.9), and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Zea maize Z195D10.9 protein, and other putative TY3/gypsy retrotransposon polyproteins. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.
Pssm-ID: 349335 Cd Length: 48 Bit Score: 37.47 E-value: 3.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1731019548 2268 QPVEVLAREVKKLRSREIpLVKilWQNHGVEEATWEKEEDMRAQYPEL 2315
Cdd:cd18979 2 FPEKVLDIRQRDKGNKEF-LVQ--WQGLSVEEATWEPYKDLVQQFPDF 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
505-650 |
4.22e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 505 RAVAE--LPAAPGEsskpicaAERPSEQPSlaRRSRVEAASARPQPT----RQPAESRRF---DPTQAQpkrQSVAVAER 575
Cdd:NF041483 173 RAEAEqaLAAARAE-------AERLAEEAR--QRLGSEAESARAEAEailrRARKDAERLlnaASTQAQ---EATDHAEQ 240
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731019548 576 SRGSRTTNSRrAARNPEAEASRAKPSRVSPvasraasppvASRAAREipvpsraASAQAEPVLSSSSRAARTKLA 650
Cdd:NF041483 241 LRSSTAAESD-QARRQAAELSRAAEQRMQE----------AEEALRE-------ARAEAEKVVAEAKEAAAKQLA 297
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
496-627 |
9.18e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 40.91 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 496 AAQPSRNRNRAVAELPAAPGEsskpicAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRFDPTQAQPKRQSVAVAER 575
Cdd:NF040712 206 AREPADARPEEVEPAPAAEGA------PATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1731019548 576 SRGSRTTNSRRAARNPE----AEASRAKPSRVSPVASRAASPPVASRAAREIPVPS 627
Cdd:NF040712 280 PPAPGAAETPEAAEPPApapaAPAAPAAPEAEEPARPEPPPAPKPKRRRRRASVPS 335
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02534 |
PLN02534 |
UDP-glycosyltransferase |
1-487 |
0e+00 |
|
UDP-glycosyltransferase
Pssm-ID: 215293 [Multi-domain] Cd Length: 491 Bit Score: 723.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1 MASTLSNQLelqpHFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNATRLESFFARAKQSSLSISLLEIPFPCLQ 80
Cdd:PLN02534 1 KAVSKAKQL----HFVLIPLMAQGHMIPMIDMARLLAERGVIVSLVTTPQNASRFAKTIDRARESGLPIRLVQIPFPCKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 81 VGLPLGCENLDTLPSRSLLRNFYKALSLLQQPLEQFLSRHHLNPTCIISDKYLYWTAQTAHKFKCPRVVFHGTGCFSLLS 160
Cdd:PLN02534 77 VGLPIGCENLDTLPSRDLLRKFYDAVDKLQQPLERFLEQAKPPPSCIISDKCLSWTSKTAQRFNIPRIVFHGMCCFSLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 161 SHNLQLYSPHTSIDSNSQPFLVPGLPHKIEITKSQLPGSLIKSPDFDDFRDKITKAEQEAYGVVVNSFSELENGYYQNYE 240
Cdd:PLN02534 157 SHNIRLHNAHLSVSSDSEPFVVPGMPQSIEITRAQLPGAFVSLPDLDDVRNKMREAESTAFGVVVNSFNELEHGCAEAYE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 241 RAISKKLWCIGPVSLCNENSIEKYNRGNKASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTRPFI 320
Cdd:PLN02534 237 KAIKKKVWCVGPVSLCNKRNLDKFERGNKASIDETQCLEWLDSMKPRSVIYACLGSLCRLVPSQLIELGLGLEASKKPFI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 321 WVIKNrDENCSELEKWLSEEEFERKTKGRGLIIRGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQF 400
Cdd:PLN02534 317 WVIKT-GEKHSELEEWLVKENFEERIKGRGLLIKGWAPQVLILSHPAIGGFLTHCGWNSTIEGICSGVPMITWPLFAEQF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 401 LNEKLVVEILKIGVRVGVEGAVRWGEEERVGVMAKKEEIEKAIEMVMDG-GEEGEERRRRVGDLSKMAPKAMENGGSSYV 479
Cdd:PLN02534 396 LNEKLIVEVLRIGVRVGVEVPVRWGDEERVGVLVKKDEVEKAVKTLMDDgGEEGERRRRRAQELGVMARKAMELGGSSHI 475
|
....*...
gi 1731019548 480 NLSLFIED 487
Cdd:PLN02534 476 NLSILIQD 483
|
|
| PLN03007 |
PLN03007 |
UDP-glucosyltransferase family protein |
14-487 |
6.34e-137 |
|
UDP-glucosyltransferase family protein
Pssm-ID: 178584 [Multi-domain] Cd Length: 482 Bit Score: 437.75 E-value: 6.34e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 14 HFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNATRLESFFARAKQ--SSLSISLLEIPFPCLQVGLPLGCENLD 91
Cdd:PLN03007 7 HILFFPFMAHGHMIPTLDMAKLFSSRGAKSTILTTPLNAKIFEKPIEAFKNlnPGLEIDIQIFNFPCVELGLPEGCENVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 92 TLPSRS------LLRNFYKALSLLQQPLEQFLSRhhLNPTCIISDKYLYWTAQTAHKFKCPRVVFHGTGCFSLLSSHNLQ 165
Cdd:PLN03007 87 FITSNNnddsgdLFLKFLFSTKYFKDQLEKLLET--TRPDCLVADMFFPWATEAAEKFGVPRLVFHGTGYFSLCASYCIR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 166 LYSPHTSIDSNSQPFLVPGLPHKIEITKSQLPGSLIKSPdFDDFRDKITKAEQEAYGVVVNSFSELENGYYQNYERAISK 245
Cdd:PLN03007 165 VHKPQKKVASSSEPFVIPDLPGDIVITEEQINDADEESP-MGKFMKEVRESEVKSFGVLVNSFYELESAYADFYKSFVAK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 246 KLWCIGPVSLCNENSIEKYNRGNKASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTRPFIWVIkN 325
Cdd:PLN03007 244 RAWHIGPLSLYNRGFEEKAERGKKANIDEQECLKWLDSKKPDSVIYLSFGSVASFKNEQLFEIAAGLEGSGQNFIWVV-R 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 326 RDENCSELEKWLSEEeFERKTKGRGLIIRGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKL 405
Cdd:PLN03007 323 KNENQGEKEEWLPEG-FEERTKGKGLIIRGWAPQVLILDHQATGGFVTHCGWNSLLEGVAAGLPMVTWPVGAEQFYNEKL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 406 VVEILKIGVRVGVEGAVRwgeeeRVGVMAKKEEIEKAIEMVMdGGEEGEERRRRVGDLSKMAPKAMENGGSSYVNLSLFI 485
Cdd:PLN03007 402 VTQVLRTGVSVGAKKLVK-----VKGDFISREKVEKAVREVI-VGEEAEERRLRAKKLAEMAKAAVEEGGSSFNDLNKFM 475
|
..
gi 1731019548 486 ED 487
Cdd:PLN03007 476 EE 477
|
|
| RT_LTR |
cd01647 |
RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long ... |
1416-1592 |
2.07e-94 |
|
RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long terminal repeats (LTRs) in their DNA copies but not in their RNA template. RT catalyzes DNA replication from an RNA template, and is responsible for the replication of retroelements. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs are present in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and Caulimoviruses.
Pssm-ID: 238825 Cd Length: 177 Bit Score: 302.98 E-value: 2.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1416 GFIRPSVSPWGAPVLFVKKKDGSMRLCIDYRELNKVTVKNRYPLPRIDDLFDQLQGATVFSKIDLRSGYHQLRIRDGDIP 1495
Cdd:cd01647 1 GIIEPSSSPYASPVVVVKKKDGKLRLCVDYRKLNKVTIKDRYPLPTIDELLEELAGAKVFSKLDLRSGYHQIPLAEESRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1496 KTAFRSRYGHYEFVVMSFGLTNAPAVFMDLMNRVFKEFLDSFVIVFIDDILIYSKTEAEHEEHLHQVLETLRANKLYAKF 1575
Cdd:cd01647 81 KTAFRTPFGLYEYTRMPFGLKNAPATFQRLMNKILGDLLGDFVEVYLDDILVYSKTEEEHLEHLREVLERLREAGLKLNP 160
|
170
....*....|....*..
gi 1731019548 1576 SKCEFWLRKVTFLGHVV 1592
Cdd:cd01647 161 EKCEFGVPEVEFLGHIV 177
|
|
| PLN02863 |
PLN02863 |
UDP-glucoronosyl/UDP-glucosyl transferase family protein |
7-486 |
4.10e-79 |
|
UDP-glucoronosyl/UDP-glucosyl transferase family protein
Pssm-ID: 215465 Cd Length: 477 Bit Score: 270.97 E-value: 4.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 7 NQLELQPHFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNATRLESFFARakqsSLSISLLEIPFPClQVGLPLG 86
Cdd:PLN02863 4 LNKPAGTHVLVFPFPAQGHMIPLLDLTHRLALRGLTITVLVTPKNLPFLNPLLSK----HPSIETLVLPFPS-HPSIPSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 87 CENLDTLPSrSLLRNFYKALSLLQQPLEQFLSRHHLNPTCIISDKYLYWTAQTAHKFKCPRVVFHGTGCFSLLSSHNLQL 166
Cdd:PLN02863 79 VENVKDLPP-SGFPLMIHALGELYAPLLSWFRSHPSPPVAIISDMFLGWTQNLACQLGIRRFVFSPSGAMALSIMYSLWR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 167 YSPHTSIDSNSQPFL----VPGLPHKIEITKSQLPGSLIKSPDFDDFRDKITKAEQEAYGVVVNSFSELENGYYQNYERA 242
Cdd:PLN02863 158 EMPTKINPDDQNEILsfskIPNCPKYPWWQISSLYRSYVEGDPAWEFIKDSFRANIASWGLVVNSFTELEGIYLEHLKKE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 243 I-SKKLWCIGPVSLCNENSIEKYNRGNKASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTRPFIW 321
Cdd:PLN02863 238 LgHDRVWAVGPILPLSGEKSGLMERGGPSSVSVDDVMTWLDTCEDHKVVYVCFGSQVVLTKEQMEALASGLEKSGVHFIW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 322 VIKNRDEncSELEKWLSEEEFERKTKGRGLIIRGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFL 401
Cdd:PLN02863 318 CVKEPVN--EESDYSNIPSGFEDRVAGRGLVIRGWAPQVAILSHRAVGAFLTHCGWNSVLEGLVAGVPMLAWPMAADQFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 402 NEKLVVEILKIGVRVgVEGAvrwgeeervGVMAKKEEIEKAIemvMDGGEEGEERRRRVGDLSKMAPKAMENGGSSYVNL 481
Cdd:PLN02863 396 NASLLVDELKVAVRV-CEGA---------DTVPDSDELARVF---MESVSENQVERERAKELRRAALDAIKERGSSVKDL 462
|
....*
gi 1731019548 482 SLFIE 486
Cdd:PLN02863 463 DGFVK 467
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
13-448 |
5.51e-67 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 233.21 E-value: 5.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 13 PHFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNatrLESFFARAKQSSLSISLLEIPFPCLQVglplgcENLDT 92
Cdd:cd03784 1 MRILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFN---FADLVEAAGLTFVPVGDDPDELELDSE------TNLGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 93 LPSRSLLRNFYKALSLLQQPLEQFLsRHHLNPTCIISDKYLYWTAQTAHKFKCPRVVFHgtgcfsllsshnlqlysphts 172
Cdd:cd03784 72 DSLLELLRRLLKAADELLDDLLAAL-RSSWKPDLVIADPFAYAGPLVAEELGIPSVRLF--------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 173 idsnSQPFLVPGLPHKIEITKSQLPGSLIKSPDFDDFRDKITKAEQEAYGVVVNSFSelengyyqNYERAISKKLWCIGP 252
Cdd:cd03784 130 ----TGPATLLSAYLHPFGVLNLLLSSLLEPELFLDPLLEVLDRLRERLGLPPFSLV--------LLLLRLVPPLYVIGP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 253 VSLCNE-------NSIEKYNRGNKASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLG-QCLESSTRPFIWVIK 324
Cdd:cd03784 198 TFPSLPpdrprlpSVLGGLRIVPKNGPLPDELWEWLDKQPPRSVVYVSFGSMVRDLPEELLELIaEALASLGQRFLWVVG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 325 NrdencselekwlSEEEFERKTKGRGLIIRgWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNeK 404
Cdd:cd03784 278 P------------DPLGGLERLPDNVLVVK-WVPQDELLAHPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNN-A 343
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1731019548 405 LVVEILKIGVRVGVEgavrwgeeervgvMAKKEEIEKAIEMVMD 448
Cdd:cd03784 344 ARVEELGAGVELDKD-------------ELTAEELAKAVREVLE 374
|
|
| RNase_HI_RT_Ty3 |
cd09274 |
Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) ... |
1686-1801 |
1.30e-57 |
|
Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Ty3/Gypsy family widely distributed among the genomes of plants, fungi and animals. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.
Pssm-ID: 260006 [Multi-domain] Cd Length: 121 Bit Score: 195.02 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1686 VIYSDASKKGLGCVLMQ-----QGKVVAYASRQLKIHEQNYPTHDLELAAVVFALKIWRHYLYGEKIQIYTDHKSLKYFF 1760
Cdd:cd09274 1 ILETDASDYGIGAVLSQedddgKERPIAFFSRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRPFTVYTDHKALKYLL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1731019548 1761 TQKELNMRQRRWLELVKDYDCEILYHPGKANVVADALSRKV 1801
Cdd:cd09274 81 TQKDLNGRLARWLLLLSEFDFEIEYRPGKENVVADALSRLP 121
|
|
| PLN02448 |
PLN02448 |
UDP-glycosyltransferase family protein |
14-487 |
2.73e-51 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215247 [Multi-domain] Cd Length: 459 Bit Score: 189.06 E-value: 2.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 14 HFVLVPLMAQGHMIPMIDIATLLARR--GVFVTFVTTpynatrlESF--FARAKQSSLSISLLEIPfpclqvglplgceN 89
Cdd:PLN02448 12 HVVAMPYPGRGHINPMMNLCKLLASRkpDILITFVVT-------EEWlgLIGSDPKPDNIRFATIP-------------N 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 90 LdtLPSRsLLRN-----FYKALSL-LQQPLEQFLSRHHLNPTCIISDKYLYWTAQTAHKFKCPRVVFHGTGC--FSLLss 161
Cdd:PLN02448 72 V--IPSE-LVRAadfpgFLEAVMTkMEAPFEQLLDRLEPPVTAIVADTYLFWAVGVGNRRNIPVASLWTMSAtfFSVF-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 162 HNLQLYSPHT------SIDSNSQPFLVPGLPhkiEITKSQLPGSLIKS--PDFDDFRDKITKAEQEAYgVVVNSFSELEN 233
Cdd:PLN02448 147 YHFDLLPQNGhfpvelSESGEERVDYIPGLS---STRLSDLPPIFHGNsrRVLKRILEAFSWVPKAQY-LLFTSFYELEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 234 GYYQNYERAISKKLWCIGPV----SLCNENSIEKYNRGnkasieQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLG 309
Cdd:PLN02448 223 QAIDALKSKFPFPVYPIGPSipymELKDNSSSSNNEDN------EPDYFQWLDSQPEGSVLYVSLGSFLSVSSAQMDEIA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 310 QCLESSTRPFIWVIknRDEnCSELEKWLSeeeferktkGRGLIIrGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVP 389
Cdd:PLN02448 297 AGLRDSGVRFLWVA--RGE-ASRLKEICG---------DMGLVV-PWCDQLKVLCHSSVGGFWTHCGWNSTLEAVFAGVP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 390 MITWPQFAEQFLNEKLVVEILKIGVRVgvegavrwGEEERVGVMAKKEEIEKAIEMVMDGGEEGEER-RRRVGDLSKMAP 468
Cdd:PLN02448 364 MLTFPLFWDQPLNSKLIVEDWKIGWRV--------KREVGEETLVGREEIAELVKRFMDLESEEGKEmRRRAKELQEICR 435
|
490
....*....|....*....
gi 1731019548 469 KAMENGGSSYVNLSLFIED 487
Cdd:PLN02448 436 GAIAKGGSSDTNLDAFIRD 454
|
|
| PLN02410 |
PLN02410 |
UDP-glucoronosyl/UDP-glucosyl transferase family protein |
16-443 |
4.36e-47 |
|
UDP-glucoronosyl/UDP-glucosyl transferase family protein
Pssm-ID: 178032 [Multi-domain] Cd Length: 451 Bit Score: 176.77 E-value: 4.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 16 VLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNATRLESFFARAKQSSLSISLLEIPFpclqvglplgcENLDTLps 95
Cdd:PLN02410 11 VLVPVPAQGHISPMMQLAKTLHLKGFSITIAQTKFNYFSPSDDFTDFQFVTIPESLPESDF-----------KNLGPI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 96 rSLLRNFYKALSL-LQQPLEQFLSRHHLNPTCIISDKYLYWTAQTAHKFKCPRVVFHGTGC--------FSLLSSHNLQ- 165
Cdd:PLN02410 78 -EFLHKLNKECQVsFKDCLGQLVLQQGNEIACVVYDEFMYFAEAAAKEFKLPNVIFSTTSAtafvcrsvFDKLYANNVLa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 166 -LYSPhtsidSNSQPFLVPGLpHKIEItkSQLPGSLIKSPD--FDDFRDKITKaeQEAYGVVVNSFSELENGYYQNYERA 242
Cdd:PLN02410 157 pLKEP-----KGQQNELVPEF-HPLRC--KDFPVSHWASLEsiMELYRNTVDK--RTASSVIINTASCLESSSLSRLQQQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 243 ISKKLWCIGPVSLCNENSIEKYNrgnkasiEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTRPFIWV 322
Cdd:PLN02410 227 LQIPVYPIGPLHLVASAPTSLLE-------ENKSCIEWLNKQKKNSVIFVSLGSLALMEINEVMETASGLDSSNQQFLWV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 323 IKNRDENCSELEKWLSEEeFERKTKGRGLIIRgWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLN 402
Cdd:PLN02410 300 IRPGSVRGSEWIESLPKE-FSKIISGRGYIVK-WAPQKEVLSHPAVGGFWSHCGWNSTLESIGEGVPMICKPFSSDQKVN 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1731019548 403 EKLVVEILKIGVRV-------GVEGAVRW------GEEERVGVMAKKEEIEKAI 443
Cdd:PLN02410 378 ARYLECVWKIGIQVegdldrgAVERAVKRlmveeeGEEMRKRAISLKEQLRASV 431
|
|
| PLN02670 |
PLN02670 |
transferase, transferring glycosyl groups |
14-416 |
7.47e-47 |
|
transferase, transferring glycosyl groups
Pssm-ID: 178275 [Multi-domain] Cd Length: 472 Bit Score: 176.63 E-value: 7.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 14 HFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNATRLESFfarAKQSSLSISLLEIPFPCLQvGLPLGCENLDTL 93
Cdd:PLN02670 8 HVAMFPWLAMGHLIPFLRLSKLLAQKGHKISFISTPRNLHRLPKI---PSQLSSSITLVSFPLPSVP-GLPSSAESSTDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 94 P--SRSLLRnfyKALSLLQQPLEQFLSRHhlNPTCIISDKYLYWTAQTAHKFkcprvvfhGTGC--FSLLSSHNLQLYSP 169
Cdd:PLN02670 84 PytKQQLLK---KAFDLLEPPLTTFLETS--KPDWIIYDYASHWLPSIAAEL--------GISKafFSLFTAATLSFIGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 170 HTSI----DSNSQP--FLV--PGLPHKI-------EITKSQLPGSLIKSPDFDDFRDKITKAEQEAygVVVNSFSELENG 234
Cdd:PLN02670 151 PSSLmeggDLRSTAedFTVvpPWVPFESnivfryhEVTKYVEKTEEDETGPSDSVRFGFAIGGSDV--VIIRSSPEFEPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 235 YYQNYERAISKKLWCIGPVSLCNENSIEKYNRGNKasiEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLES 314
Cdd:PLN02670 229 WFDLLSDLYRKPIIPIGFLPPVIEDDEEDDTIDVK---GWVRIKEWLDKQRVNSVVYVALGTEASLRREEVTELALGLEK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 315 STRPFIWVIKNRDENCSELEKWLsEEEFERKTKGRGLIIRGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWP 394
Cdd:PLN02670 306 SETPFFWVLRNEPGTTQNALEML-PDGFEERVKGRGMIHVGWVPQVKILSHESVGGFLTHCGWNSVVEGLGFGRVLILFP 384
|
410 420
....*....|....*....|..
gi 1731019548 395 QFAEQFLNEKLvVEILKIGVRV 416
Cdd:PLN02670 385 VLNEQGLNTRL-LHGKKLGLEV 405
|
|
| PLN02210 |
PLN02210 |
UDP-glucosyl transferase |
12-489 |
2.49e-46 |
|
UDP-glucosyl transferase
Pssm-ID: 215127 [Multi-domain] Cd Length: 456 Bit Score: 174.84 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 12 QPHFVLVPLMAQGHMIPMIDIA--TLLARRGVFVTFVTTpynatrlesffaraKQSSLSISLLEIP-FPCLQVGLPLGCE 88
Cdd:PLN02210 8 ETHVLMVTLAFQGHINPMLKLAkhLSLSSKNLHFTLATT--------------EQARDLLSTVEKPrRPVDLVFFSDGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 89 NLDTLPSRSLLRNFYK--ALSLLQQPLEQFLSrhhlnptCIISDKYLYWT--AQTAHKFKCPRVVFHGTGCFSLLSSHNL 164
Cdd:PLN02210 74 KDDPRAPETLLKSLNKvgAKNLSKIIEEKRYS-------CIISSPFTPWVpaVAAAHNIPCAILWIQACGAYSVYYRYYM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 165 QLySPHTSIDSNSQPFLVPGLPhKIEItkSQLPGSLIKS--PDFDDFRDKITKAEQEAYGVVVNSFSELENGYYQNYerA 242
Cdd:PLN02210 147 KT-NSFPDLEDLNQTVELPALP-LLEV--RDLPSFMLPSggAHFNNLMAEFADCLRYVKWVLVNSFYELESEIIESM--A 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 243 ISKKLWCIGP-VS---LCNENsiEKYNRGNKASIEQSN--CLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESST 316
Cdd:PLN02210 221 DLKPVIPIGPlVSpflLGDDE--EETLDGKNLDMCKSDdcCMEWLDKQARSSVVYISFGSMLESLENQVETIAKALKNRG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 317 RPFIWVI--KNRDENCSELEKWLSEeeferktkGRGLIIRgWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWP 394
Cdd:PLN02210 299 VPFLWVIrpKEKAQNVQVLQEMVKE--------GQGVVLE-WSPQEKILSHMAISCFVTHCGWNSTIETVVAGVPVVAYP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 395 QFAEQFLNEKLVVEILKIGVRV---GVEGAVrwgeeervgvmaKKEEIEKAIEMVMDgGEEGEERRRRVGDLSKMAPKAM 471
Cdd:PLN02210 370 SWTDQPIDARLLVDVFGIGVRMrndAVDGEL------------KVEEVERCIEAVTE-GPAAADIRRRAAELKHVARLAL 436
|
490
....*....|....*...
gi 1731019548 472 ENGGSSYVNLSLFIEDPP 489
Cdd:PLN02210 437 APGGSSARNLDLFISDIT 454
|
|
| PLN00164 |
PLN00164 |
glucosyltransferase; Provisional |
13-501 |
5.47e-46 |
|
glucosyltransferase; Provisional
Pssm-ID: 215084 [Multi-domain] Cd Length: 480 Bit Score: 174.09 E-value: 5.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 13 PHFVLVPLMAQGHMIPMIDIAT-LLARRG-------VFVTFVTTPYNATRLESFFARAKQSSLSISLLEIPfpclQVGLP 84
Cdd:PLN00164 4 PTVVLLPVWGSGHLMSMLEAGKrLLASSGggalsltVLVMPPPTPESASEVAAHVRREAASGLDIRFHHLP----AVEPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 85 LGCENLDTLPSRSLLR---NFYKALSLLQQPLeqflsrhhlnpTCIISDKYLYWTAQTAHKFKCPRVVFHGTGCfSLLSs 161
Cdd:PLN00164 80 TDAAGVEEFISRYIQLhapHVRAAIAGLSCPV-----------AALVVDFFCTPLLDVARELAVPAYVYFTSTA-AMLA- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 162 hnLQLYSP--HTSI----DSNSQPFLVPGLPhkiEITKSQLPGSLI--KSPDFDDFR---DKITkaeqEAYGVVVNSFSE 230
Cdd:PLN00164 147 --LMLRLPalDEEVavefEEMEGAVDVPGLP---PVPASSLPAPVMdkKSPNYAWFVyhgRRFM----EAAGIIVNTAAE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 231 LENGYYQnyerAISK----------KLWCIGPVslcnensiekYNRGNKASIEQSN--CLNWLDSMIPKSVLYICLGSLC 298
Cdd:PLN00164 218 LEPGVLA----AIADgrctpgrpapTVYPIGPV----------ISLAFTPPAEQPPheCVRWLDAQPPASVVFLCFGSMG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 299 RMLPSQLIQLGQCLESSTRPFIWVIKNR---------DENCSELekwLSEEEFERkTKGRGLIIRGWAPQLLILSHWSTG 369
Cdd:PLN00164 284 FFDAPQVREIAAGLERSGHRFLWVLRGPpaagsrhptDADLDEL---LPEGFLER-TKGRGLVWPTWAPQKEILAHAAVG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 370 GFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKLVVEILKIGVRVGV-------------EGAVR--WGEEERVGVMA 434
Cdd:PLN00164 360 GFVTHCGWNSVLESLWHGVPMAPWPLYAEQHLNAFELVADMGVAVAMKVdrkrdnfveaaelERAVRslMGGGEEEGRKA 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731019548 435 KkeeiEKAIEMvmdggeegeerrrrvgdlsKMA-PKAMENGGSSYVNLSLFIEDppsiLLCSAAQPSR 501
Cdd:PLN00164 440 R----EKAAEM-------------------KAAcRKAVEEGGSSYAALQRLARE----IRHGAVAPTR 480
|
|
| PLN02173 |
PLN02173 |
UDP-glucosyl transferase family protein |
10-485 |
2.25e-42 |
|
UDP-glucosyl transferase family protein
Pssm-ID: 177830 [Multi-domain] Cd Length: 449 Bit Score: 162.89 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 10 ELQPHFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPY--NATRLESffarakqsSLSISLLEIPFPCLQVGLplgc 87
Cdd:PLN02173 3 KMRGHVLAVPFPSQGHITPIRQFCKRLHSKGFKTTHTLTTFifNTIHLDP--------SSPISIATISDGYDQGGF---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 88 ENLDTLPSrsLLRNFYKALSllqQPLEQFLSRHHL--NP-TCIISDKYLYWTAQTAHKFKCPRVVFHGTGC-------FS 157
Cdd:PLN02173 71 SSAGSVPE--YLQNFKTFGS---KTVADIIRKHQStdNPiTCIVYDSFMPWALDLAREFGLAAAPFFTQSCavnyinyLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 158 LLSSHNLQLysPHTSIdsnsqPFL-VPGLPHKIEITKSQLPGSLIKSPDFDDFrdkitkaeQEAYGVVVNSFSELEngYY 236
Cdd:PLN02173 146 YINNGSLTL--PIKDL-----PLLeLQDLPTFVTPTGSHLAYFEMVLQQFTNF--------DKADFVLVNSFHDLD--LH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 237 QNYERAISKKLWCIGPV--SLCNENSIEK---YNRGNKASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQC 311
Cdd:PLN02173 209 ENELLSKVCPVLTIGPTvpSMYLDQQIKSdndYDLNLFDLKEAALCTDWLDKRPQGSVVYIAFGSMAKLSSEQMEEIASA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 312 LesSTRPFIWVIKNrdencSELEKwLSEEEFERKTKGRGLIIRgWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMI 391
Cdd:PLN02173 289 I--SNFSYLWVVRA-----SEESK-LPPGFLETVDKDKSLVLK-WSPQLQVLSNKAIGCFMTHCGWNSTMEGLSLGVPMV 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 392 TWPQFAEQFLNEKLVVEILKIGVRVgvegavrwgEEERVGVMAKKEEIEKAIEMVMDGGEEGEERRRRVGdLSKMAPKAM 471
Cdd:PLN02173 360 AMPQWTDQPMNAKYIQDVWKVGVRV---------KAEKESGIAKREEIEFSIKEVMEGEKSKEMKENAGK-WRDLAVKSL 429
|
490
....*....|....
gi 1731019548 472 ENGGSSYVNLSLFI 485
Cdd:PLN02173 430 SEGGSTDININTFV 443
|
|
| PLN02167 |
PLN02167 |
UDP-glycosyltransferase family protein |
16-487 |
4.35e-42 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215112 [Multi-domain] Cd Length: 475 Bit Score: 162.66 E-value: 4.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 16 VLVPLMAQGHMIPMIDIATLLARRGVFVTFVT-----TPYnATRLESFFARAKQSSLSISLLEIPfpclQVGLPLGCENL 90
Cdd:PLN02167 7 IFVPFPSTGHILVTIEFAKRLINLDRRIHTITilywsLPF-APQADAFLKSLIASEPRIRLVTLP----EVQDPPPMELF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 91 DTLPSRSLLRNFYKALSLLQQPLEQFLSRHHLNPTC----IISDKYLYWTAQTAHKFKCPRVVFHgTGCFSLLS-----S 161
Cdd:PLN02167 82 VKASEAYILEFVKKMVPLVRDALSTLVSSRDESDSVrvagLVLDFFCVPLIDVGNEFNLPSYIFL-TCNAGFLGmmkylP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 162 HNLQLYSPHTSIDSNSQPFLVPGLPHKIEiTKSQLPGSLIKspdfDDFRDKITKAEQ--EAYGVVVNSFSELENGYYQNY 239
Cdd:PLN02167 161 ERHRKTASEFDLSSGEEELPIPGFVNSVP-TKVLPPGLFMK----ESYEAWVEIAERfpEAKGILVNSFTELEPNAFDYF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 240 ERAISK--KLWCIGPVsLCNENSIEKynrgNKASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTR 317
Cdd:PLN02167 236 SRLPENypPVYPVGPI-LSLKDRTSP----NLDSSDRDRIMRWLDDQPESSVVFLCFGSLGSLPAPQIKEIAQALELVGC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 318 PFIWVIK-NRDENCSELEkwLSEEEFERKTKGRGLIIrGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQF 396
Cdd:PLN02167 311 RFLWSIRtNPAEYASPYE--PLPEGFMDRVMGRGLVC-GWAPQVEILAHKAIGGFVSHCGWNSVLESLWFGVPIATWPMY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 397 AEQFLNEKLVVEILKIGVRVGVEGAVRWGEeervgvMAKKEEIEKAIEMVMDggeEGEERRRRVGDLSKMAPKAMENGGS 476
Cdd:PLN02167 388 AEQQLNAFTMVKELGLAVELRLDYVSAYGE------IVKADEIAGAVRSLMD---GEDVPRKKVKEIAEAARKAVMDGGS 458
|
490
....*....|.
gi 1731019548 477 SYVNLSLFIED 487
Cdd:PLN02167 459 SFVAVKRFIDD 469
|
|
| PLN03004 |
PLN03004 |
UDP-glycosyltransferase |
16-447 |
1.47e-41 |
|
UDP-glycosyltransferase
Pssm-ID: 178581 Cd Length: 451 Bit Score: 160.63 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 16 VLVPLMAQGHMIPMIDIATLLARR----GVFVTFVTTPYNATRLESFFarakqSSLSISLLEIPFPCLQVGLPLGCENLD 91
Cdd:PLN03004 7 VLYPAPPIGHLVSMVELGKTILSKnpslSIHIILVPPPYQPESTATYI-----SSVSSSFPSITFHHLPAVTPYSSSSTS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 92 TLPSRSLLRNFYkALSLLQQPLEQFLSRHHLNPTCIISDKYLYWTAQTAHKFKCPRVVFHGTGCFSLLSShnlqLYSPht 171
Cdd:PLN03004 82 RHHHESLLLEIL-CFSNPSVHRTLFSLSRNFNVRAMIIDFFCTAVLDITADFTFPVYFFYTSGAACLAFS----FYLP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 172 SIDSNSQ-------PFL-VPGLPhkiEITKSQLPGSLIKSPD-----FDDFRDKITKAEqeayGVVVNSFSELENGYYQN 238
Cdd:PLN03004 155 TIDETTPgknlkdiPTVhIPGVP---PMKGSDMPKAVLERDDevydvFIMFGKQLSKSS----GIIINTFDALENRAIKA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 239 Y-ERAISKKLWCIGPvsLCNENSIEKYNRGNKASieqsnCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTR 317
Cdd:PLN03004 228 ItEELCFRNIYPIGP--LIVNGRIEDRNDNKAVS-----CLNWLDSQPEKSVVFLCFGSLGLFSKEQVIEIAVGLEKSGQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 318 PFIWVIKNRDE-NCSELE-KWLSEEEFERKTKGRGLIIRGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQ 395
Cdd:PLN03004 301 RFLWVVRNPPElEKTELDlKSLLPEGFLSRTEDKGMVVKSWAPQVPVLNHKAVGGFVTHCGWNSILEAVCAGVPMVAWPL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1731019548 396 FAEQFLNEKLVVEILKIGVRVgvegavrwgEEERVGVMAKKeEIEKAIEMVM 447
Cdd:PLN03004 381 YAEQRFNRVMIVDEIKIAISM---------NESETGFVSST-EVEKRVQEII 422
|
|
| RT_RNaseH |
pfam17917 |
RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) ... |
1685-1775 |
2.42e-41 |
|
RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) activities allow reverse transcriptases to convert the single-stranded retroviral RNA genome into double-stranded DNA, which is integrated into the host chromosome during infection. This entry represents the RNase H like domain.
Pssm-ID: 465565 Cd Length: 104 Bit Score: 148.04 E-value: 2.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1685 FVIYSDASKKGLGCVLMQQG-----KVVAYASRQLKIHEQNYPTHDLELAAVVFALKIWRHYLYGEKIQIYTDHKSLKYF 1759
Cdd:pfam17917 6 FILETDASDYGIGAVLSQKDedgkeRPIAYASRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRKFTVYTDHKPLKYL 85
|
90
....*....|....*.
gi 1731019548 1760 FTQKELNMRQRRWLEL 1775
Cdd:pfam17917 86 FTPKELNGRLARWALF 101
|
|
| PLN02555 |
PLN02555 |
limonoid glucosyltransferase |
13-487 |
5.76e-41 |
|
limonoid glucosyltransferase
Pssm-ID: 178170 [Multi-domain] Cd Length: 480 Bit Score: 159.58 E-value: 5.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 13 PHFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTpynatrlESFFARAKQSSLSISLLEIP-------FPCLQVGLPl 85
Cdd:PLN02555 8 VHVMLVSFPGQGHVNPLLRLGKLLASKGLLVTFVTT-------ESWGKKMRQANKIQDGVLKPvgdgfirFEFFEDGWA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 86 gcenlDTLPSRSLLRNFYKALSLL-QQPLEQFLSRH--HLNP-TCIISDKYLYWTAQTAHKFKCPRVVF--HGTGCFSLL 159
Cdd:PLN02555 80 -----EDDPRRQDLDLYLPQLELVgKREIPNLVKRYaeQGRPvSCLINNPFIPWVCDVAEELGIPSAVLwvQSCACFSAY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 160 S--SHNLQLYSPHTSIDSNSQPFLVPGLPHkieitkSQLPGSLIKSPDFDDFRDKIT---KAEQEAYGVVVNSFSELEng 234
Cdd:PLN02555 155 YhyYHGLVPFPTETEPEIDVQLPCMPLLKY------DEIPSFLHPSSPYPFLRRAILgqyKNLDKPFCILIDTFQELE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 235 yyQNYERAISKkLWCIGPVS--LCNENSIEKYNRGNkASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCL 312
Cdd:PLN02555 227 --KEIIDYMSK-LCPIKPVGplFKMAKTPNSDVKGD-ISKPADDCIEWLDSKPPSSVVYISFGTVVYLKQEQIDEIAYGV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 313 ESSTRPFIWVIKNRDENcSELEKWLSEEEFERKTKGRGLIIRgWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMIT 392
Cdd:PLN02555 303 LNSGVSFLWVMRPPHKD-SGVEPHVLPEEFLEKAGDKGKIVQ-WCPQEKVLAHPSVACFVTHCGWNSTMEALSSGVPVVC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 393 WPQFAEQFLNEKLVVEILKIGVRVGvegavRWGEEERVgvmAKKEEI----------EKAIEMVMDGGEegeerrrrvgd 462
Cdd:PLN02555 381 FPQWGDQVTDAVYLVDVFKTGVRLC-----RGEAENKL---ITREEVaeclleatvgEKAAELKQNALK----------- 441
|
490 500
....*....|....*....|....*
gi 1731019548 463 LSKMAPKAMENGGSSYVNLSLFIED 487
Cdd:PLN02555 442 WKEEAEAAVAEGGSSDRNFQEFVDK 466
|
|
| PLN02992 |
PLN02992 |
coniferyl-alcohol glucosyltransferase |
12-448 |
5.49e-40 |
|
coniferyl-alcohol glucosyltransferase
Pssm-ID: 178572 [Multi-domain] Cd Length: 481 Bit Score: 156.68 E-value: 5.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 12 QPHFVLVPLMAQGHMIPMIDIAT-LLARRGVFVTFVTTPYNATRLESFFArakqSSLSISLLEIPFPCL--------QVG 82
Cdd:PLN02992 5 KPHAAMFSSPGMGHVIPVIELGKrLSANHGFHVTVFVLETDAASAQSKFL----NSTGVDIVGLPSPDIsglvdpsaHVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 83 LPLGCENLDTLPSrslLRNFYKALsllqqpleqflsrhHLNPTCIISDKYLYWTAQTAHKFKCPRVVFHGTGCFSLlssh 162
Cdd:PLN02992 81 TKIGVIMREAVPT---LRSKIAEM--------------HQKPTALIVDLFGTDALCLGGEFNMLTYIFIASNARFL---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 163 NLQLYSPHTSIDSNS------QPFLVPGL-PHKIEITksqLPGSLIksPDFDDFRDKITK--AEQEAYGVVVNSFSELEN 233
Cdd:PLN02992 140 GVSIYYPTLDKDIKEehtvqrKPLAMPGCePVRFEDT---LDAYLV--PDEPVYRDFVRHglAYPKADGILVNTWEEMEP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 234 GYYQNYE------RAISKKLWCIGPvsLCnensiekynRGNKASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQ 307
Cdd:PLN02992 215 KSLKSLQdpkllgRVARVPVYPIGP--LC---------RPIQSSKTDHPVLDWLNKQPNESVLYISFGSGGSLSAKQLTE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 308 LGQCLESSTRPFIWVIKN--RDENCSElekWLSE--------------EEFERKTKGRGLIIRGWAPQLLILSHWSTGGF 371
Cdd:PLN02992 284 LAWGLEMSQQRFVWVVRPpvDGSACSA---YFSAnggetrdntpeylpEGFVSRTHDRGFVVPSWAPQAEILAHQAVGGF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 372 LTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKLVVEILKIGVRV-GVEGAV-RWGEEERV-GVMAKKE--EIEKAIEMV 446
Cdd:PLN02992 361 LTHCGWSSTLESVVGGVPMIAWPLFAEQNMNAALLSDELGIAVRSdDPKEVIsRSKIEALVrKVMVEEEgeEMRRKVKKL 440
|
..
gi 1731019548 447 MD 448
Cdd:PLN02992 441 RD 442
|
|
| PLN02152 |
PLN02152 |
indole-3-acetate beta-glucosyltransferase |
12-487 |
8.38e-40 |
|
indole-3-acetate beta-glucosyltransferase
Pssm-ID: 177813 [Multi-domain] Cd Length: 455 Bit Score: 155.21 E-value: 8.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 12 QPHFVLVPLMAQGHMIPMIDIAT-LLARRGVFVTFVTTPynatrleSFFARAKQSSLSiSLLEIPFPCLQVGLPLG-CEN 89
Cdd:PLN02152 3 PPHFLLVTFPAQGHVNPSLRFARrLIKTTGTRVTFATCL-------SVIHRSMIPNHN-NVENLSFLTFSDGFDDGvISN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 90 LDTLPSRS--LLRNFYKALSllqqpleQFL--SRHHLNP-TCIISDKYLYWTAQTAHKFKCPRVVFHGTGCFSLlsshnl 164
Cdd:PLN02152 75 TDDVQNRLvnFERNGDKALS-------DFIeaNLNGDSPvTCLIYTILPNWAPKVARRFHLPSVLLWIQPAFVF------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 165 QLYSPHTSidSNSQPFLVPGLPH-KIEITKSQLPGSLIKSPDFDDFRDKITKAEQEAY-GVVVNSFSELENGYYQNYERA 242
Cdd:PLN02152 142 DIYYNYST--GNNSVFEFPNLPSlEIRDLPSFLSPSNTNKAAQAVYQELMEFLKEESNpKILVNTFDSLEPEFLTAIPNI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 243 iskKLWCIGPVsLCNENSIEKYNRGNKASIEQSNCLN-WLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTRPFIW 321
Cdd:PLN02152 220 ---EMVAVGPL-LPAEIFTGSESGKDLSVRDQSSSYTlWLDSKTESSVIYVSFGTMVELSKKQIEELARALIEGKRPFLW 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 322 VIKNRDENCSELEkwlSEEE--------FERKTKGRGLIIrGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITW 393
Cdd:PLN02152 296 VITDKLNREAKIE---GEEEteiekiagFRHELEEVGMIV-SWCSQIEVLRHRAVGCFVTHCGWSSSLESLVLGVPVVAF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 394 PQFAEQFLNEKLVVEILKIGVRVgvegavrwgEEERVGvMAKKEEIEKAIEMVMDGGEEGEERRRRVgdLSKMAPKAMEN 473
Cdd:PLN02152 372 PMWSDQPANAKLLEEIWKTGVRV---------RENSEG-LVERGEIRRCLEAVMEEKSVELRESAEK--WKRLAIEAGGE 439
|
490
....*....|....
gi 1731019548 474 GGSSYVNLSLFIED 487
Cdd:PLN02152 440 GGSSDKNVEAFVKT 453
|
|
| PLN02207 |
PLN02207 |
UDP-glycosyltransferase |
15-487 |
3.76e-39 |
|
UDP-glycosyltransferase
Pssm-ID: 177857 [Multi-domain] Cd Length: 468 Bit Score: 153.65 E-value: 3.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 15 FVLVPLMAQGHMIPMIDIATLLARRG--VFVTFVTTPYNA-TRLESFFARAKQSSLSISLLEIPFpcLQVGLPLGcenlD 91
Cdd:PLN02207 6 LIFIPTPTVGHLVPFLEFARRLIEQDdrIRITILLMKLQGqSHLDTYVKSIASSQPFVRFIDVPE--LEEKPTLG----G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 92 TLPSRSLLRNFY-KALSLLQQPLEQFLSRHHLNPTCI---ISDKYLYWTAQTAHKFKCPRVVFHGTGC-FSLLSSHNLQL 166
Cdd:PLN02207 80 TQSVEAYVYDVIeKNIPLVRNIVMDILSSLALDGVKVkgfVADFFCLPMIDVAKDVSLPFYVFLTTNSgFLAMMQYLADR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 167 YSPHTSI-DSNSQPFL-VPGLPHKIeiTKSQLPGSLIKSPDFDDFRdKITKAEQEAYGVVVNSFSELE----NGYY--QN 238
Cdd:PLN02207 160 HSKDTSVfVRNSEEMLsIPGFVNPV--PANVLPSALFVEDGYDAYV-KLAILFTKANGILVNSSFDIEpysvNHFLdeQN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 239 YeraisKKLWCIGPVslcnensiekYNRGNKASIEQS-----NCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLE 313
Cdd:PLN02207 237 Y-----PSVYAVGPI----------FDLKAQPHPEQDlarrdELMKWLDDQPEASVVFLCFGSMGRLRGPLVKEIAHGLE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 314 SSTRPFIWVIKNRDENCSELekwlSEEEFERKTKGRGLIIrGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITW 393
Cdd:PLN02207 302 LCQYRFLWSLRTEEVTNDDL----LPEGFLDRVSGRGMIC-GWSPQVEILAHKAVGGFVSHCGWNSIVESLWFGVPIVTW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 394 PQFAEQFLNEKLVVEILKIGVRVGVEGAVRWGEeervgvMAKKEEIEKAIEMVMDggEEGEERRRRVGDLSKMAPKAMEN 473
Cdd:PLN02207 377 PMYAEQQLNAFLMVKELKLAVELKLDYRVHSDE------IVNANEIETAIRCVMN--KDNNVVRKRVMDISQMIQRATKN 448
|
490
....*....|....
gi 1731019548 474 GGSSYVNLSLFIED 487
Cdd:PLN02207 449 GGSSFAAIEKFIHD 462
|
|
| RT_RNaseH_2 |
pfam17919 |
RNase H-like domain found in reverse transcriptase; |
1655-1749 |
3.93e-38 |
|
RNase H-like domain found in reverse transcriptase;
Pssm-ID: 465567 [Multi-domain] Cd Length: 100 Bit Score: 138.40 E-value: 3.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1655 WSPACERSFQELKQKLVTAPVLTVPDGSGNFVIYSDASKKGLGCVLMQQG-----KVVAYASRQLKIHEQNYPTHDLELA 1729
Cdd:pfam17919 1 WTEECQKAFEKLKQALTSAPVLAHPDPDKPFILETDASDYGIGAVLSQEDddggeRPIAYASRKLSPAERNYSTTEKELL 80
|
90 100
....*....|....*....|
gi 1731019548 1730 AVVFALKIWRHYLYGEKIQI 1749
Cdd:pfam17919 81 AIVFALKKFRHYLLGRKFTV 100
|
|
| RVT_1 |
pfam00078 |
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ... |
1432-1592 |
6.27e-38 |
|
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. Reverse transcriptases occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses.
Pssm-ID: 395031 [Multi-domain] Cd Length: 189 Bit Score: 141.67 E-value: 6.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1432 VKKKD-GSMRLC----IDYRELNKVTVK-------NRYPLPRIDDLFDQLQGATVFSKIDLRSGYHQLRIRDGDIPKTAF 1499
Cdd:pfam00078 1 IPKKGkGKYRPIsllsIDYKALNKIIVKrlkpenlDSPPQPGFRPGLAKLKKAKWFLKLDLKKAFDQVPLDELDRKLTAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1500 R-----------SRYGHYEFVVMSFGLTNAPAVFMDLMNRVFKEFL---DSFVIVFIDDILIYSKTEAEHEEHLHQVLET 1565
Cdd:pfam00078 81 TtppininwngeLSGGRYEWKGLPQGLVLSPALFQLFMNELLRPLRkraGLTLVRYADDILIFSKSEEEHQEALEEVLEW 160
|
170 180
....*....|....*....|....*....
gi 1731019548 1566 LRANKLYAKFSKCEFWL--RKVTFLGHVV 1592
Cdd:pfam00078 161 LKESGLKINPEKTQFFLksKEVKYLGVTL 189
|
|
| PLN02554 |
PLN02554 |
UDP-glycosyltransferase family protein |
177-487 |
7.60e-38 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215304 Cd Length: 481 Bit Score: 150.32 E-value: 7.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 177 SQPFLVPGLPHkIEITKSQLPGSLIKSPDFddfrdkitkaeQEAYGVVVNSFSELE-------NGYYQNYERAiskklWC 249
Cdd:PLN02554 180 TRPYPVKCLPS-VLLSKEWLPLFLAQARRF-----------REMKGILVNTVAELEpqalkffSGSSGDLPPV-----YP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 250 IGPVsLCNENSIEKYnrgnkASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTRPFIW-------- 321
Cdd:PLN02554 243 VGPV-LHLENSGDDS-----KDEKQSEILRWLDEQPPKSVVFLCFGSMGGFSEEQAREIAIALERSGHRFLWslrraspn 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 322 VIKNRDENCSELEKWLSEEEFERkTKGRGLIIrGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFL 401
Cdd:PLN02554 317 IMKEPPGEFTNLEEILPEGFLDR-TKDIGKVI-GWAPQVAVLAKPAIGGFVTHCGWNSILESLWFGVPMAAWPLYAEQKF 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 402 NEKLVVEILKIGVRVGVE--GAVRWGEEERVGVmakkEEIEKAIEMVMDggeEGEERRRRVGDLSKMAPKAMENGGSSYV 479
Cdd:PLN02554 395 NAFEMVEELGLAVEIRKYwrGDLLAGEMETVTA----EEIERGIRCLME---QDSDVRKRVKEMSEKCHVALMDGGSSHT 467
|
....*...
gi 1731019548 480 NLSLFIED 487
Cdd:PLN02554 468 ALKKFIQD 475
|
|
| PLN03015 |
PLN03015 |
UDP-glucosyl transferase |
12-481 |
3.13e-35 |
|
UDP-glucosyl transferase
Pssm-ID: 178589 [Multi-domain] Cd Length: 470 Bit Score: 142.14 E-value: 3.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 12 QPHFVLVPLMAQGHMIPMIDIATLLAR-RGVFVTFVT-TPYNATRLESFFARAKQSSLSISLLEIPfpclqvglPLGCEN 89
Cdd:PLN03015 3 QPHALLVASPGLGHLIPILELGNRLSSvLNIHVTILAvTSGSSSPTETEAIHAAAARTTCQITEIP--------SVDVDN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 90 LdTLPSRSLLRNFYKALSLLQQPLEQFLSRHHLNPTCIISDkylywtaqtahkfkcprvvFHGTGCFSL----------- 158
Cdd:PLN03015 75 L-VEPDATIFTKMVVKMRAMKPAVRDAVKSMKRKPTVMIVD-------------------FFGTALMSIaddvgvtakyv 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 159 -LSSHN----LQLYSP--HTSIDSN----SQPFLVPGLPhkiEITKSQLPGSLIKSPDfDDFRDKITKAEQ--EAYGVVV 225
Cdd:PLN03015 135 yIPSHAwflaVMVYLPvlDTVVEGEyvdiKEPLKIPGCK---PVGPKELMETMLDRSD-QQYKECVRSGLEvpMSDGVLV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 226 NSFSELENGYY------QNYERAISKKLWCIGPVSLCNENsIEKYNrgnkaSIeqsncLNWLDSMIPKSVLYICLGSLCR 299
Cdd:PLN03015 211 NTWEELQGNTLaalredMELNRVMKVPVYPIGPIVRTNVH-VEKRN-----SI-----FEWLDKQGERSVVYVCLGSGGT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 300 MLPSQLIQLGQCLESSTRPFIWVI-----------KNRDENCSELEkwlseEEFERKTKGRGLIIRGWAPQLLILSHWST 368
Cdd:PLN03015 280 LTFEQTVELAWGLELSGQRFVWVLrrpasylgassSDDDQVSASLP-----EGFLDRTRGVGLVVTQWAPQVEILSHRSI 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 369 GGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKLVVEilKIGVrvgvegAVRWGEEERVGVMAKKEEIEKAIEMVMD 448
Cdd:PLN03015 355 GGFLSHCGWSSVLESLTKGVPIVAWPLYAEQWMNATLLTE--EIGV------AVRTSELPSEKVIGREEVASLVRKIVAE 426
|
490 500 510
....*....|....*....|....*....|...
gi 1731019548 449 GGEEGEERRRRVGDLSKMAPKAMENGGSSYVNL 481
Cdd:PLN03015 427 EDEEGQKIRAKAEEVRVSSERAWSHGGSSYNSL 459
|
|
| RVP_2 |
pfam08284 |
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ... |
1173-1304 |
3.97e-32 |
|
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases.
Pssm-ID: 400537 Cd Length: 134 Bit Score: 122.92 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1173 QGRVFATTRQEAERAGTVVTGTLPILGHYAFVLFDSGSSHSFISSVFVQHVGLEVEPLGSVLSVSTPSGEVLLSKEQIKA 1252
Cdd:pfam08284 2 QGRVNHLSAEEAEASPDVIQGTFLVNSIPATVLFDSGATHSFISHAFVGKLKLPVESLSNPLCIETPTGGSVTTNLICPS 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1731019548 1253 CRVEIANRMLDVTLLVLDMQDFDVILGMDWLSANHANIDCYGKEVVFNPPSE 1304
Cdd:pfam08284 82 CPIEIQGISFLADLILLDMKDLDVILGMDWLSKNKANIDCARRTVTLTKERE 133
|
|
| PLN00414 |
PLN00414 |
glycosyltransferase family protein |
14-448 |
9.31e-32 |
|
glycosyltransferase family protein
Pssm-ID: 177807 [Multi-domain] Cd Length: 446 Bit Score: 131.30 E-value: 9.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 14 HFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNATRLE--SFFARakqsslSISLLEIPFPCLQvGLPLGCENLD 91
Cdd:PLN00414 6 HAFMYPWFGFGHMIPYLHLANKLAEKGHRVTFFLPKKAHKQLQplNLFPD------SIVFEPLTLPPVD-GLPFGAETAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 92 TLPSrSLLRNFYKALSLLQQPLEQFLsrHHLNPTCIISDkYLYWTAQTAHKFKCPRVVFH--GTGCFSLLSSHNLQLYSP 169
Cdd:PLN00414 79 DLPN-STKKPIFDAMDLLRDQIEAKV--RALKPDLIFFD-FVHWVPEMAKEFGIKSVNYQiiSAACVAMVLAPRAELGFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 170 htsidsnsqPflvPGLPhkieITKSQLPG------SLIKSPDfdDFRDKITKAEQEAYGVVVNSFSELENGYYQNYERAI 243
Cdd:PLN00414 155 ---------P---PDYP----LSKVALRGhdanvcSLFANSH--ELFGLITKGLKNCDVVSIRTCVELEGNLCDFIERQC 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 244 SKKLWCIGPVSLcnensiEKYNRGNKASIEQSNclNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTRPF-IWV 322
Cdd:PLN00414 217 QRKVLLTGPMLP------EPQNKSGKPLEDRWN--HWLNGFEPGSVVFCAFGTQFFFEKDQFQEFCLGMELTGLPFlIAV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 323 IKNRdeNCSELEKWLSEEeFERKTKGRGLIIRGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLN 402
Cdd:PLN00414 289 MPPK--GSSTVQEALPEG-FEERVKGRGIVWEGWVEQPLILSHPSVGCFVNHCGFGSMWESLVSDCQIVFIPQLADQVLI 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1731019548 403 EKLVVEILKIGVRVgvegavrwgEEERVGVMAkKEEIEKAIEMVMD 448
Cdd:PLN00414 366 TRLLTEELEVSVKV---------QREDSGWFS-KESLRDTVKSVMD 401
|
|
| PLN02562 |
PLN02562 |
UDP-glycosyltransferase |
8-487 |
4.77e-29 |
|
UDP-glycosyltransferase
Pssm-ID: 215305 Cd Length: 448 Bit Score: 123.07 E-value: 4.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 8 QLELQPHFVLVPLMAQGHMIPMIDIATLLARRGvFVTFVTTPYNATRLESFFARAKqssLSISLLEIPfpclqvglplgc 87
Cdd:PLN02562 2 KVTQRPKIILVPYPAQGHVTPMLKLASAFLSRG-FEPVVITPEFIHRRISATLDPK---LGITFMSIS------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 88 ENLDTLPSRSLLRNFYKALSLLQQPLEQFLSR--HHLNPTCIISDKYLYWTAQTAHKFKCPRVVFHGTgcfsLLSSHNLQ 165
Cdd:PLN02562 66 DGQDDDPPRDFFSIENSMENTMPPQLERLLHKldEDGEVACMVVDLLASWAIGVADRCGVPVAGFWPV----MLAAYRLI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 166 LYSPH---TSIDSNS----QPFLVPGLPHKIEITKSQLPGsLIKSPD-----FDDFRDKITKAEQEAYgVVVNSFSELE- 232
Cdd:PLN02562 142 QAIPElvrTGLISETgcprQLEKICVLPEQPLLSTEDLPW-LIGTPKarkarFKFWTRTLERTKSLRW-ILMNSFKDEEy 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 233 ---NGYYQNYERAISKKLWCIGPVSLCNENSIEKYNRGNkasiEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQ-L 308
Cdd:PLN02562 220 ddvKNHQASYNNGQNPQILQIGPLHNQEATTITKPSFWE----EDMSCLGWLQEQKPNSVIYISFGSWVSPIGESNVRtL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 309 GQCLESSTRPFIWVIKnrdencSELEKWLSEEEFERKTKgRGLIIrGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGV 388
Cdd:PLN02562 296 ALALEASGRPFIWVLN------PVWREGLPPGYVERVSK-QGKVV-SWAPQLEVLKHQAVGCYLTHCGWNSTMEAIQCQK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 389 PMITWPQFAEQFLNEKLVVEILKIGVRVGVEGavrwgeeervgvmakKEEIEKAIEMVMDGGEEGEErrrrvgdLSKMAP 468
Cdd:PLN02562 368 RLLCYPVAGDQFVNCAYIVDVWKIGVRISGFG---------------QKEVEEGLRKVMEDSGMGER-------LMKLRE 425
|
490 500
....*....|....*....|.
gi 1731019548 469 KAM--ENGGSSYVNLSLFIED 487
Cdd:PLN02562 426 RAMgeEARLRSMMNFTTLKDE 446
|
|
| PLN02764 |
PLN02764 |
glycosyltransferase family protein |
11-439 |
3.59e-24 |
|
glycosyltransferase family protein
Pssm-ID: 178364 Cd Length: 453 Bit Score: 108.61 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 11 LQPHFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNATRLE--SFFARakqsslSISLLEIPFPCLQvGLPLGCE 88
Cdd:PLN02764 4 LKFHVLMYPWFATGHMTPFLFLANKLAEKGHTVTFLLPKKALKQLEhlNLFPH------NIVFRSVTVPHVD-GLPVGTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 89 NLDTLP--SRSLLRNfykALSLLQQPLEQFLsrHHLNPTCIISDkYLYWTAQTAHKF---KCPRVVFHGTGCFSLLSSHN 163
Cdd:PLN02764 77 TVSEIPvtSADLLMS---AMDLTRDQVEVVV--RAVEPDLIFFD-FAHWIPEVARDFglkTVKYVVVSASTIASMLVPGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 164 LQLYSPhtsidsnsqpflvPGLPHKIEITKSQLPGSL--IKSPDFDD----FRDKITKAEQEAYGVVVNSFSELENGYYQ 237
Cdd:PLN02764 151 ELGVPP-------------PGYPSSKVLLRKQDAYTMknLEPTNTIDvgpnLLERVTTSLMNSDVIAIRTAREIEGNFCD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 238 NYERAISKKLWCIGPVslcnensiekYNRGNKASIEQSNCLNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTR 317
Cdd:PLN02764 218 YIEKHCRKKVLLTGPV----------FPEPDKTRELEERWVKWLSGYEPDSVVFCALGSQVILEKDQFQELCLGMELTGS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 318 PFIWVIKNrDENCSELEKWLSEEeFERKTKGRGLIIRGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFA 397
Cdd:PLN02764 288 PFLVAVKP-PRGSSTIQEALPEG-FEERVKGRGVVWGGWVQQPLILSHPSVGCFVSHCGFGSMWESLLSDCQIVLVPQLG 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1731019548 398 EQFLNEKLVVEILKIGVRVGVEgAVRWGEEERV-----GVMAKKEEI 439
Cdd:PLN02764 366 DQVLNTRLLSDELKVSVEVARE-ETGWFSKESLrdainSVMKRDSEI 411
|
|
| RT_ZFREV_like |
cd03715 |
RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the ... |
1389-1591 |
6.36e-23 |
|
RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the intact endogenous retrovirus ZFERV from zebrafish and to Moloney murine leukemia virus RT. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. These elements can be divided into two major groups. One group contains retroviruses and DNA viruses whose propagation involves an RNA intermediate. They are grouped together with transposable elements containing long terminal repeats (LTRs). The other group, also called poly(A)-type retrotransposons, contain fungal mitochondrial introns and transposable elements that lack LTRs. Phylogenetic analysis suggests that ZFERV belongs to a distinct group of retroviruses.
Pssm-ID: 239685 [Multi-domain] Cd Length: 210 Bit Score: 98.96 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1389 PISRAPYRMAPAELKELKVQLQELLDKGFIRPSVSPWGAPVLFVKKKDG-SMRLCIDYRELNKVTVKNRYPLPRIDDLFD 1467
Cdd:cd03715 1 PVNQKQYPLPREAREGITPHIQELLEAGILVPCQSPWNTPILPVKKPGGnDYRMVQDLRLVNQAVLPIHPAVPNPYTLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1468 QLQGA-TVFSKIDLRSGYHQLRIRDGDIPKTAFRSRYGHYEFVVMSFGLTNAPAVFMDLMNRVFKEF----LDSFVIVFI 1542
Cdd:cd03715 81 LLPPKhQWYTVLDLANAFFSLPLAPDSQPLFAFEWEGQQYTFTRLPQGFKNSPTLFHEALARDLAPFplehEGTILLQYV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1731019548 1543 DDILIYSKTEAEHEEHLHQVLETLRANKLYAKFSKCEFWLRKVTFLGHV 1591
Cdd:cd03715 161 DDLLLAADSEEDCLKGTDALLTHLGELGYKVSPKKAQICRAEVKFLGVV 209
|
|
| PLN02208 |
PLN02208 |
glycosyltransferase family protein |
9-448 |
3.97e-22 |
|
glycosyltransferase family protein
Pssm-ID: 177858 Cd Length: 442 Bit Score: 102.02 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 9 LELQPHFVLVPLMAQGHMIPMIDIATLLARRGVFVTFVTTPYNATRLE--SFFArakqSSLSISLLEIPfPClqVGLPLG 86
Cdd:PLN02208 1 MEPKFHAFMFPWFAFGHMIPFLHLANKLAEKGHRVTFLLPKKAQKQLEhhNLFP----DSIVFHPLTIP-PV--NGLPAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 87 CENLDTLPSrSLLRNFYKALSLLQQPLEQflSRHHLNPTCIISDkYLYWTAQTAHKFKCPRVvfhgtgCFSLLSSHNLQl 166
Cdd:PLN02208 74 AETTSDIPI-SMDNLLSEALDLTRDQVEA--AVRALRPDLIFFD-FAQWIPEMAKEHMIKSV------SYIIVSATTIA- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 167 yspHTSIDSNSQPFLVPGLPH-KIEITKSQLPGSLIKSPDFDDFRDKITKAEQEAYGVVVNSFSELENGYYQNYERAISK 245
Cdd:PLN02208 143 ---HTHVPGGKLGVPPPGYPSsKVLFRENDAHALATLSIFYKRLYHQITTGLKSCDVIALRTCKEIEGKFCDYISRQYHK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 246 KLWCIGPVSLCNENSiekynrgnKASIEQSNclNWLDSMIPKSVLYICLGSLCRMLPSQLIQLGQCLESSTRPFIWVIKN 325
Cdd:PLN02208 220 KVLLTGPMFPEPDTS--------KPLEEQWS--HFLSGFPPKSVVFCSLGSQIILEKDQFQELCLGMELTGLPFLIAVKP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 326 rDENCSELEKWLSEEeFERKTKGRGLIIRGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKL 405
Cdd:PLN02208 290 -PRGSSTVQEGLPEG-FEERVKGRGVVWGGWVQQPLILDHPSIGCFVNHCGPGTIWESLVSDCQMVLIPFLSDQVLFTRL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1731019548 406 VVEILKIGVRVgvegavrwgEEERVGVMAkKEEIEKAIEMVMD 448
Cdd:PLN02208 368 MTEEFEVSVEV---------SREKTGWFS-KESLSNAIKSVMD 400
|
|
| Retrotrans_gag |
pfam03732 |
Retrotransposon gag protein; Gag or Capsid-like proteins from LTR retrotransposons. There is a ... |
943-1038 |
4.67e-20 |
|
Retrotransposon gag protein; Gag or Capsid-like proteins from LTR retrotransposons. There is a central motif QGXXEXXXXXFXXLXXH that is common to Retroviridae gag-proteins, but is poorly conserved.
Pssm-ID: 367628 Cd Length: 97 Bit Score: 87.00 E-value: 4.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 943 AVFFLEDRGTAWWETAERmlGGDVSKITWEQFKENFYAKFFSANVKHAKLQEFLNLEQGDMTVEQYDAEFDMLSRFAPDM 1022
Cdd:pfam03732 3 AVHSLRGAALTWWKSLVA--RSIDAFDSWDELKDAFLKRFFPSIRKDLLRNELRSLRQGTESVREYVERFKRLARQLPHH 80
|
90
....*....|....*.
gi 1731019548 1023 VRDEAARTEKFVRGLR 1038
Cdd:pfam03732 81 GRDEEALISAFLRGLR 96
|
|
| RT_Rtv |
cd01645 |
RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of ... |
1402-1566 |
2.28e-19 |
|
RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of single-stranded RNA into double-stranded viral DNA for integration into host chromosomes. Proteins in this subfamily contain long terminal repeats (LTRs) and are multifunctional enzymes with RNA-directed DNA polymerase, DNA directed DNA polymerase, and ribonuclease hybrid (RNase H) activities. The viral RNA genome enters the cytoplasm as part of a nucleoprotein complex, and the process of reverse transcription generates in the cytoplasm forming a linear DNA duplex via an intricate series of steps. This duplex DNA is colinear with its RNA template, but contains terminal duplications known as LTRs that are not present in viral RNA. It has been proposed that two specialized template switches, known as strand-transfer reactions or "jumps", are required to generate the LTRs.
Pssm-ID: 238823 [Multi-domain] Cd Length: 213 Bit Score: 88.88 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1402 LKELKVQLQELLDKGFIRPSVSPWGAPVLFVKKKDGSMRLCIDYRELNKVTVKnryplpriddlFDQLQ-GATVFSKI-- 1478
Cdd:cd01645 14 LEALTELVTEQLKEGHIEPSTSPWNTPVFVIKKKSGKWRLLHDLRAVNAQTQD-----------MGALQpGLPHPAALpk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1479 -------DLRSGYHQLRIRDGDIPKTAF-------RSRYGHYEFVVMSFGLTNAPAVFMDLMNRVFKEF----LDSFVIV 1540
Cdd:cd01645 83 gwplivlDLKDCFFSIPLHPDDRERFAFtvpsinnKGPAKRYQWKVLPQGMKNSPTICQSFVAQALEPFrkqyPDIVIYH 162
|
170 180
....*....|....*....|....*.
gi 1731019548 1541 FIDDILIYSKTEAEHEEHLHQVLETL 1566
Cdd:cd01645 163 YMDDILIASDLEGQLREIYEELRQTL 188
|
|
| Integrase_H2C2 |
pfam17921 |
Integrase zinc binding domain; This zinc binding domain is found in a wide variety of ... |
1891-1949 |
5.79e-16 |
|
Integrase zinc binding domain; This zinc binding domain is found in a wide variety of integrase proteins.
Pssm-ID: 465569 [Multi-domain] Cd Length: 58 Bit Score: 73.82 E-value: 5.79e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1731019548 1891 DSAVKTELLTEAHSSpfTMHPGSTKMYQDLRSVYWWRGMKRDVADFVSRCLVCQQVKAP 1949
Cdd:pfam17921 2 PKSLRKEILKEAHDS--GGHLGIEKTLARLRRRYWWPGMRKDVKKYVKSCETCQRRKPS 58
|
|
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
289-448 |
7.84e-12 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 70.13 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 289 VLYICLGSLCRMLPSQ-LIQLGQCLESSTRPFIWviknrdencselekwlSEEEFERKTKGRGLIIRGWAPQLLILSHWS 367
Cdd:pfam00201 277 VVVFSLGSMVSNIPEEkANAIASALAQIPQKVLW----------------RFDGTKPSTLGNNTRLVKWLPQNDLLGHPK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 368 TGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKLVVEilkigvrVGVEGAVRWGEeervgvMAkKEEIEKAIEMVM 447
Cdd:pfam00201 341 TRAFITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEA-------KGAAVTLNVLT------MT-SEDLLNALKEVI 406
|
.
gi 1731019548 448 D 448
Cdd:pfam00201 407 N 407
|
|
| RNase_HI_RT_DIRS1 |
cd09275 |
DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ... |
1686-1800 |
9.83e-11 |
|
DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. The structural features of DIRS1-group elements are different from typical LTR elements. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.
Pssm-ID: 260007 Cd Length: 120 Bit Score: 61.15 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1686 VIYSDASKKGLGCVLMQQGKVVAYASrqlkiHEQNYPTHDLELAAVVFALKIWRHYLYGEKIQIYTDHKS----LKYFFT 1761
Cdd:cd09275 1 VLFTDASLSGWGAYLLNSRAHGPWSA-----DERNKHINLLELKAVLLALQHFAAELKNRKILIRTDNTTavayINKQGG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1731019548 1762 QK--ELNMRQRRWLELVKDYDCEI--LYHPGKANVVADALSRK 1800
Cdd:cd09275 76 TSspPLLALARQILLWCEQRNIWLraSHIPGVLNTEADRLSRL 118
|
|
| Ty3_capsid |
pfam19259 |
Ty3 transposon capsid-like protein; This entry corresponds to the capsid protein found in the ... |
905-1062 |
6.99e-10 |
|
Ty3 transposon capsid-like protein; This entry corresponds to the capsid protein found in the Ty3 transposons of yeast as well as other transposable elements.
Pssm-ID: 437091 [Multi-domain] Cd Length: 197 Bit Score: 60.95 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 905 PKTFDGSMDnPTKAQMWLTSIETIFRYMKCPEDQK--VQCAVFFL---EDRGTAWWETAermlggDVSKITWEQFKENFY 979
Cdd:pfam19259 14 ILPFRGRKD-VLKLKSFISEIMLQMSMIFWPNDAEriVFCARHLTgpaAQWFHDFVQEQ------GILDATFDTFIKAFK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 980 AKFFSANVKHAKLQEFLNLEQGDMTVEQYDAEFDMLSRFAPDMVRDEAARTEKFVRGLRLDLQGIVRALRPATHADALRI 1059
Cdd:pfam19259 87 QHFYGKPDINKLFNDIVNLSEAKLGIERYNSHFNRLWDLLPPDFLSEKAAIMFYIRGLKPETYIIVRLAKPSTLKEAMEI 166
|
...
gi 1731019548 1060 ALD 1062
Cdd:pfam19259 167 AYE 169
|
|
| retropepsin_like |
cd00303 |
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ... |
1219-1283 |
9.35e-10 |
|
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.
Pssm-ID: 133136 Cd Length: 92 Bit Score: 57.35 E-value: 9.35e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731019548 1219 FVQHVGLEVEPLGSVLSVSTPSGEVLLSKEQIKACRVEIANRMLDVTLLVLDMQDFDVILGMDWL 1283
Cdd:cd00303 27 LAKKLGLPPRLLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDLLSYDVILGRPWL 91
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
352-409 |
6.59e-09 |
|
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) subfamily of the UDP-glucuronosyltransferase family. Members include a number of glucosyl transferases for macrolide antibiotic inactivation, but also include transferases of glucose-related sugars for macrolide antibiotic production. [Cellular processes, Toxin production and resistance]
Pssm-ID: 273616 [Multi-domain] Cd Length: 392 Bit Score: 60.47 E-value: 6.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1731019548 352 IIRGWAPQLLILSHwsTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKLVVEI 409
Cdd:TIGR01426 278 EVRQWVPQLEILKK--ADAFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAEL 333
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
351-416 |
8.15e-09 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 59.10 E-value: 8.15e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731019548 351 LIIRGWAPQLLILSHwsTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKLVVEiLKIGVRV 416
Cdd:COG1819 171 VRVVDYVPQDALLPR--ADAVVHHGGAGTTAEALRAGVPQVVVPFGGDQPLNAARVER-LGAGLAL 233
|
|
| RT_DIRS1 |
cd03714 |
RT_DIRS1: Reverse transcriptases (RTs) occurring in the DIRS1 group of retransposons. Members ... |
1478-1589 |
9.58e-09 |
|
RT_DIRS1: Reverse transcriptases (RTs) occurring in the DIRS1 group of retransposons. Members of the subfamily include the Dictyostelium DIRS-1, Volvox carteri kangaroo, and Panagrellus redivivus PAT elements. These elements differ from LTR and conventional non-LTR retrotransposons. They contain split direct repeat (SDR) termini, and have been proposed to integrate via double-stranded closed-circle DNA intermediates assisted by an encoded recombinase which is similar to gamma-site-specific integrase.
Pssm-ID: 239684 [Multi-domain] Cd Length: 119 Bit Score: 55.43 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1478 IDLRSGYHQLRIRDGDIPKTAFRSRYGHYEFVVMSFGLTNAPAVFMDLMNRVFKEF--LDSFVIVFIDDILIYSKTEAEH 1555
Cdd:cd03714 1 VDLKDAYFHIPILPRSRDLLGFAWQGETYQFKALPFGLSLAPRVFTKVVEALLAPLrlLGVRIFSYLDDLLIIASSIKTS 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1731019548 1556 EEHLHQVLETLRANK-LYAKFSKCEFWL-RKVTFLG 1589
Cdd:cd03714 81 EAVLRHLRATLLANLgFTLNLEKSKLGPtQRITFLG 116
|
|
| RT_like |
cd00304 |
RT_like: Reverse transcriptase (RT, RNA-dependent DNA polymerase)_like family. An RT gene is ... |
1509-1592 |
1.75e-08 |
|
RT_like: Reverse transcriptase (RT, RNA-dependent DNA polymerase)_like family. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. These elements can be divided into two major groups. One group contains retroviruses and DNA viruses whose propagation involves an RNA intermediate. They are grouped together with transposable elements containing long terminal repeats (LTRs). The other group, also called poly(A)-type retrotransposons, contain fungal mitochondrial introns and transposable elements that lack LTRs.
Pssm-ID: 238185 [Multi-domain] Cd Length: 98 Bit Score: 53.89 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1509 VVMSFGLTNAPAVFMDLMNRVFKEF----LDSFVIVFIDDILIYSKTEaEHEEHLHQVLETLRANKLYAKFSKCEF--WL 1582
Cdd:cd00304 10 IPLPQGSPLSPALANLYMEKLEAPIlkqlLDITLIRYVDDLVVIAKSE-QQAVKKRELEEFLARLGLNLSDEKTQFteKE 88
|
90
....*....|
gi 1731019548 1583 RKVTFLGHVV 1592
Cdd:cd00304 89 KKFKFLGILV 98
|
|
| RNase_H_like |
cd06222 |
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ... |
1687-1799 |
1.02e-07 |
|
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions.
Pssm-ID: 259998 [Multi-domain] Cd Length: 121 Bit Score: 52.70 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1687 IYSDASKK------GLGCVLMQQGKVVaYASRQLKIHEQNyPTHdLELAAVVFALKIWRHYLYgEKIQIYTDHKSL---- 1756
Cdd:cd06222 1 INVDGSCRgnpgpaGIGGVLRDHEGGW-LGGFALKIGAPT-ALE-AELLALLLALELALDLGY-LKVIIESDSKYVvdli 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1731019548 1757 --KYFFTQKELNMRQRRWLELVKDYDCEILYHPGKANVVADALSR 1799
Cdd:cd06222 77 nsGSFKWSPNILLIEDILLLLSRFWSVKISHVPREGNQVADALAK 121
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
497-672 |
4.35e-07 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 55.46 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 497 AQPSRNRNRAVAELPAAPGESSKPICAAE--RPSEQPSLARRsrveaasaRPQPTRQPAEsrrfdPTQAQPKRQSVAVAE 574
Cdd:PHA03378 674 YQPSPTGANTMLPIQWAPGTMQPPPRAPTpmRPPAAPPGRAQ--------RPAAATGRAR-----PPAAAPGRARPPAAA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 575 RSRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREIP--VPSRAASAQAEPV-LSSSSRAARTKLAP 651
Cdd:PHA03378 741 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPrgAPTPQPPPQAGPTsMQLMPRAAPGQQGP 820
|
170 180
....*....|....*....|.
gi 1731019548 652 STYILRGISSVGARALQPPSR 672
Cdd:PHA03378 821 TKQILRQLLTGGVKRGRPSLK 841
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
495-646 |
5.89e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 54.86 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 495 SAAQPSRNRNRAVAELPAAPGESSKPICAAERPSEQPSLARRS--------RVEAASARPQPTRQPAESRRFDPTQAQPK 566
Cdd:PRK07003 387 AAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAApappatadRGDDAADGDAPVPAKANARASADSRCDER 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 567 RQSVAVAERSRGSRTTNSRRAARNpEAEASRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPVLSSSSRAAR 646
Cdd:PRK07003 467 DAQPPADSGSASAPASDAPPDAAF-EPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAAR 545
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
496-645 |
1.33e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 53.70 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 496 AAQPSRNRNRAVAELPAAPGESSKPicAAERPSEQPSLARRSRVEAASARPQPTRQPAEsrrfdPTQAQPKRQSVAVAE- 574
Cdd:PRK07003 480 PASDAPPDAAFEPAPRAAAPSAATP--AAVPDARAPAAASREDAPAAAAPPAPEARPPT-----PAAAAPAARAGGAAAa 552
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731019548 575 ----RSRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPvlSSSSRAA 645
Cdd:PRK07003 553 ldvlRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPNGAARAEQ--AAESRGA 625
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
496-623 |
1.69e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 53.45 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 496 AAQPSRNRNRAVAELPAAPGEsskpicAAERPSEQPslARRSRVEAASARPQPTRQPAESRRFDPTQAQPKRQSVAVAER 575
Cdd:PRK07764 393 APAAAAPSAAAAAPAAAPAPA------AAAPAAAAA--PAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSA 464
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1731019548 576 SRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREI 623
Cdd:PRK07764 465 QPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATL 512
|
|
| recX |
PRK14136 |
recombination regulator RecX; Provisional |
501-763 |
1.96e-06 |
|
recombination regulator RecX; Provisional
Pssm-ID: 237620 [Multi-domain] Cd Length: 309 Bit Score: 52.31 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 501 RNRNRAVAELPAAPGESSKpicAAERPSEQPSLARRSRVEAASARPQpTRQPAES----RRFDPTQAQPKRQSVAVAERS 576
Cdd:PRK14136 3 RRRQGADPQEADHPARAAR---AGRPHASRETDRTVSGEGRPAGRTA-TRASDDAlvsfEIAAPDEPFDDDESFDAHDRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 577 RGSRttnSRRAARNPEAEASRAKPSRVSPVASRAASPPVA----SRAAREIPVPSRAASaqaePVLSSSSRAARTKLAPS 652
Cdd:PRK14136 79 RRRV---SGVGVRDAGAPGGRAADARAANLSSAAKRAEAAgdvyTRTSQHPRRTRRAAG----PFHSDSSPSASSEDDGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 653 TyiLRGISSVGARALQPPSRDFVAWKAYCLAVRTRQvdLQIYFGYDECRDG-----ECRNDLCDMLYADAMCMYTAIRVP 727
Cdd:PRK14136 152 A--RSRASSRPARSLKGRALGYLSRREYSRAELARK--LAPYADESDSVEPlldalEREGWLSDARFAESLVHRRASRVG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1731019548 728 VSLILLESYLHGcpsgsppIEDCVVE---------DEARARASWR 763
Cdd:PRK14136 228 SARIVSELKRHA-------VGDALVEsvgaqlretEFERAQAVWR 265
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
496-670 |
2.05e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 53.34 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 496 AAQPSR-NRNRAVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAESrrfdPTQAQPKRQSVAVAE 574
Cdd:PRK12323 362 AFRPGQsGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAA----PARRSPAPEALAAAR 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 575 ----RSRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPVLSSSSRAARTKLA 650
Cdd:PRK12323 438 qasaRGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAA 517
|
170 180
....*....|....*....|
gi 1731019548 651 PSTYILRGISSVGARALQPP 670
Cdd:PRK12323 518 PAGWVAESIPDPATADPDDA 537
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
486-672 |
2.29e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 53.25 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 486 EDPPSILLCSAAQPSRNRNRAVAELPAAPGESSKPICAAERPSEQPSLARRSRV-----EAASARPQPTRQPAESRRFDP 560
Cdd:PHA03307 141 VGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPpstppAAASPRPPRRSSPISASASSP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 561 TQAQPKRQSVAVAERSRGSRTTNSRRAARNPEAEASRAKPSRVS----------PVASRAASPPVASRAAREIPVPSRAA 630
Cdd:PHA03307 221 APAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITlptriweasgWNGPSSRPGPASSSSSPRERSPSPSP 300
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1731019548 631 SAQAEPVLSSSSRAARTKLAPSTYILRGISSVGARALQPPSR 672
Cdd:PHA03307 301 SSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVS 342
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
486-671 |
3.82e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 52.48 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 486 EDPPSILLCSAAQPSRNRNRAvAELPAAPGESSK---PICAA----ERPSEQPSLARRSRVEAASARPQPTRQPAESRRf 558
Cdd:PHA03307 209 RSSPISASASSPAPAPGRSAA-DDAGASSSDSSSsesSGCGWgpenECPLPRPAPITLPTRIWEASGWNGPSSRPGPAS- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 559 dPTQAQPKRQSVAVAERSRGSRTTNSRRAARN--PEAEASRAKPSRVSPVASRAASPPVASRAA---------------- 620
Cdd:PHA03307 287 -SSSSPRERSPSPSPSSPGSGPAPSSPRASSSssSSRESSSSSTSSSSESSRGAAVSPGPSPSRspspsrppppadpssp 365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1731019548 621 REIPVPSRAASAQAEPVLSSSSRAARtKLAPSTYILRGISSVGARALQPPS 671
Cdd:PHA03307 366 RKRPRPSRAPSSPAASAGRPTRRRAR-AAVAGRARRRDATGRFPAGRPRPS 415
|
|
| egt |
PHA03392 |
ecdysteroid UDP-glucosyltransferase; Provisional |
336-416 |
4.21e-06 |
|
ecdysteroid UDP-glucosyltransferase; Provisional
Pssm-ID: 223071 [Multi-domain] Cd Length: 507 Bit Score: 51.88 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 336 WLSEEEFERKTKGRGLIIRGWAPQLLILSHWSTGGFLTHCGWNSTVEGIGNGVPMITWPQFAEQFLNEKLVVEiLKIGVR 415
Cdd:PHA03392 333 WKYDGEVEAINLPANVLTQKWFPQRAVLKHKNVKAFVTQGGVQSTDEAIDALVPMVGLPMMGDQFYNTNKYVE-LGIGRA 411
|
.
gi 1731019548 416 V 416
Cdd:PHA03392 412 L 412
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
496-670 |
6.56e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 496 AAQPSRNRNRAVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPtrqPAESRRFDPTQAqPKRQSVAVAER 575
Cdd:PHA03247 2574 APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDP---PPPSPSPAANEP-DPHPPPTVPPP 2649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 576 SR------GSRTTNSRRAARNPEAEASRAKPSRVSPvasRAASPPVASRAAREIPVPSRAASAQAEPVLSSSsraarTKL 649
Cdd:PHA03247 2650 ERprddpaPGRVSRPRRARRLGRAAQASSPPQRPRR---RAARPTVGSLTSLADPPPPPPTPEPAPHALVSA-----TPL 2721
|
170 180
....*....|....*....|.
gi 1731019548 650 APSTYILRGISSVGARALQPP 670
Cdd:PHA03247 2722 PPGPAAARQASPALPAAPAPP 2742
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
505-636 |
9.32e-06 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 50.87 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 505 RAVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRfdPTQAQPKRQSVAVAERSRGSRTTNS 584
Cdd:PRK14951 365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAP--PAAAPPAPVAAPAAAAPAAAPAAAP 442
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1731019548 585 RRAARNPEAEAsRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEP 636
Cdd:PRK14951 443 AAVALAPAPPA-QAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
|
|
| transpos_IS481 |
NF033577 |
IS481 family transposase; null |
1950-2078 |
3.65e-05 |
|
IS481 family transposase; null
Pssm-ID: 468094 [Multi-domain] Cd Length: 283 Bit Score: 47.97 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1950 RQHPAGLLQplsvpgwkwesvsMDfITGLPKTL-RGYTVIWVVVDRLTKSAH--FVPGKSTYTASKwgqlYMTEIVRLHG 2026
Cdd:NF033577 124 RAHPGELWH-------------ID-IKKLGRIPdVGRLYLHTAIDDHSRFAYaeLYPDETAETAAD----FLRRAFAEHG 185
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1731019548 2027 VPV-SIISDRDARFTSKFwKGLQLAL---GTRLDFSTAFHPQTDGQTERLNQILED 2078
Cdd:NF033577 186 IPIrRVLTDNGSEFRSRA-HGFELALaelGIEHRRTRPYHPQTNGKVERFHRTLKD 240
|
|
| rve |
pfam00665 |
Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into ... |
1963-2063 |
4.41e-05 |
|
Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain pfam02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain pfam00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyzes the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.
Pssm-ID: 459897 [Multi-domain] Cd Length: 98 Bit Score: 44.23 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1963 PGWKWEsvsMDFITGLPKTLRGYTVIWVVVDRLTK--SAHFVPGKSTYTAskWGQLYMTEIVRLHGVPVSIISDRDARFT 2040
Cdd:pfam00665 1 PNQLWQ---GDFTYIRIPGGGGKLYLLVIVDDFSReiLAWALSSEMDAEL--VLDALERAIAFRGGVPLIIHSDNGSEYT 75
|
90 100
....*....|....*....|...
gi 1731019548 2041 SKFWKGLQLALGTRLDFSTAFHP 2063
Cdd:pfam00665 76 SKAFREFLKDLGIKPSFSRPGNP 98
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
497-634 |
4.62e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.83 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 497 AQPSRNRNRAVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAesrrfdPTQAQPkrqsvaVAERS 576
Cdd:PRK07764 380 RLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPA------PAPAPP------SPAGN 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1731019548 577 RGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQA 634
Cdd:PRK07764 448 APAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAG 505
|
|
| RnhA |
COG0328 |
Ribonuclease HI [Replication, recombination and repair]; |
1686-1800 |
4.79e-05 |
|
Ribonuclease HI [Replication, recombination and repair];
Pssm-ID: 440097 [Multi-domain] Cd Length: 136 Bit Score: 45.22 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1686 VIYSDAS------KKGLGCVLMQQGKVvayasRQLKIHEQNYPTHDLELAAVVFALKIWRHyLYGEKIQIYTDHKSLKYF 1759
Cdd:COG0328 4 EIYTDGAcrgnpgPGGWGAVIRYGGEE-----KELSGGLGDTTNNRAELTALIAALEALKE-LGPCEVEIYTDSQYVVNQ 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1731019548 1760 FTQKELNMRQRRW------------LELVKDYDCEILYHPGKA----NVVADALSRK 1800
Cdd:COG0328 78 ITGWIHGWKKNGWkpvknpdlwqrlDELLARHKVTFEWVKGHAghpgNERADALANK 134
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
510-653 |
6.93e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.06 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 510 LPAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAESrrfdPTQAQPKRQSVAVAersrgsrttnsRRAAR 589
Cdd:PRK07764 364 LPSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAA----PAPAAAAPAAAAAP-----------APAAA 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731019548 590 NPEAEASRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPVLSSSSRAARTKLAPST 653
Cdd:PRK07764 429 PQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAA 492
|
|
| RT_pepA17 |
cd01644 |
RT_pepA17: Reverse transcriptase (RTs) in retrotransposons. This subfamily represents the RT ... |
1464-1611 |
8.39e-05 |
|
RT_pepA17: Reverse transcriptase (RTs) in retrotransposons. This subfamily represents the RT domain of a multifunctional enzyme. C-terminal to the RT domain is a domain homologous to aspartic proteinases (corresponding to Merops family A17) encoded by retrotransposons and retroviruses. RT catalyzes DNA replication from an RNA template and is responsible for the replication of retroelements.
Pssm-ID: 238822 Cd Length: 213 Bit Score: 46.14 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1464 DLFDQL----QGATVFSKiDLRSGYHQLRIR-------------DGDIPKTAfrsrygHYEFVVMSFGLTNAPAvfmdLM 1526
Cdd:cd01644 47 SLFGVLlrfrQGKIAVSA-DIEKMFHQVKVRpedrdvlrflwrkDGDEPKPI------EYRMTVVPFGAASAPF----LA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 1527 NRVFKEFLDSF----------VIVFIDDILIYSKTEAEHEEhlhqVLETLRANKLYAKFSKCEFWLRKVTFLGHVvssEG 1596
Cdd:cd01644 116 NRALKQHAEDHpheaaakiikRNFYVDDILVSTDTLNEAVN----VAKRLIALLKKGGFNLRKWASNSQEVLDDL---PE 188
|
170
....*....|....*
gi 1731019548 1597 VSVDPAKIEAVTNWT 1611
Cdd:cd01644 189 ERVLLDRDSDVTEKT 203
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
488-634 |
8.56e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 47.92 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 488 PPSILLCSAAQPSRNRNRAVAELPAAPGESSKPIC--AAERPSEQPSLARRSRVEAASARPQPTRQPAESRRFDPTQAQP 565
Cdd:PRK07003 401 AVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATadRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAP 480
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731019548 566 KRQSVAVAERSRGSRTTNSRRAARNPEAEASR----AKPSRVSPVASRA-ASPPVASRAAREipvPSRAASAQA 634
Cdd:PRK07003 481 ASDAPPDAAFEPAPRAAAPSAATPAAVPDARApaaaSREDAPAAAAPPApEARPPTPAAAAP---AARAGGAAA 551
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
496-652 |
1.67e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 47.15 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 496 AAQPSRNRNRAVAELPAAPGESSKPICAAERPSEQPSLAR-RSRVEAASARPQP--TRQPAESRRFDPTQAQPKRQSVAV 572
Cdd:PRK07003 379 AVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAaATRAEAPPAAPAPpaTADRGDDAADGDAPVPAKANARAS 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 573 AERSRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPVLSSSSRAARTKLAPS 652
Cdd:PRK07003 459 ADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPA 538
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
511-646 |
1.77e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.90 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 511 PAAPGESSKPICAAERPSEQPSLARrSRVEAASARPQPTRQPAES--------RRFDPTQAQPKRQSVAVAERSRGSRTT 582
Cdd:PRK07764 593 GAAGGEGPPAPASSGPPEEAARPAA-PAAPAAPAAPAPAGAAAAPaeasaapaPGVAAPEHHPKHVAVPDASDGGDGWPA 671
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731019548 583 NSRRAArnPEAEASRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPVLSSSSRAAR 646
Cdd:PRK07764 672 KAGGAA--PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSP 733
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
488-641 |
1.89e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.79 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 488 PPSILLCSAAQPSRNRNRAVAELPAAPgeSSKPIcAAERPSEQPSLARRSRVEAASARPQPTRQPA---------ESRRF 558
Cdd:PRK12323 428 PAPEALAAARQASARGPGGAPAPAPAP--AAAPA-AAARPAAAGPRPVAAAAAAAPARAAPAAAPApadddpppwEELPP 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 559 DPTQAQPKRQSVAVAERSRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPVL 638
Cdd:PRK12323 505 EFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPAL 584
|
...
gi 1731019548 639 SSS 641
Cdd:PRK12323 585 AAR 587
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
507-624 |
2.38e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 46.11 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 507 VAELPAAPGESSKPICAAERPSEQPSLARRsrvEAASARPQPTRQPAESRrfdptqAQPKRQSVAVAERSRGSRTTNSRR 586
Cdd:PRK06995 52 APPAAAAPAAAQPPPAAAPAAVSRPAAPAA---EPAPWLVEHAKRLTAQR------EQLVARAAAPAAPEAQAPAAPAER 122
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1731019548 587 AARNP-EAEASRAKPS----RVSPVASRAASPPVASRAAREIP 624
Cdd:PRK06995 123 AAAENaARRLARAAAAaprpRVPADAAAAVADAVKARIERIVN 165
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
512-671 |
2.70e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.38 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 512 AAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRfdPTQAQPKRQSVAVAERSRgsrttnSRRAARNP 591
Cdd:PRK07003 366 GAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALA--PKAAAAAAATRAEAPPAA------PAPPATAD 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 592 EAEASRAKPsrvSPVASRAASP-PVASRAAREIPVPSRAASAQAEPVlSSSSRAARTKLAPSTYILRGISSVGARALQPP 670
Cdd:PRK07003 438 RGDDAADGD---APVPAKANARaSADSRCDERDAQPPADSGSASAPA-SDAPPDAAFEPAPRAAAPSAATPAAVPDARAP 513
|
.
gi 1731019548 671 S 671
Cdd:PRK07003 514 A 514
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
506-671 |
3.28e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 45.75 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 506 AVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAA-----SARPQptRQPAESRRFDPTQAQPKRQSVAVAERSRGSR 580
Cdd:PRK12727 68 APAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAaedmiAAMAL--RQPVSVPRQAPAAAPVRAASIPSPAAQALAH 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 581 TTNSRRAARNPEAEASRakPSRVSPVASRAASPPVASRAAREIPVPSRA-ASAQAEPVLSSSSRAARTKLAPSTYILrgi 659
Cdd:PRK12727 146 AAAVRTAPRQEHALSAV--PEQLFADFLTTAPVPRAPVQAPVVAAPAPVpAIAAALAAHAAYAQDDDEQLDDDGFDL--- 220
|
170
....*....|..
gi 1731019548 660 SSVGARALQPPS 671
Cdd:PRK12727 221 DDALPQILPPAA 232
|
|
| PHA03381 |
PHA03381 |
tegument protein VP22; Provisional |
514-653 |
3.70e-04 |
|
tegument protein VP22; Provisional
Pssm-ID: 177618 [Multi-domain] Cd Length: 290 Bit Score: 45.00 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 514 PGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRfdPTQAQPKRQSVAVAERSRGSrttnSRRAARNPEA 593
Cdd:PHA03381 40 PADRARRGAGQARGRSQAERRFHHYDEARADYPYYTGSSSEDER--PADPRPSRRPHAQPEASGPG----PARGARGPAG 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731019548 594 EASRAK----PSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPVLSSSSRAARTKLAPST 653
Cdd:PHA03381 114 SRGRGRraesPSPRDPPNPKGASAPRGRKSACADSAALLDAPAPAAPKRQKTPAGLARKLHFST 177
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
495-652 |
6.09e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 44.86 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 495 SAAQPSRNRNRAVAELPAAPGESSKPicAAERPSEQPSLAR-RSRVEAASARPQPTRQPAESR--RFDPTQAQPKRQSVA 571
Cdd:PRK07994 377 PAASAQATAAPTAAVAPPQAPAVPPP--PASAPQQAPAVPLpETTSQLLAARQQLQRAQGATKakKSEPAAASRARPVNS 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 572 VAERSRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREipvPSRAASAQAEPVLSSSSRAARTKLAP 651
Cdd:PRK07994 455 ALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALE---HEKTPELAAKLAAEAIERDPWAALVS 531
|
.
gi 1731019548 652 S 652
Cdd:PRK07994 532 Q 532
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
487-671 |
6.25e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 487 DPPSILLCSAAQPSRNRNRavaelPAAPGESSKPICAA----------ERPSEQPSLARRSRVEAASARPQPTRQPAESR 556
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPD-----PPPPSPSPAANEPDphppptvpppERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ 2681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 557 RFDPTQAQPkrqsvAVAERSRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRaareiPVPSRAASAQAEP 636
Cdd:PHA03247 2682 RPRRRAARP-----TVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA-----PAPPAVPAGPATP 2751
|
170 180 190
....*....|....*....|....*....|....*.
gi 1731019548 637 V-LSSSSRAARTKLAPSTYILRGISSVGARALQPPS 671
Cdd:PHA03247 2752 GgPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPA 2787
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
508-651 |
8.26e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 44.71 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 508 AELPAAPGESS------------KPICAAER--PSEQPSLARRSRVEAASARPQPTRQPAESRRFDPTQAQPKRQSVAVA 573
Cdd:PRK14951 342 AELGLAPDEYAaltmvllrllafKPAAAAEAaaPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 574 ErsrgsrttnSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREIP--VPSRAASAQAEPVLSSSSRAARTKLAP 651
Cdd:PRK14951 422 P---------PAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPvrVAPEPAVASAAPAPAAAPAAARLTPTE 492
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
523-672 |
9.16e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 523 AAERPSEQPSLARRSRVEAAsARPQPTRQPAEsrrfdptQAQPKRQSVAvAERSRGSRTTNSRRAA--RNPEAEASRAKP 600
Cdd:PRK07764 593 GAAGGEGPPAPASSGPPEEA-ARPAAPAAPAA-------PAAPAPAGAA-AAPAEASAAPAPGVAApeHHPKHVAVPDAS 663
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731019548 601 SRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPVlSSSSRAARTKLAPSTYILRGISSVGARALQPPSR 672
Cdd:PRK07764 664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQ-PAPAPAATPPAGQADDPAAQPPQAAQGASAPSPA 734
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
495-652 |
9.30e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.46 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 495 SAAQPSRNRNRAVAELPAAPGESSKPICAAerPSEQPSLARRSRVEAASArpqPTRQPAESRRFDPTQAQPKRQSVAVAE 574
Cdd:PRK07003 372 VPARVAGAVPAPGARAAAAVGASAVPAVTA--VTGAAGAALAPKAAAAAA---ATRAEAPPAAPAPPATADRGDDAADGD 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731019548 575 rSRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPVLSSSSRAARTKLAPS 652
Cdd:PRK07003 447 -APVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPA 523
|
|
| RP_DDI |
cd05479 |
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ... |
1250-1291 |
1.07e-03 |
|
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI.
Pssm-ID: 133146 Cd Length: 124 Bit Score: 41.00 E-value: 1.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1731019548 1250 IKACRVEIANRMLDVTLLVLDMQDFDVILGMDWLSANHANID 1291
Cdd:cd05479 75 IHLAQVKIGNLFLPCSFTVLEDDDVDFLIGLDMLKRHQCVID 116
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
495-676 |
1.18e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 495 SAAQPSRNRNRAVAElPAAPGESSKPI----CAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRFDP-----TQAQP 565
Cdd:PRK07764 600 PPAPASSGPPEEAAR-PAAPAAPAAPAapapAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGwpakaGGAAP 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 566 KRQSVAVAERSRGSRTTnsrrAARNPEAEASRAKPSRVSPVASRAASPPVASRAAREIPVPSRAASAQAEPVLSSSSRAA 645
Cdd:PRK07764 679 AAPPPAPAPAAPAAPAG----AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGA 754
|
170 180 190
....*....|....*....|....*....|.
gi 1731019548 646 RTKLAPSTYILRGISSVGARALQPPSRDFVA 676
Cdd:PRK07764 755 PAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
487-656 |
1.64e-03 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 44.08 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 487 DPPSILLCSAAQPSRNRNRAVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRFDPTQAQPk 566
Cdd:PLN03237 1284 KMEETVKAVPARRAAARKKPLASVSVISDSDDDDDDFAVEVSLAERLKKKGGRKPAAANKKAAKPPAAAKKRGPATVQS- 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 567 rQSVAVAERSRGSRTTNSrraarNPEaeaSRAKPSRVSPVASRAASppVASRAAREI------PVPSRAASAQAEPVLSS 640
Cdd:PLN03237 1363 -GQKLLTEMLKPAEAIGI-----SPE---KKVRKMRASPFNKKSGS--VLGRAATNKetesseNVSGSSSSEKDEIDVSA 1431
|
170
....*....|....*.
gi 1731019548 641 SSRAARTKLAPSTYIL 656
Cdd:PLN03237 1432 KPRPQRANRKQTTYVL 1447
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
496-647 |
1.71e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.71 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 496 AAQPSRNRNRAVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTrqPAESRRFDPTQAQPKRQSVAVAER 575
Cdd:PRK12323 404 AAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAA--PAAAARPAAAGPRPVAAAAAAAPA 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 576 SRGSRTTNSRRAARNPEAEASRAKPSRVSPVASRAASPPVAS-----------RAAREIPVPSRAASAQAEPVLSSSSRA 644
Cdd:PRK12323 482 RAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAesipdpatadpDDAFETLAPAPAAAPAPRAAAATEPVV 561
|
...
gi 1731019548 645 ART 647
Cdd:PRK12323 562 APR 564
|
|
| gag-asp_proteas |
pfam13975 |
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ... |
1224-1284 |
1.72e-03 |
|
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins.
Pssm-ID: 464060 Cd Length: 92 Bit Score: 39.48 E-value: 1.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731019548 1224 GLEVEPLGSVLSVSTPSGEVllSKEQIKACRVEIANRML-DVTLLVLDMQDFDVILGMDWLS 1284
Cdd:pfam13975 32 GLDRLVDAYPVTVRTANGTV--RAARVRLDSVKIGGIELrNVPAVVLPGDLDDVLLGMDFLK 91
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
505-670 |
1.90e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 505 RAVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRFDPTQAQPKRQSVAVAERSRGSRTTNS 584
Cdd:PHA03307 267 TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 585 R-RAARNPEAEASRAKPSRVSPVASRAASPPVASRAAReiPVPSRAASAQAEPVLSSSSRAARTKLAPSTYILRGISSVG 663
Cdd:PHA03307 347 PsRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGR--PTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASG 424
|
....*..
gi 1731019548 664 ARALQPP 670
Cdd:PHA03307 425 AFYARYP 431
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
505-622 |
1.97e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 505 RAVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRFDPTQAQPKRQSVAVAERSRGSRTTNS 584
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146
|
90 100 110
....*....|....*....|....*....|....*...
gi 1731019548 585 RRAARNPEAEASRAKPSRVSPVASRAASPPVASRAARE 622
Cdd:PRK12678 147 EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAE 184
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
495-642 |
2.10e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 495 SAAQPSRNRNRAVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAASAR---------PQPTRQPAESRRFDPTQAQP 565
Cdd:PHA03307 773 ALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRShtpdggsesSGPARPPGAAARPPPARSSE 852
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731019548 566 KRQSVAVAERSRGSrttnSRRAARNPEAEASRAKPSrvspvasrAASPPVASRAAREIPVPSRAASAQAEPVLSSSS 642
Cdd:PHA03307 853 SSKSKPAAAGGRAR----GKNGRRRPRPPEPRARPG--------AAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPMP 917
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
496-602 |
2.22e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 496 AAQPSRNRNRAVAELPAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRfdptqAQPKRQSVAVAER 575
Cdd:PRK12678 99 AAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADA-----AERTEEEERDERR 173
|
90 100
....*....|....*....|....*..
gi 1731019548 576 SRGSRTTNSRRAARNPEAEASRAKPSR 602
Cdd:PRK12678 174 RRGDREDRQAEAERGERGRREERGRDG 200
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
511-674 |
2.77e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 511 PAAPGESSKPICAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRFDPTQAQPKRQSVAVAERSRGSRttnsrRAARN 590
Cdd:PHA03307 78 EAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPP-----PAASP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 591 PEAEASRAkpsrvsPVASRAASPPVASRAAREIPVPSRAASAQAEPVLSSSSRAARTKLAPSTYILRGISSVGARALQPP 670
Cdd:PHA03307 153 PAAGASPA------AVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR 226
|
....
gi 1731019548 671 SRDF 674
Cdd:PHA03307 227 SAAD 230
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
532-644 |
3.46e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 42.26 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 532 SLARRSRVEAASARPQPTRQPAESRRFDPTQAQPKRQSVAVAERSRGSRTTNSRRAARNPEAEA-SRAKPSRVSPVASRA 610
Cdd:PRK06995 50 ALAPPAAAAPAAAQPPPAAAPAAVSRPAAPAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAqAPAAPAERAAAENAA 129
|
90 100 110
....*....|....*....|....*....|....
gi 1731019548 611 ASPPVASRAAREIPVPSRAASAQAEPVLSSSSRA 644
Cdd:PRK06995 130 RRLARAAAAAPRPRVPADAAAAVADAVKARIERI 163
|
|
| CD_POL_like |
cd18979 |
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins ... |
2268-2315 |
3.58e-03 |
|
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins (Z195D10.9), and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Zea maize Z195D10.9 protein, and other putative TY3/gypsy retrotransposon polyproteins. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.
Pssm-ID: 349335 Cd Length: 48 Bit Score: 37.47 E-value: 3.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1731019548 2268 QPVEVLAREVKKLRSREIpLVKilWQNHGVEEATWEKEEDMRAQYPEL 2315
Cdd:cd18979 2 FPEKVLDIRQRDKGNKEF-LVQ--WQGLSVEEATWEPYKDLVQQFPDF 46
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
503-643 |
3.78e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 42.55 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 503 RNRAVAELPAAPGESSKPICAAERPSEQPslarrsrveAASARPQPTRQPAEsrrfdPTQAQPKRQSVAVAErsrgsrTT 582
Cdd:PRK07994 360 HPAAPLPEPEVPPQSAAPAASAQATAAPT---------AAVAPPQAPAVPPP-----PASAPQQAPAVPLPE------TT 419
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731019548 583 NSRRAARNP-EAEASRAKPSRVSPVASrAASPPVASRAAREIPVPSRAASAQAEPVLSSSSR 643
Cdd:PRK07994 420 SQLLAARQQlQRAQGATKAKKSEPAAA-SRARPVNSALERLASVRPAPSALEKAPAKKEAYR 480
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
505-650 |
4.22e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 505 RAVAE--LPAAPGEsskpicaAERPSEQPSlaRRSRVEAASARPQPT----RQPAESRRF---DPTQAQpkrQSVAVAER 575
Cdd:NF041483 173 RAEAEqaLAAARAE-------AERLAEEAR--QRLGSEAESARAEAEailrRARKDAERLlnaASTQAQ---EATDHAEQ 240
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731019548 576 SRGSRTTNSRrAARNPEAEASRAKPSRVSPvasraasppvASRAAREipvpsraASAQAEPVLSSSSRAARTKLA 650
Cdd:NF041483 241 LRSSTAAESD-QARRQAAELSRAAEQRMQE----------AEEALRE-------ARAEAEKVVAEAKEAAAKQLA 297
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
494-636 |
5.12e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 494 CSAAQPSR-------NRNRAVAEL-PAAPGESSKPICAAERPSEQPSlaRRSRVEAASARPQPTRQPAESRRfdPTQAQP 565
Cdd:PHA03307 295 SPSPSPSSpgsgpapSSPRASSSSsSSRESSSSSTSSSSESSRGAAV--SPGPSPSRSPSPSRPPPPADPSS--PRKRPR 370
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731019548 566 KRQSVAVAERSRGSRTtnSRRAAR-NPEAEASRAKPSRvSPVASRAASPPVASRAAREIPVPSRAASAQAEP 636
Cdd:PHA03307 371 PSRAPSSPAASAGRPT--RRRARAaVAGRARRRDATGR-FPAGRPRPSPLDAGAASGAFYARYPLLTPSGEP 439
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
496-627 |
9.18e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 40.91 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731019548 496 AAQPSRNRNRAVAELPAAPGEsskpicAAERPSEQPSLARRSRVEAASARPQPTRQPAESRRFDPTQAQPKRQSVAVAER 575
Cdd:NF040712 206 AREPADARPEEVEPAPAAEGA------PATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1731019548 576 SRGSRTTNSRRAARNPE----AEASRAKPSRVSPVASRAASPPVASRAAREIPVPS 627
Cdd:NF040712 280 PPAPGAAETPEAAEPPApapaAPAAPAAPEAEEPARPEPPPAPKPKRRRRRASVPS 335
|
|
|