|
Name |
Accession |
Description |
Interval |
E-value |
| folA |
PRK10769 |
type 3 dihydrofolate reductase; |
1060-1217 |
1.58e-115 |
|
type 3 dihydrofolate reductase;
:
Pssm-ID: 182714 [Multi-domain] Cd Length: 159 Bit Score: 362.52 E-value: 1.58e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1060 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTDDRVTWVKSVDEA 1139
Cdd:PRK10769 2 ISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIVISSQPGTDDRVTWVKSVDEA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844115818 1140 IAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR 1217
Cdd:PRK10769 82 LAAAGDVPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYEPDEWESVFSEFHDADEQNSHSYCFEILERR 159
|
|
| CAF1 super family |
cl23804 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
303-582 |
3.07e-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: 353.46 E-value: 3.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 303 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 380
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 381 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 460
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 461 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 540
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115818 541 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 582
Cdd:COG5228 246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
|
|
| CAF1 super family |
cl23804 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
757-1036 |
3.07e-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: 353.46 E-value: 3.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 757 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 834
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 835 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 914
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 915 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 994
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115818 995 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 1036
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 ... |
1928-2076 |
1.32e-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: 1.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1928 EGEVQIVSTATQTFLATCINGVCWAVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTR 2007
Cdd:pfam02907 1 EGEVQVLGTATQRFMGTCVNGVLWTTFHGAGSRTLAGPKGPVNQMYWSASDDVVGYPLPPGAGSLTPCTCGATDLYLVTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115818 2008 HADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETT 2076
Cdd:pfam02907 81 DGDLIPGRRRGDPRVSLLSPRPLSYLKGSSGGPILCPSGHVVGMFRAAVHSGGVVKAVRFVPWETLPTT 149
|
|
| cp |
PHA00026 |
coat protein |
160-288 |
1.48e-85 |
|
coat protein
:
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 160 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 239
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115818 240 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 288
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| cp |
PHA00026 |
coat protein |
614-742 |
1.48e-85 |
|
coat protein
:
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 614 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 693
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115818 694 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 742
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| eL8_ribo |
TIGR03677 |
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version ... |
1738-1854 |
8.59e-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: 8.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1738 YVRFEVPEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKND 1817
Cdd:TIGR03677 1 YVKFEVPEELADKALEAVEKARETGKIKKGTNEVTKAVERGIAKLVVIAEDVEPPEIVAHLPALCEEKGIPYIYVKSKED 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844115818 1818 LGRAVGIEVPCASAAIINEGELRKELGSLVEKIKGLQ 1854
Cdd:TIGR03677 81 LGAAAGLEVGAASAAIVDAGKAEELLKEIIEKVEALK 117
|
|
| FRB_dom |
pfam08771 |
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ... |
1369-1461 |
1.16e-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: 1.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1369 SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLLQ 1448
Cdd:pfam08771 6 AILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDEEDLNQ 85
|
90
....*....|...
gi 1844115818 1449 AWDLYYHVFRRIS 1461
Cdd:pfam08771 86 AWDIYYSVFRRIK 98
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
1483-1586 |
3.46e-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: 3.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1483 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 1562
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115818 1563 YGATGHPGIIPPHATLVFDVELLK 1586
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
4-107 |
5.77e-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: 5.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 4 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 83
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115818 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. |
1248-1361 |
6.34e-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: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1248 ESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNG--TLLVQSLHGVFKVKNTTTLQQHLIDG 1325
Cdd:pfam00863 4 KSIAKGLRDYHHIASNLAALEYYCGDHKGEIHGICHGDKIITPAHLFKEACGndTLKIQSKHGLFDLEALDRQKIEELCG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844115818 1326 RDMIIIRMPKDFPPFPQKLKFREPQREER----ICLVTTN 1361
Cdd:pfam00863 84 QDIIVIKGPIDMPPAKMRLIFRAPIQCERavliGCRRDDN 123
|
|
| HCV_NS4a |
pfam01006 |
Hepatitis C virus non-structural protein NS4a; NS4a forms an integral part of the NS3 serine ... |
2117-2160 |
1.86e-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: 1.86e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1844115818 2117 STWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPA--MPDREVLY 2160
Cdd:pfam01006 1 STWVLVGGALAAGAAYCLTTGSVVVVGRWSVNGKPPavVPDREVLY 46
|
|
| Peptidase_C4 super family |
cl24133 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1602-1705 |
5.80e-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: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1602 DTSCTFPSS--DGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSAS----NFTNTN-NYFTSVPKNFMELLTNQE-AQQW 1673
Cdd:pfam00863 131 DESAIFPLGkeNGGFWKHGCDTKLGDCGGPIIACDDMDIIGFHGGRlmqlGANNSLaHIFAALNDDFIEMFAEMEtAKGF 210
|
90 100 110
....*....|....*....|....*....|..
gi 1844115818 1674 VSGWRLNADSVLWGGHKVFMVKPEEPFQPVKE 1705
Cdd:pfam00863 211 QRKWKFNADKVEWGRLDLTSNQPSGAFKIQKL 242
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| folA |
PRK10769 |
type 3 dihydrofolate reductase; |
1060-1217 |
1.58e-115 |
|
type 3 dihydrofolate reductase;
Pssm-ID: 182714 [Multi-domain] Cd Length: 159 Bit Score: 362.52 E-value: 1.58e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1060 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTDDRVTWVKSVDEA 1139
Cdd:PRK10769 2 ISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIVISSQPGTDDRVTWVKSVDEA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844115818 1140 IAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR 1217
Cdd:PRK10769 82 LAAAGDVPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYEPDEWESVFSEFHDADEQNSHSYCFEILERR 159
|
|
| POP2 |
COG5228 |
mRNA deadenylase subunit [RNA processing and modification]; |
303-582 |
3.07e-110 |
|
mRNA deadenylase subunit [RNA processing and modification];
Pssm-ID: 227553 Cd Length: 299 Bit Score: 353.46 E-value: 3.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 303 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 380
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 381 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 460
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 461 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 540
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115818 541 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 582
Cdd:COG5228 246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
|
|
| POP2 |
COG5228 |
mRNA deadenylase subunit [RNA processing and modification]; |
757-1036 |
3.07e-110 |
|
mRNA deadenylase subunit [RNA processing and modification];
Pssm-ID: 227553 Cd Length: 299 Bit Score: 353.46 E-value: 3.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 757 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 834
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 835 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 914
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 915 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 994
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115818 995 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 1036
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 ... |
1928-2076 |
1.32e-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: 1.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1928 EGEVQIVSTATQTFLATCINGVCWAVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTR 2007
Cdd:pfam02907 1 EGEVQVLGTATQRFMGTCVNGVLWTTFHGAGSRTLAGPKGPVNQMYWSASDDVVGYPLPPGAGSLTPCTCGATDLYLVTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115818 2008 HADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETT 2076
Cdd:pfam02907 81 DGDLIPGRRRGDPRVSLLSPRPLSYLKGSSGGPILCPSGHVVGMFRAAVHSGGVVKAVRFVPWETLPTT 149
|
|
| cp |
PHA00026 |
coat protein |
160-288 |
1.48e-85 |
|
coat protein
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 160 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 239
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115818 240 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 288
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| cp |
PHA00026 |
coat protein |
614-742 |
1.48e-85 |
|
coat protein
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 614 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 693
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115818 694 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 742
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| DHFR_1 |
pfam00186 |
Dihydrofolate reductase; |
1060-1216 |
1.69e-77 |
|
Dihydrofolate reductase;
Pssm-ID: 425512 [Multi-domain] Cd Length: 159 Bit Score: 253.62 E-value: 1.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1060 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTD-DRVTWVKSVDE 1138
Cdd:pfam00186 2 ISLIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGRPLPGRKNIVLTRNPDYKvDGVEVVHSLEE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844115818 1139 AIAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILER 1216
Cdd:pfam00186 82 ALALAAEAEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPEIDPSEWQLVSREEHEADEKNPYPYTFVTYER 159
|
|
| Levi_coat |
pfam01819 |
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ... |
161-287 |
1.56e-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: 1.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 161 SNFTQFVLVDNGGTGDVTVAPS----NFANGVAEWISSNSRSQAYK-VTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVE 235
Cdd:pfam01819 1 AKFQAFTLSDIGGNGDVTLALNprgvNFANGVAALIEAGARPAAEKrVTCSVRQPSANNKKYKIKVEIPKPASCTAGGTC 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1844115818 236 LPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGI 287
Cdd:pfam01819 81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
|
|
| Levi_coat |
pfam01819 |
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ... |
615-741 |
1.56e-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: 1.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 615 SNFTQFVLVDNGGTGDVTVAPS----NFANGVAEWISSNSRSQAYK-VTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVE 689
Cdd:pfam01819 1 AKFQAFTLSDIGGNGDVTLALNprgvNFANGVAALIEAGARPAAEKrVTCSVRQPSANNKKYKIKVEIPKPASCTAGGTC 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1844115818 690 LPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGI 741
Cdd:pfam01819 81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
|
|
| eL8_ribo |
TIGR03677 |
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version ... |
1738-1854 |
8.59e-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: 8.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1738 YVRFEVPEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKND 1817
Cdd:TIGR03677 1 YVKFEVPEELADKALEAVEKARETGKIKKGTNEVTKAVERGIAKLVVIAEDVEPPEIVAHLPALCEEKGIPYIYVKSKED 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844115818 1818 LGRAVGIEVPCASAAIINEGELRKELGSLVEKIKGLQ 1854
Cdd:TIGR03677 81 LGAAAGLEVGAASAAIVDAGKAEELLKEIIEKVEALK 117
|
|
| DHFR |
cd00209 |
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ... |
1060-1215 |
1.34e-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: 1.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1060 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIG-RPLPGRKNIILSSQPST--DDRVTWVKSV 1136
Cdd:cd00209 1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrRPLPGRTNIVLSRQLDYqdAEGVEVVHSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1137 DEAIAACG-DVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEfhDADAQNSHSYCFEILE 1215
Cdd:cd00209 81 EEALELAEnTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIDESEWELVSEE--EVFEEDGYSYTFETYE 158
|
|
| FRB_dom |
pfam08771 |
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ... |
1369-1461 |
1.16e-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: 1.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1369 SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLLQ 1448
Cdd:pfam08771 6 AILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDEEDLNQ 85
|
90
....*....|...
gi 1844115818 1449 AWDLYYHVFRRIS 1461
Cdd:pfam08771 86 AWDIYYSVFRRIK 98
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
1483-1586 |
3.46e-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: 3.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1483 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 1562
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115818 1563 YGATGHPGIIPPHATLVFDVELLK 1586
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
4-107 |
5.77e-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: 5.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 4 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 83
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115818 84 YGATGHPGIIPPHATLVFDVELLK 107
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
1493-1585 |
6.35e-42 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 149.27 E-value: 6.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1493 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 1571
Cdd:pfam00254 1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
|
90
....*....|....
gi 1844115818 1572 IPPHATLVFDVELL 1585
Cdd:pfam00254 81 IPPNATLVFEVELL 94
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
14-106 |
8.16e-41 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 145.80 E-value: 8.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 14 GRTFPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 92
Cdd:pfam00254 1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
|
90
....*....|....
gi 1844115818 93 IPPHATLVFDVELL 106
Cdd:pfam00254 81 IPPNATLVFEVELL 94
|
|
| FolA |
COG0262 |
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ... |
1060-1197 |
2.83e-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: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1060 ISLIAALAVDYVIGME-NAMPW--NLPADLAWFKRNTLN-KPVIMGRHTWESI-----GRPLPGRKNIILSSQP--STDD 1128
Cdd:COG0262 3 LILIVAVSLDGVIGGPdGDLPWlfPDPEDLAHFKELTAGaDAVLMGRKTYESIagywpTRPLPGRPKIVLSRTLdeADWE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844115818 1129 RVTWVK-SVDEAIAAC--GDVPEIMVIGGGRVIEQFLPK--AQKLYLTHIDAEV-EGDTHFPDY-EPDDWESVFSE 1197
Cdd:COG0262 83 GVTVVSgDLEEALAALkaAGGKDIWVIGGGELYRQLLPAglVDELYLTVVPVVLgEGDRLFPELdAPSRLELVESE 158
|
|
| Ribosomal_L7Ae |
pfam01248 |
Ribosomal protein L7Ae/L30e/S12e/Gadd45 family; This family includes: Ribosomal L7A from ... |
1750-1838 |
8.41e-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: 8.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1750 EALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCA 1829
Cdd:pfam01248 2 AIYEVLKKALKTGKLVLGLKEVTKALERGEAKLVIIAEDCDPEEKVKLIPALCKEKNVPYVKVPSKKELGEACGKKRPVS 81
|
....*....
gi 1844115818 1830 SAAIINEGE 1838
Cdd:pfam01248 82 ALAIKDEGD 90
|
|
| Rpl7Ae |
COG1358 |
Ribosomal protein L7Ae or related RNA K-turn-binding protein [Translation, ribosomal structure ... |
1749-1843 |
5.36e-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: 5.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1749 NEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDpPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGiEVPC 1828
Cdd:COG1358 1 DKILNLLGLARRAGKLVSGEEQVLKAIRKGKAKLVIIAEDAS-ENTKKKLLDLCEEYGVPVVEVGTKEELGKAIG-KVGR 78
|
90
....*....|....*...
gi 1844115818 1829 ASAAIINEG---ELRKEL 1843
Cdd:COG1358 79 AVVAITDEGfakKLLELL 96
|
|
| SNU13 |
cd21104 |
U4/U6.U5 small nuclear ribonucleoprotein SNU13; U4/U6.U5 small nuclear ribonucleoprotein SNU13, ... |
1744-1853 |
2.53e-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: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1744 PEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVG 1823
Cdd:cd21104 9 DAQLTQTILDLVQQAANYKQLKKGANEATKTLNRGIAEFIVMAADAEPLEILLHLPLLCEDKNVPYVFVPSKQALGRACG 88
|
90 100 110
....*....|....*....|....*....|..
gi 1844115818 1824 IEVPCASAAII-NEG-ELRKELGSLVEKIKGL 1853
Cdd:cd21104 89 VSRPVIACSVTtNEGsQLKSQIQSLKDAIEKL 120
|
|
| dihyfolred_HdrA_Halo |
NF041386 |
dihydrofolate reductase HdrA; |
1063-1200 |
4.95e-29 |
|
dihydrofolate reductase HdrA;
Pssm-ID: 469277 [Multi-domain] Cd Length: 158 Bit Score: 114.67 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1063 IAALAVDYVIGMENAMPWN-LPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPST--DDRVTWVKSVDEA 1139
Cdd:NF041386 6 VAAVAENGVIGRDGELPWPsIPADKRQYRERVADDPVILGRRTFESMRDDLPGSAQIVLSRSEREfdVETAHHAGGVDEA 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844115818 1140 --IAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHD 1200
Cdd:NF041386 86 ieIAESLGAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYPEWDEDEWELVEETEYD 148
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
1484-1588 |
6.74e-25 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1484 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 1563
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
|
90 100
....*....|....*....|....*
gi 1844115818 1564 GATGHPGiIPPHATLVFDVELLKLE 1588
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1248-1361 |
6.34e-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: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1248 ESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNG--TLLVQSLHGVFKVKNTTTLQQHLIDG 1325
Cdd:pfam00863 4 KSIAKGLRDYHHIASNLAALEYYCGDHKGEIHGICHGDKIITPAHLFKEACGndTLKIQSKHGLFDLEALDRQKIEELCG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844115818 1326 RDMIIIRMPKDFPPFPQKLKFREPQREER----ICLVTTN 1361
Cdd:pfam00863 84 QDIIVIKGPIDMPPAKMRLIFRAPIQCERavliGCRRDDN 123
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
5-109 |
1.06e-23 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 5 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 84
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
|
90 100
....*....|....*....|....*..
gi 1844115818 85 GATGHPGiIPPHATLVFDVELL--KPE 109
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLdvKPA 251
|
|
| PRK13602 |
PRK13602 |
50S ribosomal protein L7ae-like protein; |
1756-1834 |
2.39e-18 |
|
50S ribosomal protein L7ae-like protein;
Pssm-ID: 184174 [Multi-domain] Cd Length: 82 Bit Score: 81.37 E-value: 2.39e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115818 1756 EKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPeIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAAII 1834
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 ... |
2117-2160 |
1.86e-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: 1.86e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1844115818 2117 STWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPA--MPDREVLY 2160
Cdd:pfam01006 1 STWVLVGGALAAGAAYCLTTGSVVVVGRWSVNGKPPavVPDREVLY 46
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1602-1705 |
5.80e-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: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1602 DTSCTFPSS--DGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSAS----NFTNTN-NYFTSVPKNFMELLTNQE-AQQW 1673
Cdd:pfam00863 131 DESAIFPLGkeNGGFWKHGCDTKLGDCGGPIIACDDMDIIGFHGGRlmqlGANNSLaHIFAALNDDFIEMFAEMEtAKGF 210
|
90 100 110
....*....|....*....|....*....|..
gi 1844115818 1674 VSGWRLNADSVLWGGHKVFMVKPEEPFQPVKE 1705
Cdd:pfam00863 211 QRKWKFNADKVEWGRLDLTSNQPSGAFKIQKL 242
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
321-541 |
2.37e-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: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 321 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 391
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 392 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 466
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 467 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 523
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
|
250 260
....*....|....*....|..
gi 1844115818 524 ----IGPQHQAGSDSLLTGMAF 541
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
775-995 |
2.37e-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: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 775 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 845
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 846 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 920
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 921 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 977
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
|
250 260
....*....|....*....|..
gi 1844115818 978 ----IGPQHQAGSDSLLTGMAF 995
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
|
|
| TEL1 |
COG5032 |
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms]; |
1367-1463 |
2.65e-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: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1367 SGSILWHEMWHEGLEEASRLYFGERN-VKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKD 1445
Cdd:COG5032 1630 IAYPLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISL 1709
|
90
....*....|....*...
gi 1844115818 1446 LLQAWDLYYHVFRRISKQ 1463
Cdd:COG5032 1710 LNLSRKLYISVLRSIRKR 1727
|
|
| trim_DfrL |
NF041668 |
trimethoprim-resistant dihydrofolate reductase DfrL; |
1072-1217 |
7.17e-08 |
|
trimethoprim-resistant dihydrofolate reductase DfrL;
Pssm-ID: 469550 [Multi-domain] Cd Length: 176 Bit Score: 54.28 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1072 IGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIG-RPLPGRKNIILSsqpstdDRVTWVKsvDEAIaacgdVPEIM 1150
Cdd:NF041668 30 FGNSGDDDVNLMGDKKHEKIPTMDDKNRIGIKLTENIPvRADGAIICHSKE------DNKNYLA--DGAI-----ECHIH 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844115818 1151 VIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR 1217
Cdd:NF041668 97 EDGGISAFEMFIDEPIHLHGGIIAEEFEGDEVMIEHDTIIDECFDGADGMPDEDNKYFHCFDIADGK 163
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| folA |
PRK10769 |
type 3 dihydrofolate reductase; |
1060-1217 |
1.58e-115 |
|
type 3 dihydrofolate reductase;
Pssm-ID: 182714 [Multi-domain] Cd Length: 159 Bit Score: 362.52 E-value: 1.58e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1060 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTDDRVTWVKSVDEA 1139
Cdd:PRK10769 2 ISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIVISSQPGTDDRVTWVKSVDEA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844115818 1140 IAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR 1217
Cdd:PRK10769 82 LAAAGDVPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYEPDEWESVFSEFHDADEQNSHSYCFEILERR 159
|
|
| POP2 |
COG5228 |
mRNA deadenylase subunit [RNA processing and modification]; |
303-582 |
3.07e-110 |
|
mRNA deadenylase subunit [RNA processing and modification];
Pssm-ID: 227553 Cd Length: 299 Bit Score: 353.46 E-value: 3.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 303 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 380
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 381 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 460
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 461 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 540
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115818 541 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 582
Cdd:COG5228 246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
|
|
| POP2 |
COG5228 |
mRNA deadenylase subunit [RNA processing and modification]; |
757-1036 |
3.07e-110 |
|
mRNA deadenylase subunit [RNA processing and modification];
Pssm-ID: 227553 Cd Length: 299 Bit Score: 353.46 E-value: 3.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 757 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 834
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 835 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 914
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 915 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 994
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115818 995 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 1036
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 ... |
1928-2076 |
1.32e-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: 1.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1928 EGEVQIVSTATQTFLATCINGVCWAVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTR 2007
Cdd:pfam02907 1 EGEVQVLGTATQRFMGTCVNGVLWTTFHGAGSRTLAGPKGPVNQMYWSASDDVVGYPLPPGAGSLTPCTCGATDLYLVTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115818 2008 HADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETT 2076
Cdd:pfam02907 81 DGDLIPGRRRGDPRVSLLSPRPLSYLKGSSGGPILCPSGHVVGMFRAAVHSGGVVKAVRFVPWETLPTT 149
|
|
| cp |
PHA00026 |
coat protein |
160-288 |
1.48e-85 |
|
coat protein
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 160 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 239
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115818 240 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 288
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| cp |
PHA00026 |
coat protein |
614-742 |
1.48e-85 |
|
coat protein
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 1.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 614 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 693
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115818 694 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 742
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| DHFR_1 |
pfam00186 |
Dihydrofolate reductase; |
1060-1216 |
1.69e-77 |
|
Dihydrofolate reductase;
Pssm-ID: 425512 [Multi-domain] Cd Length: 159 Bit Score: 253.62 E-value: 1.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1060 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTD-DRVTWVKSVDE 1138
Cdd:pfam00186 2 ISLIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGRPLPGRKNIVLTRNPDYKvDGVEVVHSLEE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844115818 1139 AIAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILER 1216
Cdd:pfam00186 82 ALALAAEAEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPEIDPSEWQLVSREEHEADEKNPYPYTFVTYER 159
|
|
| Levi_coat |
pfam01819 |
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ... |
161-287 |
1.56e-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: 1.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 161 SNFTQFVLVDNGGTGDVTVAPS----NFANGVAEWISSNSRSQAYK-VTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVE 235
Cdd:pfam01819 1 AKFQAFTLSDIGGNGDVTLALNprgvNFANGVAALIEAGARPAAEKrVTCSVRQPSANNKKYKIKVEIPKPASCTAGGTC 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1844115818 236 LPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGI 287
Cdd:pfam01819 81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
|
|
| Levi_coat |
pfam01819 |
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ... |
615-741 |
1.56e-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: 1.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 615 SNFTQFVLVDNGGTGDVTVAPS----NFANGVAEWISSNSRSQAYK-VTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVE 689
Cdd:pfam01819 1 AKFQAFTLSDIGGNGDVTLALNprgvNFANGVAALIEAGARPAAEKrVTCSVRQPSANNKKYKIKVEIPKPASCTAGGTC 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1844115818 690 LPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGI 741
Cdd:pfam01819 81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
|
|
| eL8_ribo |
TIGR03677 |
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version ... |
1738-1854 |
8.59e-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: 8.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1738 YVRFEVPEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKND 1817
Cdd:TIGR03677 1 YVKFEVPEELADKALEAVEKARETGKIKKGTNEVTKAVERGIAKLVVIAEDVEPPEIVAHLPALCEEKGIPYIYVKSKED 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844115818 1818 LGRAVGIEVPCASAAIINEGELRKELGSLVEKIKGLQ 1854
Cdd:TIGR03677 81 LGAAAGLEVGAASAAIVDAGKAEELLKEIIEKVEALK 117
|
|
| DHFR |
cd00209 |
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ... |
1060-1215 |
1.34e-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: 1.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1060 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIG-RPLPGRKNIILSSQPST--DDRVTWVKSV 1136
Cdd:cd00209 1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPrRPLPGRTNIVLSRQLDYqdAEGVEVVHSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1137 DEAIAACG-DVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEfhDADAQNSHSYCFEILE 1215
Cdd:cd00209 81 EEALELAEnTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIDESEWELVSEE--EVFEEDGYSYTFETYE 158
|
|
| FRB_dom |
pfam08771 |
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ... |
1369-1461 |
1.16e-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: 1.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1369 SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLLQ 1448
Cdd:pfam08771 6 AILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDEEDLNQ 85
|
90
....*....|...
gi 1844115818 1449 AWDLYYHVFRRIS 1461
Cdd:pfam08771 86 AWDIYYSVFRRIK 98
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
1483-1586 |
3.46e-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: 3.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1483 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 1562
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115818 1563 YGATGHPGIIPPHATLVFDVELLK 1586
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
4-107 |
5.77e-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: 5.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 4 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 83
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115818 84 YGATGHPGIIPPHATLVFDVELLK 107
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
1493-1585 |
6.35e-42 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 149.27 E-value: 6.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1493 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 1571
Cdd:pfam00254 1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
|
90
....*....|....
gi 1844115818 1572 IPPHATLVFDVELL 1585
Cdd:pfam00254 81 IPPNATLVFEVELL 94
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
14-106 |
8.16e-41 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 145.80 E-value: 8.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 14 GRTFPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 92
Cdd:pfam00254 1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
|
90
....*....|....
gi 1844115818 93 IPPHATLVFDVELL 106
Cdd:pfam00254 81 IPPNATLVFEVELL 94
|
|
| FolA |
COG0262 |
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ... |
1060-1197 |
2.83e-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: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1060 ISLIAALAVDYVIGME-NAMPW--NLPADLAWFKRNTLN-KPVIMGRHTWESI-----GRPLPGRKNIILSSQP--STDD 1128
Cdd:COG0262 3 LILIVAVSLDGVIGGPdGDLPWlfPDPEDLAHFKELTAGaDAVLMGRKTYESIagywpTRPLPGRPKIVLSRTLdeADWE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844115818 1129 RVTWVK-SVDEAIAAC--GDVPEIMVIGGGRVIEQFLPK--AQKLYLTHIDAEV-EGDTHFPDY-EPDDWESVFSE 1197
Cdd:COG0262 83 GVTVVSgDLEEALAALkaAGGKDIWVIGGGELYRQLLPAglVDELYLTVVPVVLgEGDRLFPELdAPSRLELVESE 158
|
|
| Ribosomal_L7Ae |
pfam01248 |
Ribosomal protein L7Ae/L30e/S12e/Gadd45 family; This family includes: Ribosomal L7A from ... |
1750-1838 |
8.41e-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: 8.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1750 EALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCA 1829
Cdd:pfam01248 2 AIYEVLKKALKTGKLVLGLKEVTKALERGEAKLVIIAEDCDPEEKVKLIPALCKEKNVPYVKVPSKKELGEACGKKRPVS 81
|
....*....
gi 1844115818 1830 SAAIINEGE 1838
Cdd:pfam01248 82 ALAIKDEGD 90
|
|
| Rpl7Ae |
COG1358 |
Ribosomal protein L7Ae or related RNA K-turn-binding protein [Translation, ribosomal structure ... |
1749-1843 |
5.36e-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: 5.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1749 NEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDpPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGiEVPC 1828
Cdd:COG1358 1 DKILNLLGLARRAGKLVSGEEQVLKAIRKGKAKLVIIAEDAS-ENTKKKLLDLCEEYGVPVVEVGTKEELGKAIG-KVGR 78
|
90
....*....|....*...
gi 1844115818 1829 ASAAIINEG---ELRKEL 1843
Cdd:COG1358 79 AVVAITDEGfakKLLELL 96
|
|
| SNU13 |
cd21104 |
U4/U6.U5 small nuclear ribonucleoprotein SNU13; U4/U6.U5 small nuclear ribonucleoprotein SNU13, ... |
1744-1853 |
2.53e-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: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1744 PEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVG 1823
Cdd:cd21104 9 DAQLTQTILDLVQQAANYKQLKKGANEATKTLNRGIAEFIVMAADAEPLEILLHLPLLCEDKNVPYVFVPSKQALGRACG 88
|
90 100 110
....*....|....*....|....*....|..
gi 1844115818 1824 IEVPCASAAII-NEG-ELRKELGSLVEKIKGL 1853
Cdd:cd21104 89 VSRPVIACSVTtNEGsQLKSQIQSLKDAIEKL 120
|
|
| dihyfolred_HdrA_Halo |
NF041386 |
dihydrofolate reductase HdrA; |
1063-1200 |
4.95e-29 |
|
dihydrofolate reductase HdrA;
Pssm-ID: 469277 [Multi-domain] Cd Length: 158 Bit Score: 114.67 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1063 IAALAVDYVIGMENAMPWN-LPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPST--DDRVTWVKSVDEA 1139
Cdd:NF041386 6 VAAVAENGVIGRDGELPWPsIPADKRQYRERVADDPVILGRRTFESMRDDLPGSAQIVLSRSEREfdVETAHHAGGVDEA 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844115818 1140 --IAACGDVPEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHD 1200
Cdd:NF041386 86 ieIAESLGAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYPEWDEDEWELVEETEYD 148
|
|
| PTZ00164 |
PTZ00164 |
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional |
1055-1251 |
2.13e-25 |
|
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
Pssm-ID: 240299 [Multi-domain] Cd Length: 514 Bit Score: 112.84 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1055 SGSGSISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKP-------------VIMGRHTWESIG---RPLPGRKNI 1118
Cdd:PTZ00164 5 SSLKDFSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYVReekyekspkkqnaVIMGRKTWESIPkkfRPLKNRINV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1119 ILSS---QPSTDDRVTWVKSVDEAIAACGDVP---EIMVIGGGRVIEQFLP--KAQKLYLTHIDAEVEGDTHFPDYePDD 1190
Cdd:PTZ00164 85 VLSRtltEEEADPGVLVFGSLEDALRLLAEDLsieKIFIIGGASVYREALSanLLDKIYLTRVNSEYECDVFFPKI-PES 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844115818 1191 WESVFSEFHDADAQNShSYCFEILERRGSAVKQTL--NFDLLKLAGDVESNPGPMGRSGESLF 1251
Cdd:PTZ00164 164 FFIVAIVSQTFSTNGT-SYDFVIYEKKNDDEEDLLgkIFGQMKMTGRKKSPKEQLYKACPSLK 225
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
1484-1588 |
6.74e-25 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1484 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 1563
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
|
90 100
....*....|....*....|....*
gi 1844115818 1564 GATGHPGiIPPHATLVFDVELLKLE 1588
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1248-1361 |
6.34e-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: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1248 ESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNG--TLLVQSLHGVFKVKNTTTLQQHLIDG 1325
Cdd:pfam00863 4 KSIAKGLRDYHHIASNLAALEYYCGDHKGEIHGICHGDKIITPAHLFKEACGndTLKIQSKHGLFDLEALDRQKIEELCG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844115818 1326 RDMIIIRMPKDFPPFPQKLKFREPQREER----ICLVTTN 1361
Cdd:pfam00863 84 QDIIVIKGPIDMPPAKMRLIFRAPIQCERavliGCRRDDN 123
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
5-109 |
1.06e-23 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 5 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 84
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
|
90 100
....*....|....*....|....*..
gi 1844115818 85 GATGHPGiIPPHATLVFDVELL--KPE 109
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLdvKPA 251
|
|
| PRK11570 |
PRK11570 |
peptidyl-prolyl cis-trans isomerase; Provisional |
1482-1587 |
1.50e-20 |
|
peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 183207 [Multi-domain] Cd Length: 206 Bit Score: 92.17 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1482 GVQVETISPGDGrTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKqeVIRGWEEGVAQMSVGQRAKLTISPDY 1561
Cdd:PRK11570 103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
|
90 100
....*....|....*....|....*.
gi 1844115818 1562 AYGATGHPGIIPPHATLVFDVELLKL 1587
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELLEI 205
|
|
| PRK11570 |
PRK11570 |
peptidyl-prolyl cis-trans isomerase; Provisional |
3-106 |
3.47e-19 |
|
peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 183207 [Multi-domain] Cd Length: 206 Bit Score: 87.93 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 3 GVQVETISPGDGrTFPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFMLGKqeVIRGWEEGVAQMSVGQRAKLTISPDY 82
Cdd:PRK11570 103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
|
90 100
....*....|....*....|....
gi 1844115818 83 AYGATGHPGIIPPHATLVFDVELL 106
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELL 203
|
|
| PRK13602 |
PRK13602 |
50S ribosomal protein L7ae-like protein; |
1756-1834 |
2.39e-18 |
|
50S ribosomal protein L7ae-like protein;
Pssm-ID: 184174 [Multi-domain] Cd Length: 82 Bit Score: 81.37 E-value: 2.39e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115818 1756 EKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPeIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAAII 1834
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 ... |
2117-2160 |
1.86e-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: 1.86e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1844115818 2117 STWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPA--MPDREVLY 2160
Cdd:pfam01006 1 STWVLVGGALAAGAAYCLTTGSVVVVGRWSVNGKPPavVPDREVLY 46
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
1602-1705 |
5.80e-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: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1602 DTSCTFPSS--DGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSAS----NFTNTN-NYFTSVPKNFMELLTNQE-AQQW 1673
Cdd:pfam00863 131 DESAIFPLGkeNGGFWKHGCDTKLGDCGGPIIACDDMDIIGFHGGRlmqlGANNSLaHIFAALNDDFIEMFAEMEtAKGF 210
|
90 100 110
....*....|....*....|....*....|..
gi 1844115818 1674 VSGWRLNADSVLWGGHKVFMVKPEEPFQPVKE 1705
Cdd:pfam00863 211 QRKWKFNADKVEWGRLDLTSNQPSGAFKIQKL 242
|
|
| PTZ00365 |
PTZ00365 |
60S ribosomal protein L7Ae-like; Provisional |
1764-1842 |
3.51e-13 |
|
60S ribosomal protein L7Ae-like; Provisional
Pssm-ID: 240382 Cd Length: 266 Bit Score: 71.80 E-value: 3.51e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115818 1764 VKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGiEVPCASAAIINegeLRKE 1842
Cdd:PTZ00365 133 LKYGLNHVTDLVEYKKAKLVVIAHDVDPIELVCFLPALCRKKEVPYCIIKGKSRLGKLVH-QKTAAVVAIDN---VRKE 207
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
1498-1584 |
3.97e-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: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1498 KRGQTCVVHYTGMLEDGKKFDSSRDRnKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGatghpgiiPPHAT 1577
Cdd:COG1047 2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPE 72
|
....*..
gi 1844115818 1578 LVFDVEL 1584
Cdd:COG1047 73 LVQTVPR 79
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
19-105 |
8.29e-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: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 19 KRGQTCVVHYTGMLEDGKKVDSSRDRnKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGatghpgiiPPHAT 98
Cdd:COG1047 2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPE 72
|
....*..
gi 1844115818 99 LVFDVEL 105
Cdd:COG1047 73 LVQTVPR 79
|
|
| PTZ00222 |
PTZ00222 |
60S ribosomal protein L7a; Provisional |
1764-1823 |
1.59e-10 |
|
60S ribosomal protein L7a; Provisional
Pssm-ID: 140249 Cd Length: 263 Bit Score: 63.95 E-value: 1.59e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1764 VKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVG 1823
Cdd:PTZ00222 133 VVTGLQEVTRAIEKKQARMVVIANNVDPVELVLWMPNLCRANKIPYAIVKDMARLGDAIG 192
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
321-541 |
2.37e-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: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 321 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 391
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 392 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 466
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 467 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 523
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
|
250 260
....*....|....*....|..
gi 1844115818 524 ----IGPQHQAGSDSLLTGMAF 541
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
775-995 |
2.37e-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: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 775 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 845
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 846 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 920
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 921 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 977
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
|
250 260
....*....|....*....|..
gi 1844115818 978 ----IGPQHQAGSDSLLTGMAF 995
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
|
|
| TEL1 |
COG5032 |
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms]; |
1367-1463 |
2.65e-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: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1367 SGSILWHEMWHEGLEEASRLYFGERN-VKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKD 1445
Cdd:COG5032 1630 IAYPLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISL 1709
|
90
....*....|....*...
gi 1844115818 1446 LLQAWDLYYHVFRRISKQ 1463
Cdd:COG5032 1710 LNLSRKLYISVLRSIRKR 1727
|
|
| RPL30E |
COG1911 |
Ribosomal protein L30E [Translation, ribosomal structure and biogenesis]; Ribosomal protein ... |
1755-1838 |
3.20e-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: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1755 LEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVdPPEIVAHLPLLCEEKNVP-YIYVKSKNDLGRAVGIEVPCASAAI 1833
Cdd:COG1911 8 LRDAVKTGKVVLGSKQTIKAIKLGKAKLVILAANC-PPEIREDIEYYAKLSNVPvYVYPGTSVELGALCGKPFRVSALAI 86
|
....*
gi 1844115818 1834 INEGE 1838
Cdd:COG1911 87 IDPGE 91
|
|
| PRK01018 |
PRK01018 |
50S ribosomal protein L30e; Reviewed |
1755-1838 |
5.85e-08 |
|
50S ribosomal protein L30e; Reviewed
Pssm-ID: 179205 [Multi-domain] Cd Length: 99 Bit Score: 52.27 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1755 LEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVdPPEIVAHLPLLCEEKNVP-YIYVKSKNDLGRAVGIEVPCASAAI 1833
Cdd:PRK01018 8 LRVAVDTGKVILGSKRTIKAIKLGKAKLVIVASNC-PKDIKEDIEYYAKLSGIPvYEYEGSSVELGTLCGKPFTVSALAI 86
|
....*
gi 1844115818 1834 INEGE 1838
Cdd:PRK01018 87 VDPGE 91
|
|
| trim_DfrL |
NF041668 |
trimethoprim-resistant dihydrofolate reductase DfrL; |
1072-1217 |
7.17e-08 |
|
trimethoprim-resistant dihydrofolate reductase DfrL;
Pssm-ID: 469550 [Multi-domain] Cd Length: 176 Bit Score: 54.28 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1072 IGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIG-RPLPGRKNIILSsqpstdDRVTWVKsvDEAIaacgdVPEIM 1150
Cdd:NF041668 30 FGNSGDDDVNLMGDKKHEKIPTMDDKNRIGIKLTENIPvRADGAIICHSKE------DNKNYLA--DGAI-----ECHIH 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844115818 1151 VIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR 1217
Cdd:NF041668 97 EDGGISAFEMFIDEPIHLHGGIIAEEFEGDEVMIEHDTIIDECFDGADGMPDEDNKYFHCFDIADGK 163
|
|
| scpA |
PRK00478 |
segregation and condensation protein ScpA; |
1060-1183 |
1.27e-07 |
|
segregation and condensation protein ScpA;
Pssm-ID: 234776 [Multi-domain] Cd Length: 505 Bit Score: 56.86 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1060 ISLIAALAVDYVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPSTD----DRVTWVKS 1135
Cdd:PRK00478 2 IKLIWCEDLNFGIAKNNQIPWKIDEELNHFHQTTTNHTIVMGYNTFQAMNKILANQANIVISKKHQRElknnNELFVFND 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1844115818 1136 VDEAIAACGDVpEIMVIGGGRVIEQFLPKAQKLYLTHIDAEVEGDTHF 1183
Cdd:PRK00478 82 LKKLLIDFSNV-DLFIIGGKKTIEQFIKYADQLIISKLNADYKCDLFV 128
|
|
| PRK13601 |
PRK13601 |
putative L7Ae-like ribosomal protein; Provisional |
1767-1836 |
3.95e-07 |
|
putative L7Ae-like ribosomal protein; Provisional
Pssm-ID: 184173 Cd Length: 82 Bit Score: 49.59 E-value: 3.95e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844115818 1767 GTNETTKAVERGLAKLVYIAEDVDPpEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAA-IINE 1836
Cdd:PRK13601 12 GAKQTLKAITNCNVLQVYIAKDAEE-HVTKKIKELCEEKSIKIVYIDTMKELGVMCGIDVGAAAAAdIIGE 81
|
|
| PRK15095 |
PRK15095 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
26-85 |
3.91e-06 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 237908 [Multi-domain] Cd Length: 156 Bit Score: 48.94 E-value: 3.91e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 26 VHYTGMLEDGKKVDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYG 85
Cdd:PRK15095 13 VHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG 72
|
|
| PRK15095 |
PRK15095 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
1505-1564 |
7.76e-06 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 237908 [Multi-domain] Cd Length: 156 Bit Score: 48.16 E-value: 7.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1505 VHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYG 1564
Cdd:PRK15095 13 VHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG 72
|
|
| PRK06683 |
PRK06683 |
hypothetical protein; Provisional |
1756-1835 |
2.18e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 136002 Cd Length: 82 Bit Score: 44.68 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1756 EKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDP--PEIVAHLPLlceEKNVPYIYVKSKNDLGRAVGIEVPCASAAI 1833
Cdd:PRK06683 4 QKVSNAENVVVGHKRTLEAIKNGIVKEVVIAEDADMrlTHVIIRTAL---QHNIPITKVESVRKLGKVAGIQVGASAIGI 80
|
..
gi 1844115818 1834 IN 1835
Cdd:PRK06683 81 IS 82
|
|
| PRK07714 |
PRK07714 |
YlxQ family RNA-binding protein; |
1748-1841 |
2.35e-05 |
|
YlxQ family RNA-binding protein;
Pssm-ID: 236077 Cd Length: 100 Bit Score: 45.15 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1748 QNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDpPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVP 1827
Cdd:PRK07714 3 MSDWKSFLGLANRARKVISGEELVLKEVRSGKAKLVLLSEDAS-VNTTKKITDKCTYYNVPMRKVENRQQLGHAIGKDER 81
|
90
....*....|....
gi 1844115818 1828 CAsAAIINEGELRK 1841
Cdd:PRK07714 82 VV-VAVLDEGFAKK 94
|
|
| PTZ00106 |
PTZ00106 |
60S ribosomal protein L30; Provisional |
1755-1838 |
1.59e-04 |
|
60S ribosomal protein L30; Provisional
Pssm-ID: 185450 Cd Length: 108 Bit Score: 43.14 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1755 LEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVdPP------EIVAHLpllceEKNVPYIYVKSKNDLGRAVGIEVPC 1828
Cdd:PTZ00106 17 LQLVMKSGKYTLGTKSTLKALRNGKAKLVIISNNC-PPirrseiEYYAML-----SKTGVHHYAGNNNDLGTACGRHFRV 90
|
90
....*....|
gi 1844115818 1829 ASAAIINEGE 1838
Cdd:PTZ00106 91 SVMSITDAGD 100
|
|
| PRK13600 |
PRK13600 |
putative ribosomal protein L7Ae-like; Provisional |
1767-1835 |
6.16e-04 |
|
putative ribosomal protein L7Ae-like; Provisional
Pssm-ID: 184172 Cd Length: 84 Bit Score: 40.60 E-value: 6.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115818 1767 GTNETTKAVERGLAKLVYIAEDVDPpEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAAIIN 1835
Cdd:PRK13600 17 GLKETLKALKKDQVTSLIIAEDVEV-YLMTRVLSQINQKNIPVSFFKSKHALGKHVGINVNATIVALIK 84
|
|
| PRK05583 |
PRK05583 |
ribosomal protein L7Ae family protein; Provisional |
1747-1823 |
1.25e-03 |
|
ribosomal protein L7Ae family protein; Provisional
Pssm-ID: 235517 Cd Length: 104 Bit Score: 40.42 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115818 1747 MQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDP---PEIVAHlpllCEEKNVPYIYVKSKNDLGRAVG 1823
Cdd:PRK05583 1 MMNKFLNFLGLTKKAGKLLEGYNKCEEAIKKKKVYLIIISNDISEnskNKFKNY----CNKYNIPYIEGYSKEELGNAIG 76
|
|
| |
