NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|850990485|ref|WP_048060945|]
View 

serine protein kinase RIO [Methanothermobacter thermautotrophicus]

Protein Classification

serine protein kinase RIO( domain architecture ID 11448151)

serine protein kinase RIO is an atypical protein kinase that catalyzes the ATP-dependent phosphorylation of serine residues in substrate proteins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
22-269 7.56e-120

Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];


:

Pssm-ID: 441324  Cd Length: 252  Bit Score: 342.55  E-value: 7.56e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  22 RVDSDLGRMEavKRLKGVEDRRVGSEVFDELTLKTLYKLANSGYLAVLNGAVSTGKEANVFKGITDTDDFVAVKIYRVAT 101
Cdd:COG1718    5 RLDREIDKLR--KRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGGELVAAKIYRTAT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 102 SDFKKMQYYIQGDPRF-KVRTTNRRQLVQAWVNKEFRNLKRALEAGVRVPEPVTARDNVLIMEFIGKDGVPAPTMRDAP- 179
Cdd:COG1718   83 SSFKRMAQYIEGDPRFmGKGSFGRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLKDVEl 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 180 -PEDPEEALETIIEYMHRLYKgARLVHGDLSFFNILNHCGEPVIIDVSQAMVLDHPLAGELLERDIENIIRDFRRIGVSV 258
Cdd:COG1718  163 ePEEAEELYEQLIEYIVRLYK-AGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARFGPEL 241

                        250
                 ....*....|.
gi 850990485 259 SADYIRERITG 269
Cdd:COG1718  242 DPEELLKEIWA 252
 
Name Accession Description Interval E-value
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
22-269 7.56e-120

Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];


Pssm-ID: 441324  Cd Length: 252  Bit Score: 342.55  E-value: 7.56e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  22 RVDSDLGRMEavKRLKGVEDRRVGSEVFDELTLKTLYKLANSGYLAVLNGAVSTGKEANVFKGITDTDDFVAVKIYRVAT 101
Cdd:COG1718    5 RLDREIDKLR--KRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGGELVAAKIYRTAT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 102 SDFKKMQYYIQGDPRF-KVRTTNRRQLVQAWVNKEFRNLKRALEAGVRVPEPVTARDNVLIMEFIGKDGVPAPTMRDAP- 179
Cdd:COG1718   83 SSFKRMAQYIEGDPRFmGKGSFGRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLKDVEl 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 180 -PEDPEEALETIIEYMHRLYKgARLVHGDLSFFNILNHCGEPVIIDVSQAMVLDHPLAGELLERDIENIIRDFRRIGVSV 258
Cdd:COG1718  163 ePEEAEELYEQLIEYIVRLYK-AGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARFGPEL 241

                        250
                 ....*....|.
gi 850990485 259 SADYIRERITG 269
Cdd:COG1718  242 DPEELLKEIWA 252
RIO smart00090
RIO-like kinase;
38-269 3.87e-112

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 322.71  E-value: 3.87e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485    38 GVEDRRVGSEVFDELTLKTLYKLANSGYLAVLNGAVSTGKEANVFKG--ITDTDDFVAVKIYRVATSDFKKMQYYIQGDP 115
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHAldFDGSGKERAVKIYRTGTLEFKRRDRYVDGDF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485   116 RFKVRTTNRRQLVQAWVNKEFRNLKRALEAGVRVPEPVTARDNVLIMEFIGKDGVPAPTMRDAPPEDPE--EALETIIEY 193
Cdd:smart00090  81 RFKYRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEEefELYDDILEE 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 850990485   194 MHRLYKGARLVHGDLSFFNILNHCGEPVIIDVSQAMVLDHPLAGELLERDIENIIRDFRRIGVSV-SADYIRERITG 269
Cdd:smart00090 161 MRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDElDEEELFERITG 237
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
 69-253 3.48e-110

Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar proteins; RIO1 is present in archaea, bacteria and eukaryotes. In addition, RIO3 is present in multicellular eukaryotes. Both RIO1 and RIO3 are associated with precursors of 40S ribosomal subunits, just like RIO2. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. The specific function of RIO3 is unknown. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270696 [Multi-domain]  Cd Length: 189  Bit Score: 315.65  E-value: 3.48e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  69 LNGAVSTGKEANVFKGITDTDDFVAVKIYRVATSDFKKMQYYIQGDPRFKVRTT-NRRQLVQAWVNKEFRNLKRALEAGV 147
Cdd:cd05145    1 LGGVISTGKEANVYLARGGDGEPVAVKIYRTSTSSFKKMAKYIEGDPRFESRRRgNRRKLIFAWARKEFRNLKRLYEAGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 148 RVPEPVTARDNVLIMEFIGKDGVPAPTMRDAP--PEDPEEALETIIEYMHRLYKGARLVHGDLSFFNILNHCGEPVIIDV 225
Cdd:cd05145   81 RVPEPIAVYRNVLVMEFIGDDGSPAPRLKDVEleEEDAEELYEQVVEQMRRMYCKAGLVHGDLSEYNILYYDGKPVIIDV 160

                        170       180
                 ....*....|....*....|....*...
gi 850990485 226 SQAMVLDHPLAGELLERDIENIIRDFRR 253
Cdd:cd05145  161 SQAVTLDHPNAEEFLRRDIRNINRFFSR 188
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 80-258 2.88e-91

RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria and eukaryotes. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined.


Pssm-ID: 460091 [Multi-domain]  Cd Length: 184  Bit Score: 267.56  E-value: 2.88e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485   80 NVFKGITDTDDFVAVKIYRVATSDFKKMQYYIQGDPRFKVRTTNRRQLVQAWVNKEFRNLKRALEAGVRVPEPVTARDNV 159
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFRDRKTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNRHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  160 LIMEFIGKDGVPAPTMRDAPPEDPEEALETIIEYMHRLYKGARLVHGDLSFFNILNHCGEPVIIDVSQAMVLDHPLAGEL 239
Cdd:pfam01163  81 LVMEFIGKDGVPAPKLKDVELEEAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIIDVPQAVETDHPNALEF 160

                         170
                  ....*....|....*....
gi 850990485  240 LERDIENIIRDFRRIGVSV 258
Cdd:pfam01163 161 LERDVENIINFFRRKGVDE 179
PRK14879 PRK14879
Kae1-associated kinase Bud32;
134-224 9.75e-08

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 51.06  E-value: 9.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 134 KEFRNLKRALEAGVRVPEP--VTARDNVLIMEFIgkDGVPAPTMRDAPPEDPEEALETIIEYMHRLYKgARLVHGDLSFF 211
Cdd:PRK14879  48 REARIMSRARKAGVNVPAVyfVDPENFIIVMEYI--EGEPLKDLINSNGMEELELSREIGRLVGKLHS-AGIIHGDLTTS 124

                         90
                 ....*....|...
gi 850990485 212 NILNHCGEPVIID 224
Cdd:PRK14879 125 NMILSGGKIYLID 137
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 134-224 4.96e-07

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 49.13  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  134 KEFRNLKRALEAGVRVPEP--VTARDNVLIMEFIgkdgvPAPTMRDAPPEDPEEALETIIEYMHRLYKgARLVHGDLSFF 211
Cdd:TIGR03724  46 REARLLSRARKAGVNTPVIydVDPDNKTIVMEYI-----EGKPLKDVIEENGDELAREIGRLVGKLHK-AGIVHGDLTTS 119

                          90
                  ....*....|...
gi 850990485  212 NILNHCGEPVIID 224
Cdd:TIGR03724 120 NIIVRDDKVYLID 132
 
Name Accession Description Interval E-value
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
22-269 7.56e-120

Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];


Pssm-ID: 441324  Cd Length: 252  Bit Score: 342.55  E-value: 7.56e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  22 RVDSDLGRMEavKRLKGVEDRRVGSEVFDELTLKTLYKLANSGYLAVLNGAVSTGKEANVFKGITDTDDFVAVKIYRVAT 101
Cdd:COG1718    5 RLDREIDKLR--KRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGGELVAAKIYRTAT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 102 SDFKKMQYYIQGDPRF-KVRTTNRRQLVQAWVNKEFRNLKRALEAGVRVPEPVTARDNVLIMEFIGKDGVPAPTMRDAP- 179
Cdd:COG1718   83 SSFKRMAQYIEGDPRFmGKGSFGRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLKDVEl 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 180 -PEDPEEALETIIEYMHRLYKgARLVHGDLSFFNILNHCGEPVIIDVSQAMVLDHPLAGELLERDIENIIRDFRRIGVSV 258
Cdd:COG1718  163 ePEEAEELYEQLIEYIVRLYK-AGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARFGPEL 241

                        250
                 ....*....|.
gi 850990485 259 SADYIRERITG 269
Cdd:COG1718  242 DPEELLKEIWA 252
RIO smart00090
RIO-like kinase;
38-269 3.87e-112

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 322.71  E-value: 3.87e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485    38 GVEDRRVGSEVFDELTLKTLYKLANSGYLAVLNGAVSTGKEANVFKG--ITDTDDFVAVKIYRVATSDFKKMQYYIQGDP 115
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHAldFDGSGKERAVKIYRTGTLEFKRRDRYVDGDF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485   116 RFKVRTTNRRQLVQAWVNKEFRNLKRALEAGVRVPEPVTARDNVLIMEFIGKDGVPAPTMRDAPPEDPE--EALETIIEY 193
Cdd:smart00090  81 RFKYRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEEefELYDDILEE 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 850990485   194 MHRLYKGARLVHGDLSFFNILNHCGEPVIIDVSQAMVLDHPLAGELLERDIENIIRDFRRIGVSV-SADYIRERITG 269
Cdd:smart00090 161 MRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDElDEEELFERITG 237
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
 69-253 3.48e-110

Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar proteins; RIO1 is present in archaea, bacteria and eukaryotes. In addition, RIO3 is present in multicellular eukaryotes. Both RIO1 and RIO3 are associated with precursors of 40S ribosomal subunits, just like RIO2. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. The specific function of RIO3 is unknown. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270696 [Multi-domain]  Cd Length: 189  Bit Score: 315.65  E-value: 3.48e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  69 LNGAVSTGKEANVFKGITDTDDFVAVKIYRVATSDFKKMQYYIQGDPRFKVRTT-NRRQLVQAWVNKEFRNLKRALEAGV 147
Cdd:cd05145    1 LGGVISTGKEANVYLARGGDGEPVAVKIYRTSTSSFKKMAKYIEGDPRFESRRRgNRRKLIFAWARKEFRNLKRLYEAGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 148 RVPEPVTARDNVLIMEFIGKDGVPAPTMRDAP--PEDPEEALETIIEYMHRLYKGARLVHGDLSFFNILNHCGEPVIIDV 225
Cdd:cd05145   81 RVPEPIAVYRNVLVMEFIGDDGSPAPRLKDVEleEEDAEELYEQVVEQMRRMYCKAGLVHGDLSEYNILYYDGKPVIIDV 160

                        170       180
                 ....*....|....*....|....*...
gi 850990485 226 SQAMVLDHPLAGELLERDIENIIRDFRR 253
Cdd:cd05145  161 SQAVTLDHPNAEEFLRRDIRNINRFFSR 188
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 80-258 2.88e-91

RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria and eukaryotes. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined.


Pssm-ID: 460091 [Multi-domain]  Cd Length: 184  Bit Score: 267.56  E-value: 2.88e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485   80 NVFKGITDTDDFVAVKIYRVATSDFKKMQYYIQGDPRFKVRTTNRRQLVQAWVNKEFRNLKRALEAGVRVPEPVTARDNV 159
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFRDRKTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNRHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  160 LIMEFIGKDGVPAPTMRDAPPEDPEEALETIIEYMHRLYKGARLVHGDLSFFNILNHCGEPVIIDVSQAMVLDHPLAGEL 239
Cdd:pfam01163  81 LVMEFIGKDGVPAPKLKDVELEEAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIIDVPQAVETDHPNALEF 160

                         170
                  ....*....|....*....
gi 850990485  240 LERDIENIIRDFRRIGVSV 258
Cdd:pfam01163 161 LERDVENIINFFRRKGVDE 179
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 69-253 6.22e-67

Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is present in archaea, bacteria and eukaryotes. This subfamily is composed of RIO1 proteins from eukaryotes. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. It is associated with precursors of 40S ribosomal subunits, just like RIO2. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270698  Cd Length: 190  Bit Score: 206.27  E-value: 6.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  69 LNGAVSTGKEANVFKGITDTDDFVAVKIYRVATSDFKKMQYYIQGDPRFK--VRTTNRRQLVQAWVNKEFRNLKRALEAG 146
Cdd:cd05147    1 INGCISTGKEANVYHATTKNGGELAIKVYKTSILVFKDRDKYVSGEFRFRhgYCKHNPRKMVKTWAEKEMRNLKRLNQAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 147 VRVPEPVTARDNVLIMEFIGKDGVPAPTMRDAPPEDPE--EALETIIEYMHRLYKGARLVHGDLSFFNILNHCGEPVIID 224
Cdd:cd05147   81 IPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKwrELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYIID 160

                        170       180
                 ....*....|....*....|....*....
gi 850990485 225 VSQAMVLDHPLAGELLERDIENIIRDFRR 253
Cdd:cd05147  161 VSQSVEHDHPHALEFLRRDCVNVNDFFRK 189
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 69-253 1.08e-54

Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in multicellular eukaryotes. It is associated with precursors of 40S ribosomal subunits, just like RIO1 and RIO2. Its specific function is still unknown. Like RIO1 and RIO2, it may be involved in ribosomal subunit processing and maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO3 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270697  Cd Length: 196  Bit Score: 175.25  E-value: 1.08e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  69 LNGAVSTGKEANVFKGITDTDDFV------AVKIYRVATSDFKKMQYYIQGDPRFKVRTT--NRRQLVQAWVNKEFRNLK 140
Cdd:cd05146    1 VNGCISTGKEAVVFHANGGSMEEVllppecAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSkqNPRKIIRLWAEKEMHNLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 141 RALEAGVRVPEPVTARDNVLIMEFIGKDGVPAPTMRDA--PPEDPEEALETIIEYMHRLYKGARLVHGDLSFFNILNHCG 218
Cdd:cd05146   81 RMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAklSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNILWHEG 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 850990485 219 EPVIIDVSQAMVLDHPLAGELLERDIENIIRDFRR 253
Cdd:cd05146  161 KVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQK 195
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
 69-253 1.41e-46

Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical protein serine kinases present in archaea, bacteria and eukaryotes. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. RIO kinases contain a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. Most organisms contain at least two RIO kinases, RIO1 and RIO2. A third protein, RIO3, is present in multicellular eukaryotes. In yeast, RIO1 and RIO2 are essential for survival. They function as non-ribosomal factors necessary for late 18S rRNA processing. RIO1 is also required for proper cell cycle progression and chromosome maintenance. The biological substrates for RIO kinases are still unknown. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270689  Cd Length: 192  Bit Score: 154.41  E-value: 1.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  69 LNGAVSTGKEANVFKGITDTDD---FVAVKIYRVATSDFKKMQYYIQGDPRFKVRTTNRRQLVQAWVNKEFRNLKRALEA 145
Cdd:cd05119    1 IGGVISTGKEANVFYADGVFDGkpvACAVKIYRIETSEFDKVDEYLYGDERFDYRRISPKEKVFIWTEKEFRNLERAKEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 146 GVRVPEPVTARDNVLIMEFIGKDGVPAPTM----RDAPPEDPEEALETIIEYMHRLYKGARLVHGDLSFFNILnHCGEPV 221
Cdd:cd05119   81 GVSVPQPYTYEKNVLL*EFIGEDELPAPTLvelgRELKELDVEGIFNDVVENVKRLYQEAELVHADLSEYNIL-YIDKVY 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 850990485 222 IIDVSQAMVLDHPLAGELLERDIENIIRDFRR 253
Cdd:cd05119  160 FIDFGQAVTLRHPGAESYLERDVRNIIRFFSK 191
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 76-253 2.62e-35

C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270695 [Multi-domain]  Cd Length: 183  Bit Score: 124.92  E-value: 2.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  76 GKEANVFKGITDTDDFVAVKIYRVATSDFKKMQY---YIQgdprfkvrttNRRQLvqAWVN-------KEFRNLKRALEA 145
Cdd:cd05144   11 GKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRkrdYLK----------HRKHA--SWLYlsrlaaeKEFAALKALYEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 146 GVRVPEPVTARDNVLIMEFIgkDGVPAPTMRDapPEDPEEALETIIEYMHRLYKGArLVHGDLSFFNIL-NHCGEPVIID 224
Cdd:cd05144   79 GFPVPKPIDWNRHAVVMELI--DGYPLYQVRL--LEDPEEVLDEILELIVKLAKHG-LIHGDFSEFNILvDEDEKITVID 153

                        170       180
                 ....*....|....*....|....*....
gi 850990485 225 VSQAMVLDHPLAGELLERDIENIIRDFRR 253
Cdd:cd05144  154 FPQMVSTSHPNAEEYFDRDVECIIKFFRR 182
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 92-269 2.41e-33

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 119.63  E-value: 2.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  92 VAVKIYRVATSDFKKMQYYIQGDPRFKVRTTNRrqlVQAWvnKEFRNLKRALEAGVRVPEPVTARDNVLIMEFIgkDGVP 171
Cdd:COG0478   11 VALKFHREGRTSFRKVRRERADKEHYSWLYAAR---TRAE--REFRALERLYPAGLPVPRPIAANRHAIVMERI--EGVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 172 aptMRDAPPEDPEEALETIIEYMHRLYKgARLVHGDLSFFNIL-NHCGEPVIIDVSQAMVLDHPLAGELLERDIENIIRD 250
Cdd:COG0478   84 ---LARLKLEDPEEVLDKILEEIRRAHD-AGIVHADLSEYNILvDDDGGVWIIDWPQAVPRDHPNAEELLERDLENLLRS 159

                        170       180
                 ....*....|....*....|
gi 850990485 251 FRRI-GVSVSADYIRERITG 269
Cdd:COG0478  160 FRKKyGLEVDLDEVWAALLG 179
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 134-269 5.65e-12

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 62.28  E-value: 5.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 134 KEFRNLKRALEAGVRVPEP--VTARDNVLIMEFIgkdgvPAPTMRDAP--PEDPEEALETIIEYMHRLYKgARLVHGDLS 209
Cdd:COG3642    5 REARLLRELREAGVPVPKVldVDPDDADLVMEYI-----EGETLADLLeeGELPPELLRELGRLLARLHR-AGIVHGDLT 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 210 FFNILNHCGEPVIIDVSQAMVLDHPlagELLERDIENIIRDFRRIGVSVSADYIRERITG 269
Cdd:COG3642   79 TSNILVDDGGVYLIDFGLARYSDPL---EDKAVDLAVLKRSLESTHPDPAEELWEAFLEG 135
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 120-214 2.58e-08

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 51.67  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 120 RTTNRRQLVQAWVNKEFRNLKRALEAGVRVPEPVTARD----NVLIMEFIGKDGVPAPTMRDAPPE-DPEEALETIIEYM 194
Cdd:cd13968   25 IGDDVNNEEGEDLESEMDILRRLKGLELNIPKVLVTEDvdgpNILLMELVKGGTLIAYTQEEELDEkDVESIMYQLAECM 104

                         90       100
                 ....*....|....*....|
gi 850990485 195 HRLYKgARLVHGDLSFFNIL 214
Cdd:cd13968  105 RLLHS-FHLIHRDLNNDNIL 123
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
41-228 2.71e-08

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 53.10  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  41 DRRVGSEVFDELTLKTLYKLANSGYLAVLNGAVSTGKEANVFKGITDTDDfVAVKIYRvatSDFKKmqyyiqgdPRFKvr 120
Cdd:COG2112   16 SESELEERLEELKSLGITSIYSGGTLIGGLRLLGKGYRGVVFLGKLGGKK-VALKIRR---TDSPR--------PSLK-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 121 ttnrrqlvqawvnKEFRNLKRALEAGVrVPEPVTARDNVLIMEFIgkDGVP-APTMRDAPPEDPEEALETIIEYMHRLYK 199
Cdd:COG2112   82 -------------KEAEILKKANGAGV-GPKLYDYGRDFLVMEYI--EGEPlKDWLENLDKEELRKVIRELLEAAYLLDR 145

                        170       180       190
                 ....*....|....*....|....*....|.
gi 850990485 200 gARLVHGDLSFF--NILNHCGEPVIIDVSQA 228
Cdd:COG2112  146 -IGIDHGELSRPgkHVIVDKGRPYIIDFESA 175
PRK14879 PRK14879
Kae1-associated kinase Bud32;
134-224 9.75e-08

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 51.06  E-value: 9.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 134 KEFRNLKRALEAGVRVPEP--VTARDNVLIMEFIgkDGVPAPTMRDAPPEDPEEALETIIEYMHRLYKgARLVHGDLSFF 211
Cdd:PRK14879  48 REARIMSRARKAGVNVPAVyfVDPENFIIVMEYI--EGEPLKDLINSNGMEELELSREIGRLVGKLHS-AGIIHGDLTTS 124

                         90
                 ....*....|...
gi 850990485 212 NILNHCGEPVIID 224
Cdd:PRK14879 125 NMILSGGKIYLID 137
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 134-224 4.96e-07

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 49.13  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  134 KEFRNLKRALEAGVRVPEP--VTARDNVLIMEFIgkdgvPAPTMRDAPPEDPEEALETIIEYMHRLYKgARLVHGDLSFF 211
Cdd:TIGR03724  46 REARLLSRARKAGVNTPVIydVDPDNKTIVMEYI-----EGKPLKDVIEENGDELAREIGRLVGKLHK-AGIVHGDLTTS 119

                          90
                  ....*....|...
gi 850990485  212 NILNHCGEPVIID 224
Cdd:TIGR03724 120 NIIVRDDKVYLID 132
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
76-233 7.47e-07

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 49.89  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  76 GKEANVFKGITDTDDFV----AVKIYRVATSDFKkmqyyiqgdprfkVRTTNRRqlvqawvnKEFRNLKRALEAGVRVP- 150
Cdd:PRK09605 344 GAEADIKKGEYLGRDAVikerVPKGYRHPELDER-------------LRTERTR--------AEARLLSEARRAGVPTPv 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 151 -EPVTARDNVLIMEFIGkdgvpAPTMRDAPPEDPE--EALETIIEYMHRlykgARLVHGDLSFFNILNHCGEPVIIDVSQ 227
Cdd:PRK09605 403 iYDVDPEEKTIVMEYIG-----GKDLKDVLEGNPElvRKVGEIVAKLHK----AGIVHGDLTTSNFIVRDDRLYLIDFGL 473


                 ....*.
gi 850990485 228 AMVLDH 233
Cdd:PRK09605 474 GKYSDL 479
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
 135-264 2.54e-04

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 428872  Cd Length: 206  Bit Score: 41.22  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485  135 EFRNLKRALEAGVRVPEPVTA--------RDNVLIME----------FIGKDGVPAPTMRDAppedPEEALETIIEYMHR 196
Cdd:pfam06293  60 EFRLIRRLREAGLPVPKPVAAgevkvgggYRADLLTErlegaqsladWLADWAVPSGELRRA----IWEAVGRLIRQMHR 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 850990485  197 lykgARLVHGDLSFFNILNHCGEPviiDVSQAMVLDHPLAGELL------ERDIENIIRDFRRIGVSvSADYIR 264
Cdd:pfam06293 136 ----AGVQHGDLYAHHILLQQEGD---EGFEAWLIDLDKGRLRLparrwrNKDLARLLRSFLNIGFT-EADWER 201
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
 134-214 4.88e-04

Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This subfamily is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Subfamily 13 (ABC1K13) of plant ABC1 kinases belongs in this subfamily with yeast Abc1p and human ADCK3. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270872 [Multi-domain]  Cd Length: 251  Bit Score: 40.57  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 134 KEFRNLKRAlEAGVRVPEPVTA--RDNVLIMEFIgkDGVPAPTMRDAPPEDPEEALETIIEYMHRLYKGARLVHGDLSFF 211
Cdd:cd13970  122 RRFRELLAD-DPRFVVPEVIPElsTKRVLTTEFV--DGVPLDEAADLSQEERNRIGELLLRLCLRELFEFGFMQTDPNPG 198


                 ...
gi 850990485 212 NIL 214
Cdd:cd13970  199 NFL 201
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
 133-224 1.18e-03

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 39.40  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850990485 133 NKEFRNLKR-----ALEAGVRVPEPVT--ARDNVLIMEFIgkDGVP--APTMRDAPPEDPEEALETIIE-YMHRLYKgAR 202
Cdd:cd05121  114 RREARNAERfrknlKDSPDVYVPKVYPelSTRRVLVMEYI--DGVKltDLEALRAAGIDRKELARRLVDaYLKQIFE-DG 190

                         90       100
                 ....*....|....*....|...
gi 850990485 203 LVHGDLSFFNIL-NHCGEPVIID 224
Cdd:cd05121  191 FFHADPHPGNILvLPDGRIALLD 213
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH