|
Name |
Accession |
Description |
Interval |
E-value |
| CAF1 super family |
cl23804 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
155-434 |
3.82e-112 |
|
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: 355.00 E-value: 3.82e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 155 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 232
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 233 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 312
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 313 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 392
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115810 393 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 434
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 ... |
1152-1300 |
2.71e-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: 280.08 E-value: 2.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 1152 EGEVQIVSTATQTFLATCINGVCWAVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTR 1231
Cdd:pfam02907 1 EGEVQVLGTATQRFMGTCVNGVLWTTFHGAGSRTLAGPKGPVNQMYWSASDDVVGYPLPPGAGSLTPCTCGATDLYLVTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115810 1232 HADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETT 1300
Cdd:pfam02907 81 DGDLIPGRRRGDPRVSLLSPRPLSYLKGSSGGPILCPSGHVVGMFRAAVHSGGVVKAVRFVPWETLPTT 149
|
|
| cp |
PHA00026 |
coat protein |
5-133 |
6.65e-86 |
|
coat protein
:
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 6.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 5 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 84
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115810 85 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 133
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| eL8_ribo |
TIGR03677 |
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version ... |
962-1078 |
5.35e-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: 5.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 962 YVRFEVPEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKND 1041
Cdd:TIGR03677 1 YVKFEVPEELADKALEAVEKARETGKIKKGTNEVTKAVERGIAKLVVIAEDVEPPEIVAHLPALCEEKGIPYIYVKSKED 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844115810 1042 LGRAVGIEVPCASAAIINEGELRKELGSLVEKIKGLQ 1078
Cdd:TIGR03677 81 LGAAAGLEVGAASAAIVDAGKAEELLKEIIEKVEALK 117
|
|
| FRB_dom |
pfam08771 |
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ... |
593-685 |
7.37e-56 |
|
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: 7.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 593 SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLLQ 672
Cdd:pfam08771 6 AILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDEEDLNQ 85
|
90
....*....|...
gi 1844115810 673 AWDLYYHVFRRIS 685
Cdd:pfam08771 86 AWDIYYSVFRRIK 98
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
707-810 |
1.53e-43 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
:
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 153.41 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 707 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 786
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115810 787 YGATGHPGIIPPHATLVFDVELLK 810
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| Peptidase_C4 super family |
cl24133 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
472-585 |
3.86e-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: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 472 ESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNG--TLLVQSLHGVFKVKNTTTLQQHLIDG 549
Cdd:pfam00863 4 KSIAKGLRDYHHIASNLAALEYYCGDHKGEIHGICHGDKIITPAHLFKEACGndTLKIQSKHGLFDLEALDRQKIEELCG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844115810 550 RDMIIIRMPKDFPPFPQKLKFREPQREER----ICLVTTN 585
Cdd:pfam00863 84 QDIIVIKGPIDMPPAKMRLIFRAPIQCERavliGCRRDDN 123
|
|
| HCV_NS4a |
pfam01006 |
Hepatitis C virus non-structural protein NS4a; NS4a forms an integral part of the NS3 serine ... |
1341-1384 |
1.46e-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: 1.46e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1844115810 1341 STWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPA--MPDREVLY 1384
Cdd:pfam01006 1 STWVLVGGALAAGAAYCLTTGSVVVVGRWSVNGKPPavVPDREVLY 46
|
|
| Peptidase_C4 super family |
cl24133 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
826-929 |
3.55e-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: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 826 DTSCTFPSS--DGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSAS----NFTNTN-NYFTSVPKNFMELLTNQE-AQQW 897
Cdd:pfam00863 131 DESAIFPLGkeNGGFWKHGCDTKLGDCGGPIIACDDMDIIGFHGGRlmqlGANNSLaHIFAALNDDFIEMFAEMEtAKGF 210
|
90 100 110
....*....|....*....|....*....|..
gi 1844115810 898 VSGWRLNADSVLWGGHKVFMVKPEEPFQPVKE 929
Cdd:pfam00863 211 QRKWKFNADKVEWGRLDLTSNQPSGAFKIQKL 242
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| POP2 |
COG5228 |
mRNA deadenylase subunit [RNA processing and modification]; |
155-434 |
3.82e-112 |
|
mRNA deadenylase subunit [RNA processing and modification];
Pssm-ID: 227553 Cd Length: 299 Bit Score: 355.00 E-value: 3.82e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 155 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 232
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 233 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 312
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 313 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 392
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115810 393 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 434
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 ... |
1152-1300 |
2.71e-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: 280.08 E-value: 2.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 1152 EGEVQIVSTATQTFLATCINGVCWAVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTR 1231
Cdd:pfam02907 1 EGEVQVLGTATQRFMGTCVNGVLWTTFHGAGSRTLAGPKGPVNQMYWSASDDVVGYPLPPGAGSLTPCTCGATDLYLVTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115810 1232 HADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETT 1300
Cdd:pfam02907 81 DGDLIPGRRRGDPRVSLLSPRPLSYLKGSSGGPILCPSGHVVGMFRAAVHSGGVVKAVRFVPWETLPTT 149
|
|
| cp |
PHA00026 |
coat protein |
5-133 |
6.65e-86 |
|
coat protein
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 6.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 5 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 84
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115810 85 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 133
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| Levi_coat |
pfam01819 |
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ... |
6-132 |
9.65e-70 |
|
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: 9.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 6 SNFTQFVLVDNGGTGDVTVAPS----NFANGVAEWISSNSRSQAYK-VTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVE 80
Cdd:pfam01819 1 AKFQAFTLSDIGGNGDVTLALNprgvNFANGVAALIEAGARPAAEKrVTCSVRQPSANNKKYKIKVEIPKPASCTAGGTC 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1844115810 81 LPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGI 132
Cdd:pfam01819 81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
|
|
| eL8_ribo |
TIGR03677 |
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version ... |
962-1078 |
5.35e-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: 5.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 962 YVRFEVPEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKND 1041
Cdd:TIGR03677 1 YVKFEVPEELADKALEAVEKARETGKIKKGTNEVTKAVERGIAKLVVIAEDVEPPEIVAHLPALCEEKGIPYIYVKSKED 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844115810 1042 LGRAVGIEVPCASAAIINEGELRKELGSLVEKIKGLQ 1078
Cdd:TIGR03677 81 LGAAAGLEVGAASAAIVDAGKAEELLKEIIEKVEALK 117
|
|
| FRB_dom |
pfam08771 |
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ... |
593-685 |
7.37e-56 |
|
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: 7.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 593 SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLLQ 672
Cdd:pfam08771 6 AILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDEEDLNQ 85
|
90
....*....|...
gi 1844115810 673 AWDLYYHVFRRIS 685
Cdd:pfam08771 86 AWDIYYSVFRRIK 98
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
707-810 |
1.53e-43 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 153.41 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 707 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 786
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115810 787 YGATGHPGIIPPHATLVFDVELLK 810
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
717-809 |
2.93e-42 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 149.65 E-value: 2.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 717 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 795
Cdd:pfam00254 1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
|
90
....*....|....
gi 1844115810 796 IPPHATLVFDVELL 809
Cdd:pfam00254 81 IPPNATLVFEVELL 94
|
|
| Ribosomal_L7Ae |
pfam01248 |
Ribosomal protein L7Ae/L30e/S12e/Gadd45 family; This family includes: Ribosomal L7A from ... |
974-1062 |
5.33e-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: 5.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 974 EALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCA 1053
Cdd:pfam01248 2 AIYEVLKKALKTGKLVLGLKEVTKALERGEAKLVIIAEDCDPEEKVKLIPALCKEKNVPYVKVPSKKELGEACGKKRPVS 81
|
....*....
gi 1844115810 1054 SAAIINEGE 1062
Cdd:pfam01248 82 ALAIKDEGD 90
|
|
| Rpl7Ae |
COG1358 |
Ribosomal protein L7Ae or related RNA K-turn-binding protein [Translation, ribosomal structure ... |
973-1067 |
3.40e-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: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 973 NEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDpPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGiEVPC 1052
Cdd:COG1358 1 DKILNLLGLARRAGKLVSGEEQVLKAIRKGKAKLVIIAEDAS-ENTKKKLLDLCEEYGVPVVEVGTKEELGKAIG-KVGR 78
|
90
....*....|....*...
gi 1844115810 1053 ASAAIINEG---ELRKEL 1067
Cdd:COG1358 79 AVVAITDEGfakKLLELL 96
|
|
| SNU13 |
cd21104 |
U4/U6.U5 small nuclear ribonucleoprotein SNU13; U4/U6.U5 small nuclear ribonucleoprotein SNU13, ... |
968-1077 |
1.59e-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: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 968 PEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVG 1047
Cdd:cd21104 9 DAQLTQTILDLVQQAANYKQLKKGANEATKTLNRGIAEFIVMAADAEPLEILLHLPLLCEDKNVPYVFVPSKQALGRACG 88
|
90 100 110
....*....|....*....|....*....|..
gi 1844115810 1048 IEVPCASAAII-NEG-ELRKELGSLVEKIKGL 1077
Cdd:cd21104 89 VSRPVIACSVTtNEGsQLKSQIQSLKDAIEKL 120
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
708-812 |
4.08e-25 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 708 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 787
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
|
90 100
....*....|....*....|....*
gi 1844115810 788 GATGHPGiIPPHATLVFDVELLKLE 812
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
472-585 |
3.86e-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: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 472 ESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNG--TLLVQSLHGVFKVKNTTTLQQHLIDG 549
Cdd:pfam00863 4 KSIAKGLRDYHHIASNLAALEYYCGDHKGEIHGICHGDKIITPAHLFKEACGndTLKIQSKHGLFDLEALDRQKIEELCG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844115810 550 RDMIIIRMPKDFPPFPQKLKFREPQREER----ICLVTTN 585
Cdd:pfam00863 84 QDIIVIKGPIDMPPAKMRLIFRAPIQCERavliGCRRDDN 123
|
|
| PRK13602 |
PRK13602 |
50S ribosomal protein L7ae-like protein; |
980-1058 |
1.52e-18 |
|
50S ribosomal protein L7ae-like protein;
Pssm-ID: 184174 [Multi-domain] Cd Length: 82 Bit Score: 81.37 E-value: 1.52e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115810 980 EKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPeIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAAII 1058
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 ... |
1341-1384 |
1.46e-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: 1.46e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1844115810 1341 STWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPA--MPDREVLY 1384
Cdd:pfam01006 1 STWVLVGGALAAGAAYCLTTGSVVVVGRWSVNGKPPavVPDREVLY 46
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
826-929 |
3.55e-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: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 826 DTSCTFPSS--DGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSAS----NFTNTN-NYFTSVPKNFMELLTNQE-AQQW 897
Cdd:pfam00863 131 DESAIFPLGkeNGGFWKHGCDTKLGDCGGPIIACDDMDIIGFHGGRlmqlGANNSLaHIFAALNDDFIEMFAEMEtAKGF 210
|
90 100 110
....*....|....*....|....*....|..
gi 1844115810 898 VSGWRLNADSVLWGGHKVFMVKPEEPFQPVKE 929
Cdd:pfam00863 211 QRKWKFNADKVEWGRLDLTSNQPSGAFKIQKL 242
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
173-393 |
1.42e-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: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 173 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 243
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 244 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 318
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 319 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 375
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
|
250 260
....*....|....*....|..
gi 1844115810 376 ----IGPQHQAGSDSLLTGMAF 393
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
|
|
| TEL1 |
COG5032 |
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms]; |
591-687 |
1.56e-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: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 591 SGSILWHEMWHEGLEEASRLYFGERN-VKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKD 669
Cdd:COG5032 1630 IAYPLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISL 1709
|
90
....*....|....*...
gi 1844115810 670 LLQAWDLYYHVFRRISKQ 687
Cdd:COG5032 1710 LNLSRKLYISVLRSIRKR 1727
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| POP2 |
COG5228 |
mRNA deadenylase subunit [RNA processing and modification]; |
155-434 |
3.82e-112 |
|
mRNA deadenylase subunit [RNA processing and modification];
Pssm-ID: 227553 Cd Length: 299 Bit Score: 355.00 E-value: 3.82e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 155 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 232
Cdd:COG5228 6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 233 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 312
Cdd:COG5228 86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 313 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 392
Cdd:COG5228 166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844115810 393 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 434
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 ... |
1152-1300 |
2.71e-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: 280.08 E-value: 2.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 1152 EGEVQIVSTATQTFLATCINGVCWAVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTR 1231
Cdd:pfam02907 1 EGEVQVLGTATQRFMGTCVNGVLWTTFHGAGSRTLAGPKGPVNQMYWSASDDVVGYPLPPGAGSLTPCTCGATDLYLVTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115810 1232 HADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETT 1300
Cdd:pfam02907 81 DGDLIPGRRRGDPRVSLLSPRPLSYLKGSSGGPILCPSGHVVGMFRAAVHSGGVVKAVRFVPWETLPTT 149
|
|
| cp |
PHA00026 |
coat protein |
5-133 |
6.65e-86 |
|
coat protein
Pssm-ID: 133846 Cd Length: 129 Bit Score: 275.38 E-value: 6.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 5 ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVELPVA 84
Cdd:PHA00026 1 AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQTVGGVELPGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1844115810 85 AWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY 133
Cdd:PHA00026 81 AWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY 129
|
|
| Levi_coat |
pfam01819 |
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ... |
6-132 |
9.65e-70 |
|
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: 9.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 6 SNFTQFVLVDNGGTGDVTVAPS----NFANGVAEWISSNSRSQAYK-VTCSVRQSSAQKRKYTIKVEVPKVATQTVGGVE 80
Cdd:pfam01819 1 AKFQAFTLSDIGGNGDVTLALNprgvNFANGVAALIEAGARPAAEKrVTCSVRQPSANNKKYKIKVEIPKPASCTAGGTC 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1844115810 81 LPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGI 132
Cdd:pfam01819 81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
|
|
| eL8_ribo |
TIGR03677 |
ribosomal protein eL8, archaeal form; This model specifically identifies the archaeal version ... |
962-1078 |
5.35e-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: 5.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 962 YVRFEVPEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKND 1041
Cdd:TIGR03677 1 YVKFEVPEELADKALEAVEKARETGKIKKGTNEVTKAVERGIAKLVVIAEDVEPPEIVAHLPALCEEKGIPYIYVKSKED 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844115810 1042 LGRAVGIEVPCASAAIINEGELRKELGSLVEKIKGLQ 1078
Cdd:TIGR03677 81 LGAAAGLEVGAASAAIVDAGKAEELLKEIIEKVEALK 117
|
|
| FRB_dom |
pfam08771 |
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ... |
593-685 |
7.37e-56 |
|
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: 7.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 593 SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLLQ 672
Cdd:pfam08771 6 AILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDEEDLNQ 85
|
90
....*....|...
gi 1844115810 673 AWDLYYHVFRRIS 685
Cdd:pfam08771 86 AWDIYYSVFRRIK 98
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
707-810 |
1.53e-43 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 153.41 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 707 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 786
Cdd:COG0545 1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....
gi 1844115810 787 YGATGHPGIIPPHATLVFDVELLK 810
Cdd:COG0545 80 YGERGAGGVIPPNSTLVFEVELLD 103
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
717-809 |
2.93e-42 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 149.65 E-value: 2.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 717 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 795
Cdd:pfam00254 1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
|
90
....*....|....
gi 1844115810 796 IPPHATLVFDVELL 809
Cdd:pfam00254 81 IPPNATLVFEVELL 94
|
|
| Ribosomal_L7Ae |
pfam01248 |
Ribosomal protein L7Ae/L30e/S12e/Gadd45 family; This family includes: Ribosomal L7A from ... |
974-1062 |
5.33e-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: 5.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 974 EALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCA 1053
Cdd:pfam01248 2 AIYEVLKKALKTGKLVLGLKEVTKALERGEAKLVIIAEDCDPEEKVKLIPALCKEKNVPYVKVPSKKELGEACGKKRPVS 81
|
....*....
gi 1844115810 1054 SAAIINEGE 1062
Cdd:pfam01248 82 ALAIKDEGD 90
|
|
| Rpl7Ae |
COG1358 |
Ribosomal protein L7Ae or related RNA K-turn-binding protein [Translation, ribosomal structure ... |
973-1067 |
3.40e-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: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 973 NEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDpPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGiEVPC 1052
Cdd:COG1358 1 DKILNLLGLARRAGKLVSGEEQVLKAIRKGKAKLVIIAEDAS-ENTKKKLLDLCEEYGVPVVEVGTKEELGKAIG-KVGR 78
|
90
....*....|....*...
gi 1844115810 1053 ASAAIINEG---ELRKEL 1067
Cdd:COG1358 79 AVVAITDEGfakKLLELL 96
|
|
| SNU13 |
cd21104 |
U4/U6.U5 small nuclear ribonucleoprotein SNU13; U4/U6.U5 small nuclear ribonucleoprotein SNU13, ... |
968-1077 |
1.59e-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: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 968 PEDMQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVG 1047
Cdd:cd21104 9 DAQLTQTILDLVQQAANYKQLKKGANEATKTLNRGIAEFIVMAADAEPLEILLHLPLLCEDKNVPYVFVPSKQALGRACG 88
|
90 100 110
....*....|....*....|....*....|..
gi 1844115810 1048 IEVPCASAAII-NEG-ELRKELGSLVEKIKGL 1077
Cdd:cd21104 89 VSRPVIACSVTtNEGsQLKSQIQSLKDAIEKL 120
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
708-812 |
4.08e-25 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 708 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 787
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
|
90 100
....*....|....*....|....*
gi 1844115810 788 GATGHPGiIPPHATLVFDVELLKLE 812
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
472-585 |
3.86e-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: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 472 ESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNG--TLLVQSLHGVFKVKNTTTLQQHLIDG 549
Cdd:pfam00863 4 KSIAKGLRDYHHIASNLAALEYYCGDHKGEIHGICHGDKIITPAHLFKEACGndTLKIQSKHGLFDLEALDRQKIEELCG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844115810 550 RDMIIIRMPKDFPPFPQKLKFREPQREER----ICLVTTN 585
Cdd:pfam00863 84 QDIIVIKGPIDMPPAKMRLIFRAPIQCERavliGCRRDDN 123
|
|
| PRK11570 |
PRK11570 |
peptidyl-prolyl cis-trans isomerase; Provisional |
706-811 |
7.99e-21 |
|
peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 183207 [Multi-domain] Cd Length: 206 Bit Score: 92.17 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 706 GVQVETISPGDGrTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKqeVIRGWEEGVAQMSVGQRAKLTISPDY 785
Cdd:PRK11570 103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
|
90 100
....*....|....*....|....*.
gi 1844115810 786 AYGATGHPGIIPPHATLVFDVELLKL 811
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELLEI 205
|
|
| PRK13602 |
PRK13602 |
50S ribosomal protein L7ae-like protein; |
980-1058 |
1.52e-18 |
|
50S ribosomal protein L7ae-like protein;
Pssm-ID: 184174 [Multi-domain] Cd Length: 82 Bit Score: 81.37 E-value: 1.52e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115810 980 EKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDPPeIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAAII 1058
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 ... |
1341-1384 |
1.46e-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: 1.46e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1844115810 1341 STWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPA--MPDREVLY 1384
Cdd:pfam01006 1 STWVLVGGALAAGAAYCLTTGSVVVVGRWSVNGKPPavVPDREVLY 46
|
|
| Peptidase_C4 |
pfam00863 |
Peptidase family C4; This peptidase is present in the nuclear inclusion protein of potyviruses. |
826-929 |
3.55e-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: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 826 DTSCTFPSS--DGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSAS----NFTNTN-NYFTSVPKNFMELLTNQE-AQQW 897
Cdd:pfam00863 131 DESAIFPLGkeNGGFWKHGCDTKLGDCGGPIIACDDMDIIGFHGGRlmqlGANNSLaHIFAALNDDFIEMFAEMEtAKGF 210
|
90 100 110
....*....|....*....|....*....|..
gi 1844115810 898 VSGWRLNADSVLWGGHKVFMVKPEEPFQPVKE 929
Cdd:pfam00863 211 QRKWKFNADKVEWGRLDLTSNQPSGAFKIQKL 242
|
|
| PTZ00365 |
PTZ00365 |
60S ribosomal protein L7Ae-like; Provisional |
988-1066 |
2.14e-13 |
|
60S ribosomal protein L7Ae-like; Provisional
Pssm-ID: 240382 Cd Length: 266 Bit Score: 71.80 E-value: 2.14e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115810 988 VKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGiEVPCASAAIINegeLRKE 1066
Cdd:PTZ00365 133 LKYGLNHVTDLVEYKKAKLVVIAHDVDPIELVCFLPALCRKKEVPYCIIKGKSRLGKLVH-QKTAAVVAIDN---VRKE 207
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
722-808 |
2.18e-12 |
|
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440668 [Multi-domain] Cd Length: 138 Bit Score: 65.89 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 722 KRGQTCVVHYTGMLEDGKKFDSSRDRnKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGatghpgiiPPHAT 801
Cdd:COG1047 2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPE 72
|
....*..
gi 1844115810 802 LVFDVEL 808
Cdd:COG1047 73 LVQTVPR 79
|
|
| PTZ00222 |
PTZ00222 |
60S ribosomal protein L7a; Provisional |
988-1047 |
9.69e-11 |
|
60S ribosomal protein L7a; Provisional
Pssm-ID: 140249 Cd Length: 263 Bit Score: 63.95 E-value: 9.69e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 988 VKKGTNETTKAVERGLAKLVYIAEDVDPPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVG 1047
Cdd:PTZ00222 133 VVTGLQEVTRAIEKKQARMVVIANNVDPVELVLWMPNLCRANKIPYAIVKDMARLGDAIG 192
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
173-393 |
1.42e-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: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 173 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 243
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 244 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 318
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 319 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 375
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
|
250 260
....*....|....*....|..
gi 1844115810 376 ----IGPQHQAGSDSLLTGMAF 393
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
|
|
| TEL1 |
COG5032 |
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms]; |
591-687 |
1.56e-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: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 591 SGSILWHEMWHEGLEEASRLYFGERN-VKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKD 669
Cdd:COG5032 1630 IAYPLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISL 1709
|
90
....*....|....*...
gi 1844115810 670 LLQAWDLYYHVFRRISKQ 687
Cdd:COG5032 1710 LNLSRKLYISVLRSIRKR 1727
|
|
| RPL30E |
COG1911 |
Ribosomal protein L30E [Translation, ribosomal structure and biogenesis]; Ribosomal protein ... |
979-1062 |
2.03e-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: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 979 LEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVdPPEIVAHLPLLCEEKNVP-YIYVKSKNDLGRAVGIEVPCASAAI 1057
Cdd:COG1911 8 LRDAVKTGKVVLGSKQTIKAIKLGKAKLVILAANC-PPEIREDIEYYAKLSNVPvYVYPGTSVELGALCGKPFRVSALAI 86
|
....*
gi 1844115810 1058 INEGE 1062
Cdd:COG1911 87 IDPGE 91
|
|
| PRK01018 |
PRK01018 |
50S ribosomal protein L30e; Reviewed |
979-1062 |
3.70e-08 |
|
50S ribosomal protein L30e; Reviewed
Pssm-ID: 179205 [Multi-domain] Cd Length: 99 Bit Score: 52.27 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 979 LEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVdPPEIVAHLPLLCEEKNVP-YIYVKSKNDLGRAVGIEVPCASAAI 1057
Cdd:PRK01018 8 LRVAVDTGKVILGSKRTIKAIKLGKAKLVIVASNC-PKDIKEDIEYYAKLSGIPvYEYEGSSVELGTLCGKPFTVSALAI 86
|
....*
gi 1844115810 1058 INEGE 1062
Cdd:PRK01018 87 VDPGE 91
|
|
| PRK13601 |
PRK13601 |
putative L7Ae-like ribosomal protein; Provisional |
991-1060 |
2.51e-07 |
|
putative L7Ae-like ribosomal protein; Provisional
Pssm-ID: 184173 Cd Length: 82 Bit Score: 49.59 E-value: 2.51e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844115810 991 GTNETTKAVERGLAKLVYIAEDVDPpEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAA-IINE 1060
Cdd:PRK13601 12 GAKQTLKAITNCNVLQVYIAKDAEE-HVTKKIKELCEEKSIKIVYIDTMKELGVMCGIDVGAAAAAdIIGE 81
|
|
| PRK15095 |
PRK15095 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
729-788 |
4.86e-06 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 237908 [Multi-domain] Cd Length: 156 Bit Score: 48.16 E-value: 4.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 729 VHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYG 788
Cdd:PRK15095 13 VHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG 72
|
|
| PRK06683 |
PRK06683 |
hypothetical protein; Provisional |
980-1059 |
1.38e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 136002 Cd Length: 82 Bit Score: 44.68 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 980 EKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDP--PEIVAHLPLlceEKNVPYIYVKSKNDLGRAVGIEVPCASAAI 1057
Cdd:PRK06683 4 QKVSNAENVVVGHKRTLEAIKNGIVKEVVIAEDADMrlTHVIIRTAL---QHNIPITKVESVRKLGKVAGIQVGASAIGI 80
|
..
gi 1844115810 1058 IN 1059
Cdd:PRK06683 81 IS 82
|
|
| PRK07714 |
PRK07714 |
YlxQ family RNA-binding protein; |
972-1065 |
1.49e-05 |
|
YlxQ family RNA-binding protein;
Pssm-ID: 236077 Cd Length: 100 Bit Score: 45.15 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 972 QNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDpPEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVP 1051
Cdd:PRK07714 3 MSDWKSFLGLANRARKVISGEELVLKEVRSGKAKLVLLSEDAS-VNTTKKITDKCTYYNVPMRKVENRQQLGHAIGKDER 81
|
90
....*....|....
gi 1844115810 1052 CAsAAIINEGELRK 1065
Cdd:PRK07714 82 VV-VAVLDEGFAKK 94
|
|
| PTZ00106 |
PTZ00106 |
60S ribosomal protein L30; Provisional |
979-1062 |
1.01e-04 |
|
60S ribosomal protein L30; Provisional
Pssm-ID: 185450 Cd Length: 108 Bit Score: 43.14 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 979 LEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVdPP------EIVAHLpllceEKNVPYIYVKSKNDLGRAVGIEVPC 1052
Cdd:PTZ00106 17 LQLVMKSGKYTLGTKSTLKALRNGKAKLVIISNNC-PPirrseiEYYAML-----SKTGVHHYAGNNNDLGTACGRHFRV 90
|
90
....*....|
gi 1844115810 1053 ASAAIINEGE 1062
Cdd:PTZ00106 91 SVMSITDAGD 100
|
|
| PRK13600 |
PRK13600 |
putative ribosomal protein L7Ae-like; Provisional |
991-1059 |
3.69e-04 |
|
putative ribosomal protein L7Ae-like; Provisional
Pssm-ID: 184172 Cd Length: 84 Bit Score: 40.60 E-value: 3.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844115810 991 GTNETTKAVERGLAKLVYIAEDVDPpEIVAHLPLLCEEKNVPYIYVKSKNDLGRAVGIEVPCASAAIIN 1059
Cdd:PRK13600 17 GLKETLKALKKDQVTSLIIAEDVEV-YLMTRVLSQINQKNIPVSFFKSKHALGKHVGINVNATIVALIK 84
|
|
| PRK05583 |
PRK05583 |
ribosomal protein L7Ae family protein; Provisional |
971-1047 |
7.94e-04 |
|
ribosomal protein L7Ae family protein; Provisional
Pssm-ID: 235517 Cd Length: 104 Bit Score: 40.42 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844115810 971 MQNEALSLLEKVRESGKVKKGTNETTKAVERGLAKLVYIAEDVDP---PEIVAHlpllCEEKNVPYIYVKSKNDLGRAVG 1047
Cdd:PRK05583 1 MMNKFLNFLGLTKKAGKLLEGYNKCEEAIKKKKVYLIIISNDISEnskNKFKNY----CNKYNIPYIEGYSKEELGNAIG 76
|
|
| |
