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Conserved domains on  [gi|229331967|ref|NP_060813|]
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serine/threonine-protein kinase RIO2 isoform 1 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase RIO2( domain architecture ID 10557840)

serine/threonine-protein kinase RIO2 is an atypical serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit

CATH:  1.10.510.10
EC:  2.7.11.1
Gene Symbol:  RIOK2
Gene Ontology:  GO:0005524|GO:0004674|GO:0006468
PubMed:  16183636|16182620|19614568|16244704

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 94-276 7.47e-130

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: 376.46  E-value: 7.47e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  94 VESVGNQMGVGKESDIYIVANEEGQQFALKLHRLGRTSFRNLKNKRDYHKHRHNVSWLYLSRLSAMKEFAYMKALYERKF 173
Cdd:cd05144    1 ISSVGNQIGVGKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRKRDYLKHRKHASWLYLSRLAAEKEFAALKALYEEGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 174 PVPKPIDYNRHAVVMELINGYPLCQIHHVEDPASVYDEAMELIVKLANHGLIHGDFNEFNLILDESDHITMIDFPQMVST 253
Cdd:cd05144   81 PVPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDEDEKITVIDFPQMVST 160

                        170       180
                 ....*....|....*....|...
gi 229331967 254 SHPNAEWYFDRDVKCIKDFFMKR 276
Cdd:cd05144  161 SHPNAEEYFDRDVECIIKFFRRK 183
Rio2_N pfam09202
Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to ...
 9-91 7.63e-40

Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to the winged helix (wHTH) domain. They adopt a structure consisting of four alpha helices followed by two beta strands and a fifth alpha helix. The domain confers DNA binding properties to the protein, as per other winged helix domains.


:

Pssm-ID: 462715  Cd Length: 82  Bit Score: 139.61  E-value: 7.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967    9 LRYMSRDDFRVLTAVEMGMKNHEIVPGSLIASIASLKHGGCNKVLRELVKHKLIAwERTKTVQGYRLTNAGYDYLALKTL 88
Cdd:pfam09202   1 MRYLSKEDFRVLTAVEMGMRNHEVVPTELITSISRLRHGGVNKRLSRLAKRKLIS-RKNAKYDGYRLTYLGYDYLALRTL 79


                  ...
gi 229331967   89 SSR 91
Cdd:pfam09202  80 VKR 82
 
Name Accession Description Interval E-value
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 94-276 7.47e-130

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: 376.46  E-value: 7.47e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  94 VESVGNQMGVGKESDIYIVANEEGQQFALKLHRLGRTSFRNLKNKRDYHKHRHNVSWLYLSRLSAMKEFAYMKALYERKF 173
Cdd:cd05144    1 ISSVGNQIGVGKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRKRDYLKHRKHASWLYLSRLAAEKEFAALKALYEEGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 174 PVPKPIDYNRHAVVMELINGYPLCQIHHVEDPASVYDEAMELIVKLANHGLIHGDFNEFNLILDESDHITMIDFPQMVST 253
Cdd:cd05144   81 PVPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDEDEKITVIDFPQMVST 160

                        170       180
                 ....*....|....*....|...
gi 229331967 254 SHPNAEWYFDRDVKCIKDFFMKR 276
Cdd:cd05144  161 SHPNAEEYFDRDVECIIKFFRRK 183
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 108-280 2.79e-75

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: 236.36  E-value: 2.79e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  108 DIYIVANEEGQQFALKLHRLGRTSFRNLKNKRDYHKHR--HNVSWLYLSRLSAMKEFAYMKALYERKFPVPKPIDYNRHA 185
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFrdRKTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNRHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  186 VVMELI--NGYPLCQIHHV--EDPASVYDEAM-ELIVKLANHGLIHGDFNEFNLILDEsDHITMIDFPQMVSTSHPNAEW 260
Cdd:pfam01163  81 LVMEFIgkDGVPAPKLKDVelEEAEEIYDEIIrEMRRLYQEAGLVHGDLSEYNILVHD-DKPVIIDVPQAVETDHPNALE 159

                         170       180
                  ....*....|....*....|
gi 229331967  261 YFDRDVKCIKDFFMKRFSYE 280
Cdd:pfam01163 160 FLERDVENIINFFRRKGVDE 179
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 115-293 5.24e-56

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: 186.26  E-value: 5.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 115 EEGQQFALKLHRLGRTSFRNLKNKRDYHKHrhnVSWLYLSRLSAMKEFAYMKALYERKFPVPKPIDYNRHAVVMELINGY 194
Cdd:COG0478    6 PGGGPVALKFHREGRTSFRKVRRERADKEH---YSWLYAARTRAEREFRALERLYPAGLPVPRPIAANRHAIVMERIEGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 195 PLCQIHhVEDPASVYDEAMELIVKLANHGLIHGDFNEFNLILDESDHITMIDFPQMVSTSHPNAEWYFDRDVKCIKDFFM 274
Cdd:COG0478   83 ELARLK-LEDPEEVLDKILEEIRRAHDAGIVHADLSEYNILVDDDGGVWIIDWPQAVPRDHPNAEELLERDLENLLRSFR 161

                        170
                 ....*....|....*....
gi 229331967 275 KRFSYESELFPTFKDIRRE 293
Cdd:COG0478  162 KKYGLEVDLDEVWAALLGG 180
RIO smart00090
RIO-like kinase;
72-280 1.35e-53

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 181.73  E-value: 1.35e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967    72 GYRLTNAGYDYLALKTLSSRQVVESVGNQMGVGKESDIY--IVANEEGQQFALKLHRLGRTSFRNLKNKRDYHK--HRHN 147
Cdd:smart00090   7 TYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYhaLDFDGSGKERAVKIYRTGTLEFKRRDRYVDGDFrfKYRK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967   148 VSWLYLSRLSAMKEFAYMKALYERKFPVPKPIDYNRHAVVMELI--NGYPLCQIHHV----EDPASVYDEAMELIVKLAN 221
Cdd:smart00090  87 INPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIggDGLPAPRLKDVepeeEEEFELYDDILEEMRKLYK 166

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967   222 HG-LIHGDFNEFNLILDEsDHITMIDFPQMVSTSHPNAEWYFDRDVKCIKDFFMKRFSYE 280
Cdd:smart00090 167 EGeLVHGDLSEYNILVHD-GKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDE 225
Rio2_N pfam09202
Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to ...
 9-91 7.63e-40

Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to the winged helix (wHTH) domain. They adopt a structure consisting of four alpha helices followed by two beta strands and a fifth alpha helix. The domain confers DNA binding properties to the protein, as per other winged helix domains.


Pssm-ID: 462715  Cd Length: 82  Bit Score: 139.61  E-value: 7.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967    9 LRYMSRDDFRVLTAVEMGMKNHEIVPGSLIASIASLKHGGCNKVLRELVKHKLIAwERTKTVQGYRLTNAGYDYLALKTL 88
Cdd:pfam09202   1 MRYLSKEDFRVLTAVEMGMRNHEVVPTELITSISRLRHGGVNKRLSRLAKRKLIS-RKNAKYDGYRLTYLGYDYLALRTL 79


                  ...
gi 229331967   89 SSR 91
Cdd:pfam09202  80 VKR 82
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
 150-247 1.06e-11

3-deoxy-D-manno-octulosonic-acid kinase; Reviewed


Pssm-ID: 234975  Cd Length: 239  Bit Score: 64.90  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 150 WLYLSRLSAMKEFAYMKALYERKFPVPKPI--DYNRH------AVVMElingyplcQIHHVEDPASVYDEAM-------- 213
Cdd:PRK01723  79 FTGLERTRAFAEFRLLAQLYEAGLPVPRPIaaRVVRHglfyraDILIE--------RIEGARDLVALLQEAPlseeqwqa 150

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 229331967 214 --ELIVKLANHGLIHGDFNEFNLILDESDHITMIDF 247
Cdd:PRK01723 151 igQLIARFHDAGVYHADLNAHNILLDPDGKFWLIDF 186
prot_kin_PA4780 NF041645
PA4780 family RIO1-like protein kinase; Members of this family are putative serine ...
 175-273 1.19e-10

PA4780 family RIO1-like protein kinase; Members of this family are putative serine/threonine-protein kinases, closely related to founding member PA4780 from Pseudomonas aeruginosa PAO1, which was shown to be upregulated by and important for the biodegradation of phenanthrene and naphthalene. Members belong more generally to the RIO1 atypical kinase family (see PF01163).


Pssm-ID: 469527  Cd Length: 274  Bit Score: 62.27  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 175 VPKPIDYNRHAVVMELI---NGYPLCQIHHV---EDPASVYDEAM-ELIVKLANHGLIHGDFNEFNLILDeSDHITMIDF 247
Cdd:NF041645 108 VPQPYGFFDGVLLMELVtdeEGDAAPRLNDVsltPEQAREYHALLiRYVVRMLCAGLVHGDLSEFNVLVD-ADGPVIIDL 186

                         90       100
                 ....*....|....*....|....*..
gi 229331967 248 PQMVS-TSHPNAEWYFDRDVKCIKDFF 273
Cdd:NF041645 187 PQAVDaAGNNNARRMLERDVNNLAAYF 213
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 160-247 1.52e-05

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: 46.05  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  160 KEFAYMKALYERKFPVPKP--IDYNRHAVVMELINGYPLCQIHHvEDPASVYDEAMELIVKLANHGLIHGDFNEFNLILD 237
Cdd:TIGR03724  46 REARLLSRARKAGVNTPVIydVDPDNKTIVMEYIEGKPLKDVIE-ENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVR 124

                          90
                  ....*....|
gi 229331967  238 eSDHITMIDF 247
Cdd:TIGR03724 125 -DDKVYLIDF 133
 
Name Accession Description Interval E-value
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 94-276 7.47e-130

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: 376.46  E-value: 7.47e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  94 VESVGNQMGVGKESDIYIVANEEGQQFALKLHRLGRTSFRNLKNKRDYHKHRHNVSWLYLSRLSAMKEFAYMKALYERKF 173
Cdd:cd05144    1 ISSVGNQIGVGKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRKRDYLKHRKHASWLYLSRLAAEKEFAALKALYEEGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 174 PVPKPIDYNRHAVVMELINGYPLCQIHHVEDPASVYDEAMELIVKLANHGLIHGDFNEFNLILDESDHITMIDFPQMVST 253
Cdd:cd05144   81 PVPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDEDEKITVIDFPQMVST 160

                        170       180
                 ....*....|....*....|...
gi 229331967 254 SHPNAEWYFDRDVKCIKDFFMKR 276
Cdd:cd05144  161 SHPNAEEYFDRDVECIIKFFRRK 183
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 108-280 2.79e-75

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: 236.36  E-value: 2.79e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  108 DIYIVANEEGQQFALKLHRLGRTSFRNLKNKRDYHKHR--HNVSWLYLSRLSAMKEFAYMKALYERKFPVPKPIDYNRHA 185
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFrdRKTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNRHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  186 VVMELI--NGYPLCQIHHV--EDPASVYDEAM-ELIVKLANHGLIHGDFNEFNLILDEsDHITMIDFPQMVSTSHPNAEW 260
Cdd:pfam01163  81 LVMEFIgkDGVPAPKLKDVelEEAEEIYDEIIrEMRRLYQEAGLVHGDLSEYNILVHD-DKPVIIDVPQAVETDHPNALE 159

                         170       180
                  ....*....|....*....|
gi 229331967  261 YFDRDVKCIKDFFMKRFSYE 280
Cdd:pfam01163 160 FLERDVENIINFFRRKGVDE 179
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 115-293 5.24e-56

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: 186.26  E-value: 5.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 115 EEGQQFALKLHRLGRTSFRNLKNKRDYHKHrhnVSWLYLSRLSAMKEFAYMKALYERKFPVPKPIDYNRHAVVMELINGY 194
Cdd:COG0478    6 PGGGPVALKFHREGRTSFRKVRRERADKEH---YSWLYAARTRAEREFRALERLYPAGLPVPRPIAANRHAIVMERIEGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 195 PLCQIHhVEDPASVYDEAMELIVKLANHGLIHGDFNEFNLILDESDHITMIDFPQMVSTSHPNAEWYFDRDVKCIKDFFM 274
Cdd:COG0478   83 ELARLK-LEDPEEVLDKILEEIRRAHDAGIVHADLSEYNILVDDDGGVWIIDWPQAVPRDHPNAEELLERDLENLLRSFR 161

                        170
                 ....*....|....*....
gi 229331967 275 KRFSYESELFPTFKDIRRE 293
Cdd:COG0478  162 KKYGLEVDLDEVWAALLGG 180
RIO smart00090
RIO-like kinase;
72-280 1.35e-53

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 181.73  E-value: 1.35e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967    72 GYRLTNAGYDYLALKTLSSRQVVESVGNQMGVGKESDIY--IVANEEGQQFALKLHRLGRTSFRNLKNKRDYHK--HRHN 147
Cdd:smart00090   7 TYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYhaLDFDGSGKERAVKIYRTGTLEFKRRDRYVDGDFrfKYRK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967   148 VSWLYLSRLSAMKEFAYMKALYERKFPVPKPIDYNRHAVVMELI--NGYPLCQIHHV----EDPASVYDEAMELIVKLAN 221
Cdd:smart00090  87 INPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIggDGLPAPRLKDVepeeEEEFELYDDILEEMRKLYK 166

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967   222 HG-LIHGDFNEFNLILDEsDHITMIDFPQMVSTSHPNAEWYFDRDVKCIKDFFMKRFSYE 280
Cdd:smart00090 167 EGeLVHGDLSEYNILVHD-GKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDE 225
Rio2_N pfam09202
Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to ...
 9-91 7.63e-40

Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to the winged helix (wHTH) domain. They adopt a structure consisting of four alpha helices followed by two beta strands and a fifth alpha helix. The domain confers DNA binding properties to the protein, as per other winged helix domains.


Pssm-ID: 462715  Cd Length: 82  Bit Score: 139.61  E-value: 7.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967    9 LRYMSRDDFRVLTAVEMGMKNHEIVPGSLIASIASLKHGGCNKVLRELVKHKLIAwERTKTVQGYRLTNAGYDYLALKTL 88
Cdd:pfam09202   1 MRYLSKEDFRVLTAVEMGMRNHEVVPTELITSISRLRHGGVNKRLSRLAKRKLIS-RKNAKYDGYRLTYLGYDYLALRTL 79


                  ...
gi 229331967   89 SSR 91
Cdd:pfam09202  80 VKR 82
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
82-276 3.02e-36

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 135.32  E-value: 3.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  82 YLALKTLSSRQVVESVGNQMGVGKESDIYIVANEEGQQFALKLHRLGRTSFRNL----------KNKRDYHKHRHNVSWl 151
Cdd:COG1718   35 PKALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGGELVAAKIYRTATSSFKRMaqyiegdprfMGKGSFGRRQLIFAW- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 152 ylsrlsAMKEFAYMKALYERKFPVPKPIDYNRHAVVMELI--NGYP---LCQIH-HVEDPASVYDEAMELIVKLANHGLI 225
Cdd:COG1718  114 ------ARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIgdDGVPaprLKDVElEPEEAEELYEQLIEYIVRLYKAGLV 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 229331967 226 HGDFNEFNLILDEsDHITMIDFPQMVSTSHPNAEWYFDRDVKCIKDFFMKR 276
Cdd:COG1718  188 HGDLSEYNILVDD-GGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARF 237
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
 104-276 9.82e-31

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: 118.42  E-value: 9.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 104 GKESDIYIVANEEGQQFALKLHRLGRTSFRN----------LKNKRDYHKHRHNVSWlylsrlsAMKEFAYMKALYERKF 173
Cdd:cd05145    8 GKEANVYLARGGDGEPVAVKIYRTSTSSFKKmakyiegdprFESRRRGNRRKLIFAW-------ARKEFRNLKRLYEAGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 174 PVPKPIDYNRHAVVMELI--NGYPLCQIHHV----EDPASVYDEAMELIVKLANH-GLIHGDFNEFNLILDEsDHITMID 246
Cdd:cd05145   81 RVPEPIAVYRNVLVMEFIgdDGSPAPRLKDVeleeEDAEELYEQVVEQMRRMYCKaGLVHGDLSEYNILYYD-GKPVIID 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 229331967 247 FPQMVSTSHPNAEWYFDRDVKCIKDFFMKR 276
Cdd:cd05145  160 VSQAVTLDHPNAEEFLRRDIRNINRFFSRK 189
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
 97-275 4.79e-21

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: 90.85  E-value: 4.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  97 VGNQMGVGKESDIYIVANEEGQQF---ALKLHRLGRTSFRNLK------NKRDYHKhrhnVSWLYLSRLSAMKEFAYMKA 167
Cdd:cd05119    1 IGGVISTGKEANVFYADGVFDGKPvacAVKIYRIETSEFDKVDeylygdERFDYRR----ISPKEKVFIWTEKEFRNLER 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 168 LYERKFPVPKPIDYNRHAVVMELING--------YPLCQIHHVEDPASVYDEAMELIVKLANH-GLIHGDFNEFNLILde 238
Cdd:cd05119   77 AKEAGVSVPQPYTYEKNVLL*EFIGEdelpaptlVELGRELKELDVEGIFNDVVENVKRLYQEaELVHADLSEYNILY-- 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 229331967 239 SDHITMIDFPQMVSTSHPNAEWYFDRDVKCIKDFFMK 275
Cdd:cd05119  155 IDKVYFIDFGQAVTLRHPGAESYLERDVRNIIRFFSK 191
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 104-276 1.03e-15

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: 75.68  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 104 GKESDIYIVANEEGQQFALKLHRlgrTSFRNLKN-----------KRDYHKH--RHNVswlylsRLSAMKEFAYMKALYE 170
Cdd:cd05147    8 GKEANVYHATTKNGGELAIKVYK---TSILVFKDrdkyvsgefrfRHGYCKHnpRKMV------KTWAEKEMRNLKRLNQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 171 RKFPVPKPIDYNRHAVVMELI--NGYPLCQIHHVEDPASVYDEA-MELIV---KLANHG-LIHGDFNEFNLILDEsDHIT 243
Cdd:cd05147   79 AGIPCPEPILLRSHVLVMEFIgkDGWPAPRLKDAKLSESKWRELyLQVIKimrRMYQKCrLVHADLSEYNLLYHK-GKVY 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 229331967 244 MIDFPQMVSTSHPNAEWYFDRDVKCIKDFFMKR 276
Cdd:cd05147  158 IIDVSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 158-300 6.45e-14

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: 69.60  E-value: 6.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 158 AMKEFAYMKALYERKFPVPKPIDYNRH--AVVMELINGYPLCQ-IHHVEDPASVYDEAMELIVKLANHGLIHGDFNEFNL 234
Cdd:COG3642    3 TRREARLLRELREAGVPVPKVLDVDPDdaDLVMEYIEGETLADlLEEGELPPELLRELGRLLARLHRAGIVHGDLTTSNI 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229331967 235 ILDEsDHITMIDFPQMVSTSHPnaEWYfDRDVKCIKDFFMKRFS-YESELFPTFKDIRREDTLDVEV 300
Cdd:COG3642   83 LVDD-GGVYLIDFGLARYSDPL--EDK-AVDLAVLKRSLESTHPdPAEELWEAFLEGYREVGPAEEV 145
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
 150-247 1.06e-11

3-deoxy-D-manno-octulosonic-acid kinase; Reviewed


Pssm-ID: 234975  Cd Length: 239  Bit Score: 64.90  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 150 WLYLSRLSAMKEFAYMKALYERKFPVPKPI--DYNRH------AVVMElingyplcQIHHVEDPASVYDEAM-------- 213
Cdd:PRK01723  79 FTGLERTRAFAEFRLLAQLYEAGLPVPRPIaaRVVRHglfyraDILIE--------RIEGARDLVALLQEAPlseeqwqa 150

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 229331967 214 --ELIVKLANHGLIHGDFNEFNLILDESDHITMIDF 247
Cdd:PRK01723 151 igQLIARFHDAGVYHADLNAHNILLDPDGKFWLIDF 186
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 155-276 1.08e-10

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: 61.23  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 155 RLSAMKEFAYMKALYERKFPVPKPIDYNRHAVVMELI--NGYPLCQIHHV----EDPASVYDEAMELIVKLANHG-LIHG 227
Cdd:cd05146   69 RLWAEKEMHNLKRMQKAGIPCPEVVLLKKHVLVMSFIgkDQVPAPKLKDAklssADLKLAYEQVVQMMKTMYNEChLVHA 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 229331967 228 DFNEFNLILDEsDHITMIDFPQMVSTSHPNAEWYFDRDVKCIKDFFMKR 276
Cdd:cd05146  149 DLSEYNILWHE-GKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
prot_kin_PA4780 NF041645
PA4780 family RIO1-like protein kinase; Members of this family are putative serine ...
 175-273 1.19e-10

PA4780 family RIO1-like protein kinase; Members of this family are putative serine/threonine-protein kinases, closely related to founding member PA4780 from Pseudomonas aeruginosa PAO1, which was shown to be upregulated by and important for the biodegradation of phenanthrene and naphthalene. Members belong more generally to the RIO1 atypical kinase family (see PF01163).


Pssm-ID: 469527  Cd Length: 274  Bit Score: 62.27  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 175 VPKPIDYNRHAVVMELI---NGYPLCQIHHV---EDPASVYDEAM-ELIVKLANHGLIHGDFNEFNLILDeSDHITMIDF 247
Cdd:NF041645 108 VPQPYGFFDGVLLMELVtdeEGDAAPRLNDVsltPEQAREYHALLiRYVVRMLCAGLVHGDLSEFNVLVD-ADGPVIIDL 186

                         90       100
                 ....*....|....*....|....*..
gi 229331967 248 PQMVS-TSHPNAEWYFDRDVKCIKDFF 273
Cdd:NF041645 187 PQAVDaAGNNNARRMLERDVNNLAAYF 213
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
 126-247 3.95e-08

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: 53.93  E-value: 3.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  126 RLGRTSFRNLKNKRDYHKHRHNVSWLYLSRLSAMKEFAYMKALYERKFPVPKPIDYN--------RHAVVMELINGY--- 194
Cdd:pfam06293  25 RVGNGVLRKYYRGGMWGHLNRDLYRYPLGRTRAFREFRLIRRLREAGLPVPKPVAAGevkvgggyRADLLTERLEGAqsl 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229331967  195 -PLCQIHHVEDPASvyDEAM-----ELIVKLANHGLIHGDFNEFNLILDESD----HITMIDF 247
Cdd:pfam06293 105 aDWLADWAVPSGEL--RRAIweavgRLIRQMHRAGVQHGDLYAHHILLQQEGdegfEAWLIDL 165
PRK14879 PRK14879
Kae1-associated kinase Bud32;
160-247 3.50e-07

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 51.06  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 160 KEFAYMKALYERKFPVPKP--IDYNRHAVVMELINGYPLCQ-IHHVEDPASVYDEAM-ELIVKLANHGLIHGDFNEFNLI 235
Cdd:PRK14879  48 REARIMSRARKAGVNVPAVyfVDPENFIIVMEYIEGEPLKDlINSNGMEELELSREIgRLVGKLHSAGIIHGDLTTSNMI 127

                         90
                 ....*....|..
gi 229331967 236 LDESDhITMIDF 247
Cdd:PRK14879 128 LSGGK-IYLIDF 138
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 160-247 6.36e-07

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK 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), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 49.22  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 160 KEFAYMKALYERK-FPVPKPIDY----NRHAVVMELINGYPLCQIHHVEDPASVYD------EAMELIVKLANHGLIHGD 228
Cdd:cd05120   38 KEAAMLQLLAGKLsLPVPKVYGFgesdGWEYLLMERIEGETLSEVWPRLSEEEKEKiadqlaEILAALHRIDSSVLTHGD 117

                         90       100
                 ....*....|....*....|
gi 229331967 229 FNEFNLILDESDHIT-MIDF 247
Cdd:cd05120  118 LHPGNILVKPDGKLSgIIDW 137
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
154-247 6.83e-07

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


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 50.41  E-value: 6.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 154 SRLSAMKEFAYMKALYerKFPV-PKPIDYNRHAVVMELINGYPL---CQIHHVEDPASVYDEAMELIVKLANHGLIHGDF 229
Cdd:COG2112   76 PRPSLKKEAEILKKAN--GAGVgPKLYDYGRDFLVMEYIEGEPLkdwLENLDKEELRKVIRELLEAAYLLDRIGIDHGEL 153

                         90
                 ....*....|....*....
gi 229331967 230 N-EFNLILDESDHITMIDF 247
Cdd:COG2112  154 SrPGKHVIVDKGRPYIIDF 172
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 106-247 3.95e-06

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 48.77  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 106 ESDIYIVANEEGQQFALKLHRLGRTSFRNLknkrdyhkhrhnvswlylsrlsaMKEFAYMKALYERKFPVPKPI------ 179
Cdd:COG2334   25 ENRNYRVETEDGRRYVLKLYRPGRWSPEEI-----------------------PFELALLAHLAAAGLPVPAPVptrdge 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 180 ----DYNRHAVVMELINGYPLC---------------QIH---------------------------HVEDPA--SVYDE 211
Cdd:COG2334   82 tlleLEGRPAALFPFLPGRSPEepspeqleelgrllaRLHraladfprpnardlawwdellerllgpLLPDPEdrALLEE 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 229331967 212 AMELIVKLA-------NHGLIHGDFNEFNLILDESDHITMIDF 247
Cdd:COG2334  162 LLDRLEARLapllgalPRGVIHGDLHPDNVLFDGDGVSGLIDF 204
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
175-247 4.96e-06

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 49.24  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 175 VPKPIDY----NRHAVVMELINGYPLCQIHHVEDPASVyDEAMELIVKLA-------NHGLIHGDFNEFNLILDESDHIT 243
Cdd:COG0515   69 IVRVYDVgeedGRPYLVMEYVEGESLADLLRRRGPLPP-AEALRILAQLAealaaahAAGIVHRDIKPANILLTPDGRVK 147


                 ....
gi 229331967 244 MIDF 247
Cdd:COG0515  148 LIDF 151
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 160-247 1.52e-05

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: 46.05  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967  160 KEFAYMKALYERKFPVPKP--IDYNRHAVVMELINGYPLCQIHHvEDPASVYDEAMELIVKLANHGLIHGDFNEFNLILD 237
Cdd:TIGR03724  46 REARLLSRARKAGVNTPVIydVDPDNKTIVMEYIEGKPLKDVIE-ENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVR 124

                          90
                  ....*....|
gi 229331967  238 eSDHITMIDF 247
Cdd:TIGR03724 125 -DDKVYLIDF 133
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 160-247 3.43e-05

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: 43.97  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 160 KEFAYMKALYERKFPVPKPIDYNRHA----VVMELINGYPLCQIHHVE-----DPASVYDEAMELIVKLANHGLIHGDFN 230
Cdd:cd13968   39 SEMDILRRLKGLELNIPKVLVTEDVDgpniLLMELVKGGTLIAYTQEEeldekDVESIMYQLAECMRLLHSFHLIHRDLN 118

                         90
                 ....*....|....*..
gi 229331967 231 EFNLILDESDHITMIDF 247
Cdd:cd13968  119 NDNILLSEDGNVKLIDF 135
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
160-247 6.34e-04

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 42.57  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229331967 160 KEFAYMKALyeRKFPVPKP----IDYNRHAVVMELINGYPLCQIhhVEDPASVYDEAMELIVKLANHGLIHGDFNEFNLI 235
Cdd:PRK09605 385 AEARLLSEA--RRAGVPTPviydVDPEEKTIVMEYIGGKDLKDV--LEGNPELVRKVGEIVAKLHKAGIVHGDLTTSNFI 460

                         90
                 ....*....|..
gi 229331967 236 LDEsDHITMIDF 247
Cdd:PRK09605 461 VRD-DRLYLIDF 471
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 206-256 7.91e-03

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 38.25  E-value: 7.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 229331967  206 ASVYDEAMELIVKLANHGLIHGDFNEFNLILDESDHIT-MIDFpQMVSTSHP 256
Cdd:pfam01636 151 ERLLAALLALLPAELPPVLVHGDLHPGNLLVDPGGRVSgVIDF-EDAGLGDP 201
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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