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Conserved domains on  [gi|1844115814|gb|QJX60197|]
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degron-tvmvS-MCP-cNOT7-E2A-MCP-cNOT7-tevS-degron-F2A-nTEVp-FRB-T2A-FKBP-cTEVp-P2A-L7Ae-SMASh [Cloning vector pB-4-NOR-degron-tvmvS-MCP-cNOT7-E2A-MCP-cNOT7-tevS-degron-F2A-nTEVp-FRB-T2A-FKBP-cTEVp-P2A-L7Ae-SMASh]

Protein Classification

Graphical summary

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List of domain hits

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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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