|
Name |
Accession |
Description |
Interval |
E-value |
| folA |
PRK10769 |
type 3 dihydrofolate reductase; |
1038-1195 |
1.77e-115 |
|
type 3 dihydrofolate reductase;
:
Pssm-ID: 182714 [Multi-domain] Cd Length: 159 Bit Score: 362.13 E-value: 1.77e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1038 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTDDRVTWVKSVDEA 1117
Cdd:PRK10769 2 ISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIVISSQPGTDDRVTWVKSVDEA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844115814 1118 IAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR 1195
Cdd:PRK10769 82 LAAAGDVPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYEPDEWESVFSEFHDADEQNSHSYCFEILERR 159
|
|
| CAF1 super family |
cl23804 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
292-571 |
2.31e-110 |
|
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.
The actual alignment was detected with superfamily member COG5228:
Pssm-ID: 474062 Cd Length: 299 Bit Score: 353.84 E-value: 2.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 292 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 369
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 370 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 449
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 450 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 529
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115814 530 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 571
Cdd:COG5228 246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
|
|
| CAF1 super family |
cl23804 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
735-1014 |
2.31e-110 |
|
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.
The actual alignment was detected with superfamily member COG5228:
Pssm-ID: 474062 Cd Length: 299 Bit Score: 353.84 E-value: 2.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 735 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 812
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 813 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 892
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 893 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 972
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115814 973 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 1014
Cdd:COG5228 246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
|
|
| Peptidase_S29 |
pfam02907 |
Hepatitis C virus NS3 protease; Hepatitis C virus NS3 protein is a serine protease which has a ... |
1906-2054 |
1.30e-87 |
|
Hepatitis C virus NS3 protease; Hepatitis C virus NS3 protein is a serine protease which has a trypsin-like fold. The non-structural (NS) protein NS3 is one of the NS proteins involved in replication of the HCV genome. NS2-3 proteinase, a zinc-dependent enzyme, performs a single proteolytic cut to release the N-terminus of NS3. The action of NS3 proteinase (NS3P), which resides in the N-terminal one-third of the NS3 protein, then yields all remaining non-structural proteins. The C-terminal two-thirds of the NS3 protein contain a helicase. The functional relationship between the proteinase and helicase domains is unknown. NS3 has a structural zinc-binding site and requires cofactor NS4A.
:
Pssm-ID: 427049 Cd Length: 149 Bit Score: 282.01 E-value: 1.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1906 EGEVQIVSTATQTFLATCINGVCWAVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTR 1985
Cdd:pfam02907 1 EGEVQVLGTATQRFMGTCVNGVLWTTFHGAGSRTLAGPKGPVNQMYWSASDDVVGYPLPPGAGSLTPCTCGATDLYLVTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115814 1986 HADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETT 2054
Cdd:pfam02907 81 DGDLIPGRRRGDPRVSLLSPRPLSYLKGSSGGPILCPSGHVVGMFRAAVHSGGVVKAVRFVPWETLPTT 149
|
|
| cp |
PHA00026 |
coat protein |
160-288 |
1.46e-85 |
|
coat protein
:
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 160 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 239
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115814 240 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 288
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| cp |
PHA00026 |
coat protein |
603-731 |
1.46e-85 |
|
coat protein
:
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 603 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 682
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115814 683 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 731
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| eL8_ribo |
TIGR03677 |
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version ... |
1716-1832 |
8.50e-69 |
|
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version of the large ribosomal complex protein eL8, previously designated L8 in yeast and L7Ae in the archaea. The family is a narrower version of the pfam01248 model which also recognizes the L30 protein.
:
Pssm-ID: 188367 [Multi-domain] Cd Length: 117 Bit Score: 226.95 E-value: 8.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1716 YVRFEVPEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKND 1795
Cdd:TIGR03677 1 YVKFEVPEELADKALEAVEKARETGKIKKGTNEVTKAVERGIAKLVVIAEDVEPPEIVAHLPALCEEKGIPYIYVKSKED 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844115814 1796 LGRAVGIEVPCASAAIINEGELRKELGSLVEKIKGLQ 1832
Cdd:TIGR03677 81 LGAAAGLEVGAASAAIVDAGKAEELLKEIIEKVEALK 117
|
|
| FRB_dom |
pfam08771 |
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ... |
1347-1439 |
1.15e-55 |
|
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein FKBP12 can form a complex which specifically inhibits the TORC1 complex, leading to growth arrest. The FKBP12-rapamycin complex interferes with TORC1 function by binding to the FKBP12-rapamycin binding domain (FRB) of the TOR proteins. This entry represents the FRB domain.
:
Pssm-ID: 462596 Cd Length: 98 Bit Score: 188.56 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1347 SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLLQ 1426
Cdd:pfam08771 6 AILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDEEDLNQ 85
|
90
....*....|...
gi 1844115814 1427 AWDLYYHVFRRIS 1439
Cdd:pfam08771 86 AWDIYYSVFRRIK 98
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
1461-1564 |
3.26e-43 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
:
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 153.03 E-value: 3.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1461 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 1540
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115814 1541 YGATGHPGIIPPHATLVFDVELLK 1564
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
4-107 |
5.44e-42 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
:
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 149.56 E-value: 5.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 4 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 83
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115814 84 YGATGHPGIIPPHATLVFDVELLK 107
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| Peptidase_C4 super family |
cl24133 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1226-1339 |
6.27e-24 |
|
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses.
The actual alignment was detected with superfamily member pfam00863:
Pssm-ID: 279235 Cd Length: 243 Bit Score: 102.86 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1226 ESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNG--TLLVQSLHGVFKVKNTTTLQQHLIDG 1303
Cdd:pfam00863 4 KSIAKGLRDYHHIASNLAALEYYCGDHKGEIHGICHGDKIITPAHLFKEACGndTLKIQSKHGLFDLEALDRQKIEELCG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844115814 1304 RDMIIIRMPKDFPPFPQKLKFREPQREER----ICLVTTN 1339
Cdd:pfam00863 84 QDIIVIKGPIDMPPAKMRLIFRAPIQCERavliGCRRDDN 123
|
|
| HCV_NS4a |
pfam01006 |
Hepatitis C virus non-structural protein NS4a; NS4a forms an integral part of the NS3 serine ... |
2095-2138 |
1.89e-17 |
|
Hepatitis C virus non-structural protein NS4a; NS4a forms an integral part of the NS3 serine protease, as it is required in a number of cases as a cofactor of cleavage. It has also been reported that NS4a interacts with NS4b and NS3 to form a multi-subunit replicase complex.
:
Pssm-ID: 366414 Cd Length: 55 Bit Score: 77.89 E-value: 1.89e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1844115814 2095 STWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPA--MPDREVLY 2138
Cdd:pfam01006 1 STWVLVGGALAAGAAYCLTTGSVVVVGRWSVNGKPPavVPDREVLY 46
|
|
| Peptidase_C4 super family |
cl24133 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1580-1683 |
5.74e-14 |
|
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses.
The actual alignment was detected with superfamily member pfam00863:
Pssm-ID: 279235 Cd Length: 243 Bit Score: 73.97 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1580 DTSCTFPSS--DGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSAS----NFTNTN-NYFTSVPKNFMELLTNQE-AQQW 1651
Cdd:pfam00863 131 DESAIFPLGkeNGGFWKHGCDTKLGDCGGPIIACDDMDIIGFHGGRlmqlGANNSLaHIFAALNDDFIEMFAEMEtAKGF 210
|
90 100 110
....*....|....*....|....*....|..
gi 1844115814 1652 VSGWRLNADSVLWGGHKVFMVKPEEPFQPVKE 1683
Cdd:pfam00863 211 QRKWKFNADKVEWGRLDLTSNQPSGAFKIQKL 242
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| folA |
PRK10769 |
type 3 dihydrofolate reductase; |
1038-1195 |
1.77e-115 |
|
type 3 dihydrofolate reductase;
Pssm-ID: 182714 [Multi-domain] Cd Length: 159 Bit Score: 362.13 E-value: 1.77e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1038 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTDDRVTWVKSVDEA 1117
Cdd:PRK10769 2 ISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIVISSQPGTDDRVTWVKSVDEA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844115814 1118 IAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR 1195
Cdd:PRK10769 82 LAAAGDVPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYEPDEWESVFSEFHDADEQNSHSYCFEILERR 159
|
|
| POP2 |
COG5228 |
mRNA deadenylase subunit [RNA processing and modification]; |
292-571 |
2.31e-110 |
|
mRNA deadenylase subunit [RNA processing and modification];
Pssm-ID: 227553 Cd Length: 299 Bit Score: 353.84 E-value: 2.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 292 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 369
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 370 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 449
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 450 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 529
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115814 530 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 571
Cdd:COG5228 246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
|
|
| POP2 |
COG5228 |
mRNA deadenylase subunit [RNA processing and modification]; |
735-1014 |
2.31e-110 |
|
mRNA deadenylase subunit [RNA processing and modification];
Pssm-ID: 227553 Cd Length: 299 Bit Score: 353.84 E-value: 2.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 735 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 812
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 813 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 892
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 893 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 972
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115814 973 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 1014
Cdd:COG5228 246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
|
|
| Peptidase_S29 |
pfam02907 |
Hepatitis C virus NS3 protease; Hepatitis C virus NS3 protein is a serine protease which has a ... |
1906-2054 |
1.30e-87 |
|
Hepatitis C virus NS3 protease; Hepatitis C virus NS3 protein is a serine protease which has a trypsin-like fold. The non-structural (NS) protein NS3 is one of the NS proteins involved in replication of the HCV genome. NS2-3 proteinase, a zinc-dependent enzyme, performs a single proteolytic cut to release the N-terminus of NS3. The action of NS3 proteinase (NS3P), which resides in the N-terminal one-third of the NS3 protein, then yields all remaining non-structural proteins. The C-terminal two-thirds of the NS3 protein contain a helicase. The functional relationship between the proteinase and helicase domains is unknown. NS3 has a structural zinc-binding site and requires cofactor NS4A.
Pssm-ID: 427049 Cd Length: 149 Bit Score: 282.01 E-value: 1.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1906 EGEVQIVSTATQTFLATCINGVCWAVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTR 1985
Cdd:pfam02907 1 EGEVQVLGTATQRFMGTCVNGVLWTTFHGAGSRTLAGPKGPVNQMYWSASDDVVGYPLPPGAGSLTPCTCGATDLYLVTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115814 1986 HADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETT 2054
Cdd:pfam02907 81 DGDLIPGRRRGDPRVSLLSPRPLSYLKGSSGGPILCPSGHVVGMFRAAVHSGGVVKAVRFVPWETLPTT 149
|
|
| cp |
PHA00026 |
coat protein |
160-288 |
1.46e-85 |
|
coat protein
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 160 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 239
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115814 240 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 288
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| cp |
PHA00026 |
coat protein |
603-731 |
1.46e-85 |
|
coat protein
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 603 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 682
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115814 683 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 731
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| DHFR_1 |
pfam00186 |
Dihydrofolate reductase; |
1038-1194 |
1.67e-77 |
|
Dihydrofolate reductase;
Pssm-ID: 425512 [Multi-domain] Cd Length: 159 Bit Score: 253.62 E-value: 1.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1038 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTD-DRVTWVKSVDE 1116
Cdd:pfam00186 2 ISLIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGRPLPGRKNIVLTRNPDYKvDGVEVVHSLEE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844115814 1117 AIAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILER 1194
Cdd:pfam00186 82 ALALAAEAEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPEIDPSEWQLVSREEHEADEKNPYPYTFVTYER 159
|
|
| Levi_coat |
pfam01819 |
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ... |
161-287 |
1.55e-69 |
|
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that encapsidates the viral RNA. 180 copies of this protein form the virion shell. The MS2 bacteriophage coat protein controls two distinct processes: sequence-specific RNA encapsidation and repression of replicase translation-by binding to an RNA stem-loop structure of 19 nucleotides containing the initiation codon of the replicase gene. The binding of a coat protein dimer to this hairpin shuts off synthesis of the viral replicase, switching the viral replication cycle to virion assembly rather than continued replication.
Pssm-ID: 396403 Cd Length: 132 Bit Score: 229.62 E-value: 1.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 161 SNFTQFVLVDNGGTGDVTVAPS----NFANGVAEWISSNSRSQAYK-VTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVE 235
Cdd:pfam01819 1 AKFQAFTLSDIGGNGDVTLALNprgvNFANGVAALIEAGARPAAEKrVTCSVRQPSANNKKYKIKVEIPKPASCTAGGTC 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1844115814 236 LPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGI 287
Cdd:pfam01819 81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
|
|
| Levi_coat |
pfam01819 |
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ... |
604-730 |
1.55e-69 |
|
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that encapsidates the viral RNA. 180 copies of this protein form the virion shell. The MS2 bacteriophage coat protein controls two distinct processes: sequence-specific RNA encapsidation and repression of replicase translation-by binding to an RNA stem-loop structure of 19 nucleotides containing the initiation codon of the replicase gene. The binding of a coat protein dimer to this hairpin shuts off synthesis of the viral replicase, switching the viral replication cycle to virion assembly rather than continued replication.
Pssm-ID: 396403 Cd Length: 132 Bit Score: 229.62 E-value: 1.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 604 SNFTQFVLVDNGGTGDVTVAPS----NFANGVAEWISSNSRSQAYK-VTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVE 678
Cdd:pfam01819 1 AKFQAFTLSDIGGNGDVTLALNprgvNFANGVAALIEAGARPAAEKrVTCSVRQPSANNKKYKIKVEIPKPASCTAGGTC 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1844115814 679 LPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGI 730
Cdd:pfam01819 81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
|
|
| eL8_ribo |
TIGR03677 |
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version ... |
1716-1832 |
8.50e-69 |
|
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version of the large ribosomal complex protein eL8, previously designated L8 in yeast and L7Ae in the archaea. The family is a narrower version of the pfam01248 model which also recognizes the L30 protein.
Pssm-ID: 188367 [Multi-domain] Cd Length: 117 Bit Score: 226.95 E-value: 8.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1716 YVRFEVPEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKND 1795
Cdd:TIGR03677 1 YVKFEVPEELADKALEAVEKARETGKIKKGTNEVTKAVERGIAKLVVIAEDVEPPEIVAHLPALCEEKGIPYIYVKSKED 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844115814 1796 LGRAVGIEVPCASAAIINEGELRKELGSLVEKIKGLQ 1832
Cdd:TIGR03677 81 LGAAAGLEVGAASAAIVDAGKAEELLKEIIEKVEALK 117
|
|
| DHFR |
cd00209 |
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ... |
1038-1193 |
1.48e-65 |
|
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.
Pssm-ID: 238127 [Multi-domain] Cd Length: 158 Bit Score: 219.32 E-value: 1.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1038 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIG-RPLPGRKNIILSSQPST--DDRVTWVKSV 1114
Cdd:cd00209 1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrRPLPGRTNIVLSRQLDYqdAEGVEVVHSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1115 DEAIAACG-DVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEfhDADAQNSHSYCFEILE 1193
Cdd:cd00209 81 EEALELAEnTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIDESEWELVSEE--EVFEEDGYSYTFETYE 158
|
|
| FRB_dom |
pfam08771 |
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ... |
1347-1439 |
1.15e-55 |
|
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein FKBP12 can form a complex which specifically inhibits the TORC1 complex, leading to growth arrest. The FKBP12-rapamycin complex interferes with TORC1 function by binding to the FKBP12-rapamycin binding domain (FRB) of the TOR proteins. This entry represents the FRB domain.
Pssm-ID: 462596 Cd Length: 98 Bit Score: 188.56 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1347 SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLLQ 1426
Cdd:pfam08771 6 AILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDEEDLNQ 85
|
90
....*....|...
gi 1844115814 1427 AWDLYYHVFRRIS 1439
Cdd:pfam08771 86 AWDIYYSVFRRIK 98
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
1461-1564 |
3.26e-43 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 153.03 E-value: 3.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1461 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 1540
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115814 1541 YGATGHPGIIPPHATLVFDVELLK 1564
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
4-107 |
5.44e-42 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 149.56 E-value: 5.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 4 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 83
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115814 84 YGATGHPGIIPPHATLVFDVELLK 107
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
1471-1563 |
6.17e-42 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 149.27 E-value: 6.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1471 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 1549
Cdd:pfam00254 1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
|
90
....*....|....
gi 1844115814 1550 IPPHATLVFDVELL 1563
Cdd:pfam00254 81 IPPNATLVFEVELL 94
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
14-106 |
7.92e-41 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 145.80 E-value: 7.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 14 GRTFPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 92
Cdd:pfam00254 1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
|
90
....*....|....
gi 1844115814 93 IPPHATLVFDVELL 106
Cdd:pfam00254 81 IPPNATLVFEVELL 94
|
|
| FolA |
COG0262 |
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ... |
1038-1175 |
2.80e-37 |
|
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440032 [Multi-domain] Cd Length: 168 Bit Score: 138.83 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1038 ISLIAALAVDYVIGME-NAMPW--NLPADLAWFKRNTLN-KPVIMGRHTWESI-----GRPLPGRKNIILSSQP--STDD 1106
Cdd:COG0262 3 LILIVAVSLDGVIGGPdGDLPWlfPDPEDLAHFKELTAGaDAVLMGRKTYESIagywpTRPLPGRPKIVLSRTLdeADWE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844115814 1107 RVTWVK-SVDEAIAAC--GDVPEIMVIGGGRVIEQFLPK--AQKLYLTHIDAEV-EGDTHFPDY-EPDDWESVFSE 1175
Cdd:COG0262 83 GVTVVSgDLEEALAALkaAGGKDIWVIGGGELYRQLLPAglVDELYLTVVPVVLgEGDRLFPELdAPSRLELVESE 158
|
|
| Ribosomal_L7Ae |
pfam01248 |
Ribosomal protein L7Ae/L30e/S12e/Gadd45 family; This family includes: Ribosomal L7A from ... |
1728-1816 |
8.32e-35 |
|
Ribosomal protein L7Ae/L30e/S12e/Gadd45 family; This family includes: Ribosomal L7A from metazoa, Ribosomal L8-A and L8-B from fungi, 30S ribosomal protein HS6 from archaebacteria, 40S ribosomal protein S12 from eukaryotes, Ribosomal protein L30 from eukaryotes and archaebacteria. Gadd45 and MyD118.
Pssm-ID: 426153 [Multi-domain] Cd Length: 95 Bit Score: 128.87 E-value: 8.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1728 EALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCA 1807
Cdd:pfam01248 2 AIYEVLKKALKTGKLVLGLKEVTKALERGEAKLVIIAEDCDPEEKVKLIPALCKEKNVPYVKVPSKKELGEACGKKRPVS 81
|
....*....
gi 1844115814 1808 SAAIINEGE 1816
Cdd:pfam01248 82 ALAIKDEGD 90
|
|
| Rpl7Ae |
COG1358 |
Ribosomal protein L7Ae or related RNA K-turn-binding protein [Translation, ribosomal structure ... |
1727-1821 |
5.31e-34 |
|
Ribosomal protein L7Ae or related RNA K-turn-binding protein [Translation, ribosomal structure and biogenesis]; Ribosomal protein L7Ae or related RNA K-turn-binding protein is part of the Pathway/BioSystem: Ribosome 50S subunit
Pssm-ID: 440969 [Multi-domain] Cd Length: 98 Bit Score: 126.43 E-value: 5.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1727 NEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDpPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGiEVPC 1806
Cdd:COG1358 1 DKILNLLGLARRAGKLVSGEEQVLKAIRKGKAKLVIIAEDAS-ENTKKKLLDLCEEYGVPVVEVGTKEELGKAIG-KVGR 78
|
90
....*....|....*...
gi 1844115814 1807 ASAAIINEG---ELRKEL 1821
Cdd:COG1358 79 AVVAITDEGfakKLLELL 96
|
|
| SNU13 |
cd21104 |
U4/U6.U5 small nuclear ribonucleoprotein SNU13; U4/U6.U5 small nuclear ribonucleoprotein SNU13, ... |
1722-1831 |
2.50e-29 |
|
U4/U6.U5 small nuclear ribonucleoprotein SNU13; U4/U6.U5 small nuclear ribonucleoprotein SNU13, also known as NHP2-like protein 1 or U4/U6.U5 tri-snRNP 15.5 kDa protein, is a component of the spliceosome B complex, involved in pre-mRNA splicing. It binds to the 5'-stem-loop of U4 snRNA.
Pssm-ID: 411046 Cd Length: 122 Bit Score: 114.35 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1722 PEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVG 1801
Cdd:cd21104 9 DAQLTQTILDLVQQAANYKQLKKGANEATKTLNRGIAEFIVMAADAEPLEILLHLPLLCEDKNVPYVFVPSKQALGRACG 88
|
90 100 110
....*....|....*....|....*....|..
gi 1844115814 1802 IEVPCASAAII-NEG-ELRKELGSLVEKIKGL 1831
Cdd:cd21104 89 VSRPVIACSVTtNEGsQLKSQIQSLKDAIEKL 120
|
|
| dihyfolred_HdrA_Halo |
NF041386 |
dihydrofolate reductase HdrA; |
1041-1178 |
4.89e-29 |
|
dihydrofolate reductase HdrA;
Pssm-ID: 469277 [Multi-domain] Cd Length: 158 Bit Score: 114.67 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1041 IAALAVDYVIGMENAMPWN-LPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPST--DDRVTWVKSVDEA 1117
Cdd:NF041386 6 VAAVAENGVIGRDGELPWPsIPADKRQYRERVADDPVILGRRTFESMRDDLPGSAQIVLSRSEREfdVETAHHAGGVDEA 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844115814 1118 --IAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHD 1178
Cdd:NF041386 86 ieIAESLGAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYPEWDEDEWELVEETEYD 148
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
1462-1566 |
6.67e-25 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1462 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 1541
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
|
90 100
....*....|....*....|....*
gi 1844115814 1542 GATGHPGiIPPHATLVFDVELLKLE 1566
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1226-1339 |
6.27e-24 |
|
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses.
Pssm-ID: 279235 Cd Length: 243 Bit Score: 102.86 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1226 ESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNG--TLLVQSLHGVFKVKNTTTLQQHLIDG 1303
Cdd:pfam00863 4 KSIAKGLRDYHHIASNLAALEYYCGDHKGEIHGICHGDKIITPAHLFKEACGndTLKIQSKHGLFDLEALDRQKIEELCG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844115814 1304 RDMIIIRMPKDFPPFPQKLKFREPQREER----ICLVTTN 1339
Cdd:pfam00863 84 QDIIVIKGPIDMPPAKMRLIFRAPIQCERavliGCRRDDN 123
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
5-109 |
1.05e-23 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 5 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 84
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
|
90 100
....*....|....*....|....*..
gi 1844115814 85 GATGHPGiIPPHATLVFDVELL--KPE 109
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLdvKPA 251
|
|
| PRK13602 |
PRK13602 |
50S ribosomal protein L7ae-like protein; |
1734-1812 |
2.37e-18 |
|
50S ribosomal protein L7ae-like protein;
Pssm-ID: 184174 [Multi-domain] Cd Length: 82 Bit Score: 81.37 E-value: 2.37e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115814 1734 EKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPeIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAAII 1812
Cdd:PRK13602 4 EKVSQAKSIVIGTKQTVKALKRGSVKEVVVAEDADPR-LTEKVEALANEKGVPVSKVDSMKKLGKACGIEVGAAAVAII 81
|
|
| HCV_NS4a |
pfam01006 |
Hepatitis C virus non-structural protein NS4a; NS4a forms an integral part of the NS3 serine ... |
2095-2138 |
1.89e-17 |
|
Hepatitis C virus non-structural protein NS4a; NS4a forms an integral part of the NS3 serine protease, as it is required in a number of cases as a cofactor of cleavage. It has also been reported that NS4a interacts with NS4b and NS3 to form a multi-subunit replicase complex.
Pssm-ID: 366414 Cd Length: 55 Bit Score: 77.89 E-value: 1.89e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1844115814 2095 STWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPA--MPDREVLY 2138
Cdd:pfam01006 1 STWVLVGGALAAGAAYCLTTGSVVVVGRWSVNGKPPavVPDREVLY 46
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1580-1683 |
5.74e-14 |
|
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses.
Pssm-ID: 279235 Cd Length: 243 Bit Score: 73.97 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1580 DTSCTFPSS--DGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSAS----NFTNTN-NYFTSVPKNFMELLTNQE-AQQW 1651
Cdd:pfam00863 131 DESAIFPLGkeNGGFWKHGCDTKLGDCGGPIIACDDMDIIGFHGGRlmqlGANNSLaHIFAALNDDFIEMFAEMEtAKGF 210
|
90 100 110
....*....|....*....|....*....|..
gi 1844115814 1652 VSGWRLNADSVLWGGHKVFMVKPEEPFQPVKE 1683
Cdd:pfam00863 211 QRKWKFNADKVEWGRLDLTSNQPSGAFKIQKL 242
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
310-530 |
2.34e-10 |
|
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.
Pssm-ID: 461457 Cd Length: 375 Bit Score: 64.74 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 310 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 380
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 381 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 455
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 456 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 512
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
|
250 260
....*....|....*....|..
gi 1844115814 513 ----IGPQHQAGSDSLLTGMAF 530
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
753-973 |
2.34e-10 |
|
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.
Pssm-ID: 461457 Cd Length: 375 Bit Score: 64.74 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 753 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 823
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 824 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 898
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 899 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 955
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
|
250 260
....*....|....*....|..
gi 1844115814 956 ----IGPQHQAGSDSLLTGMAF 973
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
|
|
| TEL1 |
COG5032 |
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms]; |
1345-1441 |
2.62e-10 |
|
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
Pssm-ID: 227365 [Multi-domain] Cd Length: 2105 Bit Score: 66.34 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1345 SGSILWHEMWHEGLEEASRLYFGERN-VKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKD 1423
Cdd:COG5032 1630 IAYPLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISL 1709
|
90
....*....|....*...
gi 1844115814 1424 LLQAWDLYYHVFRRISKQ 1441
Cdd:COG5032 1710 LNLSRKLYISVLRSIRKR 1727
|
|
| trim_DfrL |
NF041668 |
trimethoprim-resistant dihydrofolate reductase DfrL; |
1050-1195 |
7.09e-08 |
|
trimethoprim-resistant dihydrofolate reductase DfrL;
Pssm-ID: 469550 [Multi-domain] Cd Length: 176 Bit Score: 54.28 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1050 IGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIG-RPLPGRKNIILSsqpstdDRVTWVKsvDEAIaacgdVPEIM 1128
Cdd:NF041668 30 FGNSGDDDVNLMGDKKHEKIPTMDDKNRIGIKLTENIPvRADGAIICHSKE------DNKNYLA--DGAI-----ECHIH 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844115814 1129 VIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR 1195
Cdd:NF041668 97 EDGGISAFEMFIDEPIHLHGGIIAEEFEGDEVMIEHDTIIDECFDGADGMPDEDNKYFHCFDIADGK 163
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| folA |
PRK10769 |
type 3 dihydrofolate reductase; |
1038-1195 |
1.77e-115 |
|
type 3 dihydrofolate reductase;
Pssm-ID: 182714 [Multi-domain] Cd Length: 159 Bit Score: 362.13 E-value: 1.77e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1038 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTDDRVTWVKSVDEA 1117
Cdd:PRK10769 2 ISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIVISSQPGTDDRVTWVKSVDEA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844115814 1118 IAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR 1195
Cdd:PRK10769 82 LAAAGDVPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYEPDEWESVFSEFHDADEQNSHSYCFEILERR 159
|
|
| POP2 |
COG5228 |
mRNA deadenylase subunit [RNA processing and modification]; |
292-571 |
2.31e-110 |
|
mRNA deadenylase subunit [RNA processing and modification];
Pssm-ID: 227553 Cd Length: 299 Bit Score: 353.84 E-value: 2.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 292 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 369
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 370 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 449
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 450 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 529
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115814 530 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 571
Cdd:COG5228 246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
|
|
| POP2 |
COG5228 |
mRNA deadenylase subunit [RNA processing and modification]; |
735-1014 |
2.31e-110 |
|
mRNA deadenylase subunit [RNA processing and modification];
Pssm-ID: 227553 Cd Length: 299 Bit Score: 353.84 E-value: 2.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 735 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 812
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 813 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 892
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 893 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 972
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115814 973 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 1014
Cdd:COG5228 246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
|
|
| Peptidase_S29 |
pfam02907 |
Hepatitis C virus NS3 protease; Hepatitis C virus NS3 protein is a serine protease which has a ... |
1906-2054 |
1.30e-87 |
|
Hepatitis C virus NS3 protease; Hepatitis C virus NS3 protein is a serine protease which has a trypsin-like fold. The non-structural (NS) protein NS3 is one of the NS proteins involved in replication of the HCV genome. NS2-3 proteinase, a zinc-dependent enzyme, performs a single proteolytic cut to release the N-terminus of NS3. The action of NS3 proteinase (NS3P), which resides in the N-terminal one-third of the NS3 protein, then yields all remaining non-structural proteins. The C-terminal two-thirds of the NS3 protein contain a helicase. The functional relationship between the proteinase and helicase domains is unknown. NS3 has a structural zinc-binding site and requires cofactor NS4A.
Pssm-ID: 427049 Cd Length: 149 Bit Score: 282.01 E-value: 1.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1906 EGEVQIVSTATQTFLATCINGVCWAVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTR 1985
Cdd:pfam02907 1 EGEVQVLGTATQRFMGTCVNGVLWTTFHGAGSRTLAGPKGPVNQMYWSASDDVVGYPLPPGAGSLTPCTCGATDLYLVTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115814 1986 HADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETT 2054
Cdd:pfam02907 81 DGDLIPGRRRGDPRVSLLSPRPLSYLKGSSGGPILCPSGHVVGMFRAAVHSGGVVKAVRFVPWETLPTT 149
|
|
| cp |
PHA00026 |
coat protein |
160-288 |
1.46e-85 |
|
coat protein
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 160 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 239
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115814 240 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 288
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| cp |
PHA00026 |
coat protein |
603-731 |
1.46e-85 |
|
coat protein
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 603 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 682
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115814 683 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 731
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| DHFR_1 |
pfam00186 |
Dihydrofolate reductase; |
1038-1194 |
1.67e-77 |
|
Dihydrofolate reductase;
Pssm-ID: 425512 [Multi-domain] Cd Length: 159 Bit Score: 253.62 E-value: 1.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1038 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTD-DRVTWVKSVDE 1116
Cdd:pfam00186 2 ISLIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGRPLPGRKNIVLTRNPDYKvDGVEVVHSLEE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844115814 1117 AIAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILER 1194
Cdd:pfam00186 82 ALALAAEAEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPEIDPSEWQLVSREEHEADEKNPYPYTFVTYER 159
|
|
| Levi_coat |
pfam01819 |
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ... |
161-287 |
1.55e-69 |
|
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that encapsidates the viral RNA. 180 copies of this protein form the virion shell. The MS2 bacteriophage coat protein controls two distinct processes: sequence-specific RNA encapsidation and repression of replicase translation-by binding to an RNA stem-loop structure of 19 nucleotides containing the initiation codon of the replicase gene. The binding of a coat protein dimer to this hairpin shuts off synthesis of the viral replicase, switching the viral replication cycle to virion assembly rather than continued replication.
Pssm-ID: 396403 Cd Length: 132 Bit Score: 229.62 E-value: 1.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 161 SNFTQFVLVDNGGTGDVTVAPS----NFANGVAEWISSNSRSQAYK-VTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVE 235
Cdd:pfam01819 1 AKFQAFTLSDIGGNGDVTLALNprgvNFANGVAALIEAGARPAAEKrVTCSVRQPSANNKKYKIKVEIPKPASCTAGGTC 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1844115814 236 LPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGI 287
Cdd:pfam01819 81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
|
|
| Levi_coat |
pfam01819 |
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ... |
604-730 |
1.55e-69 |
|
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that encapsidates the viral RNA. 180 copies of this protein form the virion shell. The MS2 bacteriophage coat protein controls two distinct processes: sequence-specific RNA encapsidation and repression of replicase translation-by binding to an RNA stem-loop structure of 19 nucleotides containing the initiation codon of the replicase gene. The binding of a coat protein dimer to this hairpin shuts off synthesis of the viral replicase, switching the viral replication cycle to virion assembly rather than continued replication.
Pssm-ID: 396403 Cd Length: 132 Bit Score: 229.62 E-value: 1.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 604 SNFTQFVLVDNGGTGDVTVAPS----NFANGVAEWISSNSRSQAYK-VTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVE 678
Cdd:pfam01819 1 AKFQAFTLSDIGGNGDVTLALNprgvNFANGVAALIEAGARPAAEKrVTCSVRQPSANNKKYKIKVEIPKPASCTAGGTC 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1844115814 679 LPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGI 730
Cdd:pfam01819 81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
|
|
| eL8_ribo |
TIGR03677 |
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version ... |
1716-1832 |
8.50e-69 |
|
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version of the large ribosomal complex protein eL8, previously designated L8 in yeast and L7Ae in the archaea. The family is a narrower version of the pfam01248 model which also recognizes the L30 protein.
Pssm-ID: 188367 [Multi-domain] Cd Length: 117 Bit Score: 226.95 E-value: 8.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1716 YVRFEVPEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKND 1795
Cdd:TIGR03677 1 YVKFEVPEELADKALEAVEKARETGKIKKGTNEVTKAVERGIAKLVVIAEDVEPPEIVAHLPALCEEKGIPYIYVKSKED 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844115814 1796 LGRAVGIEVPCASAAIINEGELRKELGSLVEKIKGLQ 1832
Cdd:TIGR03677 81 LGAAAGLEVGAASAAIVDAGKAEELLKEIIEKVEALK 117
|
|
| DHFR |
cd00209 |
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ... |
1038-1193 |
1.48e-65 |
|
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.
Pssm-ID: 238127 [Multi-domain] Cd Length: 158 Bit Score: 219.32 E-value: 1.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1038 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIG-RPLPGRKNIILSSQPST--DDRVTWVKSV 1114
Cdd:cd00209 1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrRPLPGRTNIVLSRQLDYqdAEGVEVVHSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1115 DEAIAACG-DVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEfhDADAQNSHSYCFEILE 1193
Cdd:cd00209 81 EEALELAEnTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIDESEWELVSEE--EVFEEDGYSYTFETYE 158
|
|
| FRB_dom |
pfam08771 |
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ... |
1347-1439 |
1.15e-55 |
|
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein FKBP12 can form a complex which specifically inhibits the TORC1 complex, leading to growth arrest. The FKBP12-rapamycin complex interferes with TORC1 function by binding to the FKBP12-rapamycin binding domain (FRB) of the TOR proteins. This entry represents the FRB domain.
Pssm-ID: 462596 Cd Length: 98 Bit Score: 188.56 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1347 SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLLQ 1426
Cdd:pfam08771 6 AILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDEEDLNQ 85
|
90
....*....|...
gi 1844115814 1427 AWDLYYHVFRRIS 1439
Cdd:pfam08771 86 AWDIYYSVFRRIK 98
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
1461-1564 |
3.26e-43 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 153.03 E-value: 3.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1461 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 1540
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115814 1541 YGATGHPGIIPPHATLVFDVELLK 1564
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
4-107 |
5.44e-42 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 149.56 E-value: 5.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 4 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 83
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115814 84 YGATGHPGIIPPHATLVFDVELLK 107
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
1471-1563 |
6.17e-42 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 149.27 E-value: 6.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1471 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 1549
Cdd:pfam00254 1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
|
90
....*....|....
gi 1844115814 1550 IPPHATLVFDVELL 1563
Cdd:pfam00254 81 IPPNATLVFEVELL 94
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
14-106 |
7.92e-41 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 145.80 E-value: 7.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 14 GRTFPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 92
Cdd:pfam00254 1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
|
90
....*....|....
gi 1844115814 93 IPPHATLVFDVELL 106
Cdd:pfam00254 81 IPPNATLVFEVELL 94
|
|
| FolA |
COG0262 |
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ... |
1038-1175 |
2.80e-37 |
|
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440032 [Multi-domain] Cd Length: 168 Bit Score: 138.83 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1038 ISLIAALAVDYVIGME-NAMPW--NLPADLAWFKRNTLN-KPVIMGRHTWESI-----GRPLPGRKNIILSSQP--STDD 1106
Cdd:COG0262 3 LILIVAVSLDGVIGGPdGDLPWlfPDPEDLAHFKELTAGaDAVLMGRKTYESIagywpTRPLPGRPKIVLSRTLdeADWE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844115814 1107 RVTWVK-SVDEAIAAC--GDVPEIMVIGGGRVIEQFLPK--AQKLYLTHIDAEV-EGDTHFPDY-EPDDWESVFSE 1175
Cdd:COG0262 83 GVTVVSgDLEEALAALkaAGGKDIWVIGGGELYRQLLPAglVDELYLTVVPVVLgEGDRLFPELdAPSRLELVESE 158
|
|
| Ribosomal_L7Ae |
pfam01248 |
Ribosomal protein L7Ae/L30e/S12e/Gadd45 family; This family includes: Ribosomal L7A from ... |
1728-1816 |
8.32e-35 |
|
Ribosomal protein L7Ae/L30e/S12e/Gadd45 family; This family includes: Ribosomal L7A from metazoa, Ribosomal L8-A and L8-B from fungi, 30S ribosomal protein HS6 from archaebacteria, 40S ribosomal protein S12 from eukaryotes, Ribosomal protein L30 from eukaryotes and archaebacteria. Gadd45 and MyD118.
Pssm-ID: 426153 [Multi-domain] Cd Length: 95 Bit Score: 128.87 E-value: 8.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1728 EALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCA 1807
Cdd:pfam01248 2 AIYEVLKKALKTGKLVLGLKEVTKALERGEAKLVIIAEDCDPEEKVKLIPALCKEKNVPYVKVPSKKELGEACGKKRPVS 81
|
....*....
gi 1844115814 1808 SAAIINEGE 1816
Cdd:pfam01248 82 ALAIKDEGD 90
|
|
| Rpl7Ae |
COG1358 |
Ribosomal protein L7Ae or related RNA K-turn-binding protein [Translation, ribosomal structure ... |
1727-1821 |
5.31e-34 |
|
Ribosomal protein L7Ae or related RNA K-turn-binding protein [Translation, ribosomal structure and biogenesis]; Ribosomal protein L7Ae or related RNA K-turn-binding protein is part of the Pathway/BioSystem: Ribosome 50S subunit
Pssm-ID: 440969 [Multi-domain] Cd Length: 98 Bit Score: 126.43 E-value: 5.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1727 NEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDpPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGiEVPC 1806
Cdd:COG1358 1 DKILNLLGLARRAGKLVSGEEQVLKAIRKGKAKLVIIAEDAS-ENTKKKLLDLCEEYGVPVVEVGTKEELGKAIG-KVGR 78
|
90
....*....|....*...
gi 1844115814 1807 ASAAIINEG---ELRKEL 1821
Cdd:COG1358 79 AVVAITDEGfakKLLELL 96
|
|
| SNU13 |
cd21104 |
U4/U6.U5 small nuclear ribonucleoprotein SNU13; U4/U6.U5 small nuclear ribonucleoprotein SNU13, ... |
1722-1831 |
2.50e-29 |
|
U4/U6.U5 small nuclear ribonucleoprotein SNU13; U4/U6.U5 small nuclear ribonucleoprotein SNU13, also known as NHP2-like protein 1 or U4/U6.U5 tri-snRNP 15.5 kDa protein, is a component of the spliceosome B complex, involved in pre-mRNA splicing. It binds to the 5'-stem-loop of U4 snRNA.
Pssm-ID: 411046 Cd Length: 122 Bit Score: 114.35 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1722 PEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVG 1801
Cdd:cd21104 9 DAQLTQTILDLVQQAANYKQLKKGANEATKTLNRGIAEFIVMAADAEPLEILLHLPLLCEDKNVPYVFVPSKQALGRACG 88
|
90 100 110
....*....|....*....|....*....|..
gi 1844115814 1802 IEVPCASAAII-NEG-ELRKELGSLVEKIKGL 1831
Cdd:cd21104 89 VSRPVIACSVTtNEGsQLKSQIQSLKDAIEKL 120
|
|
| dihyfolred_HdrA_Halo |
NF041386 |
dihydrofolate reductase HdrA; |
1041-1178 |
4.89e-29 |
|
dihydrofolate reductase HdrA;
Pssm-ID: 469277 [Multi-domain] Cd Length: 158 Bit Score: 114.67 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1041 IAALAVDYVIGMENAMPWN-LPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPST--DDRVTWVKSVDEA 1117
Cdd:NF041386 6 VAAVAENGVIGRDGELPWPsIPADKRQYRERVADDPVILGRRTFESMRDDLPGSAQIVLSRSEREfdVETAHHAGGVDEA 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844115814 1118 --IAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHD 1178
Cdd:NF041386 86 ieIAESLGAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYPEWDEDEWELVEETEYD 148
|
|
| PTZ00164 |
PTZ00164 |
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional |
1033-1229 |
2.11e-25 |
|
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
Pssm-ID: 240299 [Multi-domain] Cd Length: 514 Bit Score: 112.84 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1033 SGSGSISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKP-------------VIMGRHTWESIG---RPLPGRKNI 1096
Cdd:PTZ00164 5 SSLKDFSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYVReekyekspkkqnaVIMGRKTWESIPkkfRPLKNRINV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1097 ILSS---QPSTDDRVTWVKSVDEAIAACGDVP---EIMVIGGGRVIEQFLP--KAQKLYLTHIDAEVEGDTHFPDYePDD 1168
Cdd:PTZ00164 85 VLSRtltEEEADPGVLVFGSLEDALRLLAEDLsieKIFIIGGASVYREALSanLLDKIYLTRVNSEYECDVFFPKI-PES 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844115814 1169 WESVFSEFHDADAQNShSYCFEILERRGSAVKQTL--NFDLLKLAGDVESNPGPMGRSGESLF 1229
Cdd:PTZ00164 164 FFIVAIVSQTFSTNGT-SYDFVIYEKKNDDEEDLLgkIFGQMKMTGRKKSPKEQLYKACPSLK 225
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
1462-1566 |
6.67e-25 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1462 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 1541
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
|
90 100
....*....|....*....|....*
gi 1844115814 1542 GATGHPGiIPPHATLVFDVELLKLE 1566
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1226-1339 |
6.27e-24 |
|
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses.
Pssm-ID: 279235 Cd Length: 243 Bit Score: 102.86 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1226 ESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNG--TLLVQSLHGVFKVKNTTTLQQHLIDG 1303
Cdd:pfam00863 4 KSIAKGLRDYHHIASNLAALEYYCGDHKGEIHGICHGDKIITPAHLFKEACGndTLKIQSKHGLFDLEALDRQKIEELCG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844115814 1304 RDMIIIRMPKDFPPFPQKLKFREPQREER----ICLVTTN 1339
Cdd:pfam00863 84 QDIIVIKGPIDMPPAKMRLIFRAPIQCERavliGCRRDDN 123
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
5-109 |
1.05e-23 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 5 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 84
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
|
90 100
....*....|....*....|....*..
gi 1844115814 85 GATGHPGiIPPHATLVFDVELL--KPE 109
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLdvKPA 251
|
|
| PRK11570 |
PRK11570 |
peptidyl-prolyl cis-trans isomerase; Provisional |
1460-1565 |
1.44e-20 |
|
peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 183207 [Multi-domain] Cd Length: 206 Bit Score: 92.17 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1460 GVQVETISPGDGrTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKqeVIRGWEEGVAQMSVGQRAKLTISPDY 1539
Cdd:PRK11570 103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
|
90 100
....*....|....*....|....*.
gi 1844115814 1540 AYGATGHPGIIPPHATLVFDVELLKL 1565
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELLEI 205
|
|
| PRK11570 |
PRK11570 |
peptidyl-prolyl cis-trans isomerase; Provisional |
3-106 |
3.33e-19 |
|
peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 183207 [Multi-domain] Cd Length: 206 Bit Score: 87.93 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 3 GVQVETISPGDGrTFPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKqeVIRGWEEGVAQMSVGQRAKLTISPDY 82
Cdd:PRK11570 103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
|
90 100
....*....|....*....|....
gi 1844115814 83 AYGATGHPGIIPPHATLVFDVELL 106
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELL 203
|
|
| PRK13602 |
PRK13602 |
50S ribosomal protein L7ae-like protein; |
1734-1812 |
2.37e-18 |
|
50S ribosomal protein L7ae-like protein;
Pssm-ID: 184174 [Multi-domain] Cd Length: 82 Bit Score: 81.37 E-value: 2.37e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115814 1734 EKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPeIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAAII 1812
Cdd:PRK13602 4 EKVSQAKSIVIGTKQTVKALKRGSVKEVVVAEDADPR-LTEKVEALANEKGVPVSKVDSMKKLGKACGIEVGAAAVAII 81
|
|
| HCV_NS4a |
pfam01006 |
Hepatitis C virus non-structural protein NS4a; NS4a forms an integral part of the NS3 serine ... |
2095-2138 |
1.89e-17 |
|
Hepatitis C virus non-structural protein NS4a; NS4a forms an integral part of the NS3 serine protease, as it is required in a number of cases as a cofactor of cleavage. It has also been reported that NS4a interacts with NS4b and NS3 to form a multi-subunit replicase complex.
Pssm-ID: 366414 Cd Length: 55 Bit Score: 77.89 E-value: 1.89e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1844115814 2095 STWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPA--MPDREVLY 2138
Cdd:pfam01006 1 STWVLVGGALAAGAAYCLTTGSVVVVGRWSVNGKPPavVPDREVLY 46
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1580-1683 |
5.74e-14 |
|
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses.
Pssm-ID: 279235 Cd Length: 243 Bit Score: 73.97 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1580 DTSCTFPSS--DGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSAS----NFTNTN-NYFTSVPKNFMELLTNQE-AQQW 1651
Cdd:pfam00863 131 DESAIFPLGkeNGGFWKHGCDTKLGDCGGPIIACDDMDIIGFHGGRlmqlGANNSLaHIFAALNDDFIEMFAEMEtAKGF 210
|
90 100 110
....*....|....*....|....*....|..
gi 1844115814 1652 VSGWRLNADSVLWGGHKVFMVKPEEPFQPVKE 1683
Cdd:pfam00863 211 QRKWKFNADKVEWGRLDLTSNQPSGAFKIQKL 242
|
|
| PTZ00365 |
PTZ00365 |
60S ribosomal protein L7Ae-like; Provisional |
1742-1820 |
3.48e-13 |
|
60S ribosomal protein L7Ae-like; Provisional
Pssm-ID: 240382 Cd Length: 266 Bit Score: 71.80 E-value: 3.48e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115814 1742 VKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGiEVPCASAAIINegeLRKE 1820
Cdd:PTZ00365 133 LKYGLNHVTDLVEYKKAKLVVIAHDVDPIELVCFLPALCRKKEVPYCIIKGKSRLGKLVH-QKTAAVVAIDN---VRKE 207
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
1476-1562 |
4.17e-12 |
|
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440668 [Multi-domain] Cd Length: 138 Bit Score: 65.51 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1476 KRGQTCVVHYTGMLEDGKKFDSSRDRnKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGatghpgiiPPHAT 1555
Cdd:COG1047 2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPE 72
|
....*..
gi 1844115814 1556 LVFDVEL 1562
Cdd:COG1047 73 LVQTVPR 79
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
19-105 |
8.69e-12 |
|
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440668 [Multi-domain] Cd Length: 138 Bit Score: 64.74 E-value: 8.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 19 KRGQTCVVHYTGMLEDGKKVDSSRDRnKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGatghpgiiPPHAT 98
Cdd:COG1047 2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPE 72
|
....*..
gi 1844115814 99 LVFDVEL 105
Cdd:COG1047 73 LVQTVPR 79
|
|
| PTZ00222 |
PTZ00222 |
60S ribosomal protein L7a; Provisional |
1742-1801 |
1.57e-10 |
|
60S ribosomal protein L7a; Provisional
Pssm-ID: 140249 Cd Length: 263 Bit Score: 63.95 E-value: 1.57e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1742 VKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVG 1801
Cdd:PTZ00222 133 VVTGLQEVTRAIEKKQARMVVIANNVDPVELVLWMPNLCRANKIPYAIVKDMARLGDAIG 192
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
310-530 |
2.34e-10 |
|
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.
Pssm-ID: 461457 Cd Length: 375 Bit Score: 64.74 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 310 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 380
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 381 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 455
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 456 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 512
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
|
250 260
....*....|....*....|..
gi 1844115814 513 ----IGPQHQAGSDSLLTGMAF 530
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
753-973 |
2.34e-10 |
|
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.
Pssm-ID: 461457 Cd Length: 375 Bit Score: 64.74 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 753 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 823
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 824 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 898
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 899 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 955
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
|
250 260
....*....|....*....|..
gi 1844115814 956 ----IGPQHQAGSDSLLTGMAF 973
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
|
|
| TEL1 |
COG5032 |
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms]; |
1345-1441 |
2.62e-10 |
|
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
Pssm-ID: 227365 [Multi-domain] Cd Length: 2105 Bit Score: 66.34 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1345 SGSILWHEMWHEGLEEASRLYFGERN-VKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKD 1423
Cdd:COG5032 1630 IAYPLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISL 1709
|
90
....*....|....*...
gi 1844115814 1424 LLQAWDLYYHVFRRISKQ 1441
Cdd:COG5032 1710 LNLSRKLYISVLRSIRKR 1727
|
|
| RPL30E |
COG1911 |
Ribosomal protein L30E [Translation, ribosomal structure and biogenesis]; Ribosomal protein ... |
1733-1816 |
3.17e-10 |
|
Ribosomal protein L30E [Translation, ribosomal structure and biogenesis]; Ribosomal protein L30E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
Pssm-ID: 441515 [Multi-domain] Cd Length: 97 Bit Score: 58.68 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1733 LEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVdPPEIVAHLPLLCEEKNVP-YIYVKSKNDLGRAVGIEVPCASAAI 1811
Cdd:COG1911 8 LRDAVKTGKVVLGSKQTIKAIKLGKAKLVILAANC-PPEIREDIEYYAKLSNVPvYVYPGTSVELGALCGKPFRVSALAI 86
|
....*
gi 1844115814 1812 INEGE 1816
Cdd:COG1911 87 IDPGE 91
|
|
| PRK01018 |
PRK01018 |
50S ribosomal protein L30e; Reviewed |
1733-1816 |
5.79e-08 |
|
50S ribosomal protein L30e; Reviewed
Pssm-ID: 179205 [Multi-domain] Cd Length: 99 Bit Score: 52.27 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1733 LEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVdPPEIVAHLPLLCEEKNVP-YIYVKSKNDLGRAVGIEVPCASAAI 1811
Cdd:PRK01018 8 LRVAVDTGKVILGSKRTIKAIKLGKAKLVIVASNC-PKDIKEDIEYYAKLSGIPvYEYEGSSVELGTLCGKPFTVSALAI 86
|
....*
gi 1844115814 1812 INEGE 1816
Cdd:PRK01018 87 VDPGE 91
|
|
| trim_DfrL |
NF041668 |
trimethoprim-resistant dihydrofolate reductase DfrL; |
1050-1195 |
7.09e-08 |
|
trimethoprim-resistant dihydrofolate reductase DfrL;
Pssm-ID: 469550 [Multi-domain] Cd Length: 176 Bit Score: 54.28 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1050 IGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIG-RPLPGRKNIILSsqpstdDRVTWVKsvDEAIaacgdVPEIM 1128
Cdd:NF041668 30 FGNSGDDDVNLMGDKKHEKIPTMDDKNRIGIKLTENIPvRADGAIICHSKE------DNKNYLA--DGAI-----ECHIH 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844115814 1129 VIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR 1195
Cdd:NF041668 97 EDGGISAFEMFIDEPIHLHGGIIAEEFEGDEVMIEHDTIIDECFDGADGMPDEDNKYFHCFDIADGK 163
|
|
| scpA |
PRK00478 |
segregation and condensation protein ScpA; |
1038-1161 |
1.25e-07 |
|
segregation and condensation protein ScpA;
Pssm-ID: 234776 [Multi-domain] Cd Length: 505 Bit Score: 56.86 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1038 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTD----DRVTWVKS 1113
Cdd:PRK00478 2 IKLIWCEDLNFGIAKNNQIPWKIDEELNHFHQTTTNHTIVMGYNTFQAMNKILANQANIVISKKHQRElknnNELFVFND 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1844115814 1114 VDEAIAACGDVpEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHF 1161
Cdd:PRK00478 82 LKKLLIDFSNV-DLFIIGGKKTIEQFIKYADQLIISKLNADYKCDLFV 128
|
|
| PRK13601 |
PRK13601 |
putative L7Ae-like ribosomal protein; Provisional |
1745-1814 |
3.90e-07 |
|
putative L7Ae-like ribosomal protein; Provisional
Pssm-ID: 184173 Cd Length: 82 Bit Score: 49.59 E-value: 3.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844115814 1745 GTNETTKAVERGLAKLVYIAEDVDPpEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAA-IINE 1814
Cdd:PRK13601 12 GAKQTLKAITNCNVLQVYIAKDAEE-HVTKKIKELCEEKSIKIVYIDTMKELGVMCGIDVGAAAAAdIIGE 81
|
|
| PRK15095 |
PRK15095 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
26-85 |
3.87e-06 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 237908 [Multi-domain] Cd Length: 156 Bit Score: 48.94 E-value: 3.87e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 26 VHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYG 85
Cdd:PRK15095 13 VHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG 72
|
|
| PRK15095 |
PRK15095 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
1483-1542 |
7.68e-06 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 237908 [Multi-domain] Cd Length: 156 Bit Score: 48.16 E-value: 7.68e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1483 VHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYG 1542
Cdd:PRK15095 13 VHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG 72
|
|
| PRK06683 |
PRK06683 |
hypothetical protein; Provisional |
1734-1813 |
2.16e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 136002 Cd Length: 82 Bit Score: 44.68 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1734 EKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDP--PEIVAHLPLlceEKNVPYIYVKSKNDLGRAVGIEVPCASAAI 1811
Cdd:PRK06683 4 QKVSNAENVVVGHKRTLEAIKNGIVKEVVIAEDADMrlTHVIIRTAL---QHNIPITKVESVRKLGKVAGIQVGASAIGI 80
|
..
gi 1844115814 1812 IN 1813
Cdd:PRK06683 81 IS 82
|
|
| PRK07714 |
PRK07714 |
YlxQ family RNA-binding protein; |
1726-1819 |
2.33e-05 |
|
YlxQ family RNA-binding protein;
Pssm-ID: 236077 Cd Length: 100 Bit Score: 45.15 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1726 QNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDpPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVP 1805
Cdd:PRK07714 3 MSDWKSFLGLANRARKVISGEELVLKEVRSGKAKLVLLSEDAS-VNTTKKITDKCTYYNVPMRKVENRQQLGHAIGKDER 81
|
90
....*....|....
gi 1844115814 1806 CAsAAIINEGELRK 1819
Cdd:PRK07714 82 VV-VAVLDEGFAKK 94
|
|
| PTZ00106 |
PTZ00106 |
60S ribosomal protein L30; Provisional |
1733-1816 |
1.57e-04 |
|
60S ribosomal protein L30; Provisional
Pssm-ID: 185450 Cd Length: 108 Bit Score: 43.14 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1733 LEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVdPP------EIVAHLpllceEKNVPYIYVKSKNDLGRAVGIEVPC 1806
Cdd:PTZ00106 17 LQLVMKSGKYTLGTKSTLKALRNGKAKLVIISNNC-PPirrseiEYYAML-----SKTGVHHYAGNNNDLGTACGRHFRV 90
|
90
....*....|
gi 1844115814 1807 ASAAIINEGE 1816
Cdd:PTZ00106 91 SVMSITDAGD 100
|
|
| PRK13600 |
PRK13600 |
putative ribosomal protein L7Ae-like; Provisional |
1745-1813 |
6.10e-04 |
|
putative ribosomal protein L7Ae-like; Provisional
Pssm-ID: 184172 Cd Length: 84 Bit Score: 40.60 E-value: 6.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115814 1745 GTNETTKAVERGLAKLVYIAEDVDPpEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAAIIN 1813
Cdd:PRK13600 17 GLKETLKALKKDQVTSLIIAEDVEV-YLMTRVLSQINQKNIPVSFFKSKHALGKHVGINVNATIVALIK 84
|
|
| PRK05583 |
PRK05583 |
ribosomal protein L7Ae family protein; Provisional |
1725-1801 |
1.24e-03 |
|
ribosomal protein L7Ae family protein; Provisional
Pssm-ID: 235517 Cd Length: 104 Bit Score: 40.42 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115814 1725 MQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDP---PEIVAHlpllCEEKNVPYIYVKSKNDLGRAVG 1801
Cdd:PRK05583 1 MMNKFLNFLGLTKKAGKLLEGYNKCEEAIKKKKVYLIIISNDISEnskNKFKNY----CNKYNIPYIEGYSKEELGNAIG 76
|
|
| |
