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Conserved domains on  [gi|6324122|ref|NP_014192|]
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protein kinase RIO2 [Saccharomyces cerevisiae S288C]

Protein Classification

serine/threonine-protein kinase RIO2( domain architecture ID 11422272)

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

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 ...
 94-283 6.05e-101

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: 298.26  E-value: 6.05e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   94 VYSVGNTIGVGKESDIYKVSDKNGNPRVMKIHRLGRTSFHSVRNNRDYLKKSnQGANWMHLSRLAANKEYQFMSMLYSKG 173
Cdd:cd05144   1 ISSVGNQIGVGKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRKRDYLKHR-KHASWLYLSRLAAEKEFAALKALYEEG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  174 FKVPEPFDNSRHIVVMELIEGYPMRRLRKHKNIPKLYSDLMCFIVDLANSGLIHCDFNEFNIMIKDkledenDCGFVVID 253
Cdd:cd05144  80 FPVPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDE------DEKITVID 153

                       170       180       190
                ....*....|....*....|....*....|
gi 6324122  254 FPQCISIQHQDADYYFQRDVDCIRRFFKKK 283
Cdd:cd05144 154 FPQMVSTSHPNAEEYFDRDVECIIKFFRRK 183
Rio2_N pfam09202
Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to ...
 8-91 2.42e-38

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: 133.44  E-value: 2.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122      8 MRYLTTDDFRVLQAVEQGSRSHEVVPTPLIHQISGMRSqSGTNRAISDLAKLSLISKmRNVKYDGYRLTYNGIDYLALKT 87
Cdd:pfam09202   1 MRYLSKEDFRVLTAVEMGMRNHEVVPTELITSISRLRH-GGVNKRLSRLAKRKLISR-KNAKYDGYRLTYLGYDYLALRT 78


                  ....
gi 6324122     88 MLNR 91
Cdd:pfam09202  79 LVKR 82
DNA_pol_phi super family cl47903
DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7. ...
 355-407 1.87e-04

DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7.7. Pol5p is localized exclusively to the nucleolus and binds near or at the enhancer region of rRNA-encoding DNA repeating units.


The actual alignment was detected with superfamily member pfam04931:

Pssm-ID: 461488  Cd Length: 765  Bit Score: 43.77  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6324122    355 DDDMSNDEAEEENGEGDYSEEDEYyDSELDNESSEDDSEDAQEEEN--ERIIEAL 407
Cdd:pfam04931 642 DEEDDDEEEDDDDEDDEDSEEDDD-EDDDDEDEEDDDDEDVDEIDElrAKLAEAL 695
TAF7 super family cl04653
TATA Binding Protein (TBP) Associated Factor 7 (TAF7) is one of several TAFs that bind TBP and ...
 319-425 7.08e-03

TATA Binding Protein (TBP) Associated Factor 7 (TAF7) is one of several TAFs that bind TBP and is involved in forming Transcription Factor IID (TFIID) complex; The TATA Binding Protein (TBP) Associated Factor 7 (TAF7) is one of several TAFs that bind TBP and are involved in forming the Transcription Factor IID (TFIID) complex. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) that are involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and assembly of the preinitiation complex. TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs functions such as serving as activator-binding sites, core-promoter recognition or a role in essential catalytic activity. Each TAF, with the help of a specific activator, is required only for expression of subset of genes and is not universally involved for transcription as are GTFs. TAF7 is involved in the regulation of the transition from PIC assembly to initiation and elongation. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers.


The actual alignment was detected with superfamily member COG5414:

Pssm-ID: 471075  Cd Length: 392  Bit Score: 38.53  E-value: 7.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  319 DNLDELVQASGFSKKHPGDRGLETAVESMRNAvynSDDDMSNDEAEEENGEGDYSEEDEYYDSELDNESSEDDSEDAQEE 398
Cdd:COG5414 258 KKEKQGAEEEGEEGMSEEDLDVGAAEIENKEV---SEGDKEQQQEEVENAEAHKEEVQSDRPDEIGEEKEEDDENEENER 334

                        90       100       110
                ....*....|....*....|....*....|..
gi 6324122  399 ENERI---IEALSSGVENLK--MDKLGNYILE 425
Cdd:COG5414 335 HTELLadeLNELEKGIEEKRrqMESATNPILQ 366
 
Name Accession Description Interval E-value
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 94-283 6.05e-101

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: 298.26  E-value: 6.05e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   94 VYSVGNTIGVGKESDIYKVSDKNGNPRVMKIHRLGRTSFHSVRNNRDYLKKSnQGANWMHLSRLAANKEYQFMSMLYSKG 173
Cdd:cd05144   1 ISSVGNQIGVGKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRKRDYLKHR-KHASWLYLSRLAAEKEFAALKALYEEG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  174 FKVPEPFDNSRHIVVMELIEGYPMRRLRKHKNIPKLYSDLMCFIVDLANSGLIHCDFNEFNIMIKDkledenDCGFVVID 253
Cdd:cd05144  80 FPVPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDE------DEKITVID 153

                       170       180       190
                ....*....|....*....|....*....|
gi 6324122  254 FPQCISIQHQDADYYFQRDVDCIRRFFKKK 283
Cdd:cd05144 154 FPQMVSTSHPNAEEYFDRDVECIIKFFRRK 183
RIO smart00090
RIO-like kinase;
67-302 1.03e-86

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 263.78  E-value: 1.03e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122      67 NVKYDGYRLTYNGIDYLALKTMLNRDTVYSVGNTIGVGKESDIYKVS--DKNGNPRVMKIHRLGRTSFHSVRNNRDYLKK 144
Cdd:smart00090   2 KEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHALdfDGSGKERAVKIYRTGTLEFKRRDRYVDGDFR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122     145 SN-QGANWMHLSRLAANKEYQFMSMLYSKGFKVPEPFDNSRHIVVMELI--EGYPMRRLRKHKNIP----KLYSDLMCFI 217
Cdd:smart00090  82 FKyRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIggDGLPAPRLKDVEPEEeeefELYDDILEEM 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122     218 VDLANSG-LIHCDFNEFNIMIKdkledenDCGFVVIDFPQCISIQHQDADYYFQRDVDCIRRFFKKKLKYEPKPdssMLD 296
Cdd:smart00090 162 RKLYKEGeLVHGDLSEYNILVH-------DGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELDE---EEL 231


                   ....*.
gi 6324122     297 TEGFGD 302
Cdd:smart00090 232 FERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 108-292 1.35e-43

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: 150.46  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122    108 DIYKVSDKNGNPRVMKIHRLGRTSFHSVRNNRDYLKKSNQG-ANWMHLSRLAANKEYQFMSMLYSKGFKVPEPFDNSRHI 186
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFRDRkTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNRHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122    187 VVMELI--EGYPMRRLR--KHKNIPKLYSDLM-CFIVDLANSGLIHCDFNEFNIMIKDKledendcGFVVIDFPQCISIQ 261
Cdd:pfam01163  81 LVMEFIgkDGVPAPKLKdvELEEAEEIYDEIIrEMRRLYQEAGLVHGDLSEYNILVHDD-------KPVIIDVPQAVETD 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 6324122    262 HQDADYYFQRDVDCIRRFFKKKLKYEPKPDS 292
Cdd:pfam01163 154 HPNALEFLERDVENIINFFRRKGVDEVDERK 184
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 116-285 1.40e-39

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: 140.04  E-value: 1.40e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  116 NGNPRVMKIHRLGRTSFHSVRNNRDYLKKSNqganWMHLSRLAANKEYQFMSMLYSKGFKVPEPFDNSRHIVVMELIEGY 195
Cdd:COG0478   7 GGGPVALKFHREGRTSFRKVRRERADKEHYS----WLYAARTRAEREFRALERLYPAGLPVPRPIAANRHAIVMERIEGV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  196 PMRRLRKHkNIPKLYSDLMCFIVDLANSGLIHCDFNEFNIMIkdkleDENDcGFVVIDFPQCISIQHQDADYYFQRDVDC 275
Cdd:COG0478  83 ELARLKLE-DPEEVLDKILEEIRRAHDAGIVHADLSEYNILV-----DDDG-GVWIIDWPQAVPRDHPNAEELLERDLEN 155

                       170
                ....*....|
gi 6324122  276 IRRFFKKKLK 285
Cdd:COG0478 156 LLRSFRKKYG 165
Rio2_N pfam09202
Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to ...
 8-91 2.42e-38

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: 133.44  E-value: 2.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122      8 MRYLTTDDFRVLQAVEQGSRSHEVVPTPLIHQISGMRSqSGTNRAISDLAKLSLISKmRNVKYDGYRLTYNGIDYLALKT 87
Cdd:pfam09202   1 MRYLSKEDFRVLTAVEMGMRNHEVVPTELITSISRLRH-GGVNKRLSRLAKRKLISR-KNAKYDGYRLTYLGYDYLALRT 78


                  ....
gi 6324122     88 MLNR 91
Cdd:pfam09202  79 LVKR 82
DNA_pol_phi pfam04931
DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7. ...
 355-407 1.87e-04

DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7.7. Pol5p is localized exclusively to the nucleolus and binds near or at the enhancer region of rRNA-encoding DNA repeating units.


Pssm-ID: 461488  Cd Length: 765  Bit Score: 43.77  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6324122    355 DDDMSNDEAEEENGEGDYSEEDEYyDSELDNESSEDDSEDAQEEEN--ERIIEAL 407
Cdd:pfam04931 642 DEEDDDEEEDDDDEDDEDSEEDDD-EDDDDEDEEDDDDEDVDEIDElrAKLAEAL 695
PRK14879 PRK14879
Kae1-associated kinase Bud32;
161-254 3.18e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 41.82  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   161 KEYQFMSMLYSKGFKVPEP--FDNSRHIVVMELIEGYPMRRL--RKHKNIPKLYSDLMCFIVDLANSGLIHCDFNEFNIM 236
Cdd:PRK14879  48 REARIMSRARKAGVNVPAVyfVDPENFIIVMEYIEGEPLKDLinSNGMEELELSREIGRLVGKLHSAGIIHGDLTTSNMI 127

                         90
                 ....*....|....*...
gi 6324122   237 IKDKledendcGFVVIDF 254
Cdd:PRK14879 128 LSGG-------KIYLIDF 138
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 322-408 1.85e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.75  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122     322 DELVQASGFSKKHPGDRGLETAVESMRNAVYNSDDDMSNDEAEEENGEGD--YSEEDEYYDSELDNESSEDDSEDAQEEE 399
Cdd:TIGR00927  810 GEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDggDSEEEEEEEEEEEEEEEEEEEEEEEEEE 889


                   ....*....
gi 6324122     400 NEriiEALS 408
Cdd:TIGR00927  890 NE---EPLS 895
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
 353-401 3.28e-03

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 39.78  E-value: 3.28e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6324122  353 NSDDDMSNDEAEEENGEGDYSEEDEYYDSElDNESSEDDSEDAQEEENE 401
Cdd:COG4547 221 DDEDDSGEQEEDEEDGEDEDEESDEGAEAE-DAEASGDDAEEGESEAAE 268
Taf7 COG5414
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ...
 319-425 7.08e-03

TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];


Pssm-ID: 227701  Cd Length: 392  Bit Score: 38.53  E-value: 7.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  319 DNLDELVQASGFSKKHPGDRGLETAVESMRNAvynSDDDMSNDEAEEENGEGDYSEEDEYYDSELDNESSEDDSEDAQEE 398
Cdd:COG5414 258 KKEKQGAEEEGEEGMSEEDLDVGAAEIENKEV---SEGDKEQQQEEVENAEAHKEEVQSDRPDEIGEEKEEDDENEENER 334

                        90       100       110
                ....*....|....*....|....*....|..
gi 6324122  399 ENERI---IEALSSGVENLK--MDKLGNYILE 425
Cdd:COG5414 335 HTELLadeLNELEKGIEEKRrqMESATNPILQ 366
 
Name Accession Description Interval E-value
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 94-283 6.05e-101

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: 298.26  E-value: 6.05e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   94 VYSVGNTIGVGKESDIYKVSDKNGNPRVMKIHRLGRTSFHSVRNNRDYLKKSnQGANWMHLSRLAANKEYQFMSMLYSKG 173
Cdd:cd05144   1 ISSVGNQIGVGKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRKRDYLKHR-KHASWLYLSRLAAEKEFAALKALYEEG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  174 FKVPEPFDNSRHIVVMELIEGYPMRRLRKHKNIPKLYSDLMCFIVDLANSGLIHCDFNEFNIMIKDkledenDCGFVVID 253
Cdd:cd05144  80 FPVPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDE------DEKITVID 153

                       170       180       190
                ....*....|....*....|....*....|
gi 6324122  254 FPQCISIQHQDADYYFQRDVDCIRRFFKKK 283
Cdd:cd05144 154 FPQMVSTSHPNAEEYFDRDVECIIKFFRRK 183
RIO smart00090
RIO-like kinase;
67-302 1.03e-86

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 263.78  E-value: 1.03e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122      67 NVKYDGYRLTYNGIDYLALKTMLNRDTVYSVGNTIGVGKESDIYKVS--DKNGNPRVMKIHRLGRTSFHSVRNNRDYLKK 144
Cdd:smart00090   2 KEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHALdfDGSGKERAVKIYRTGTLEFKRRDRYVDGDFR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122     145 SN-QGANWMHLSRLAANKEYQFMSMLYSKGFKVPEPFDNSRHIVVMELI--EGYPMRRLRKHKNIP----KLYSDLMCFI 217
Cdd:smart00090  82 FKyRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIggDGLPAPRLKDVEPEEeeefELYDDILEEM 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122     218 VDLANSG-LIHCDFNEFNIMIKdkledenDCGFVVIDFPQCISIQHQDADYYFQRDVDCIRRFFKKKLKYEPKPdssMLD 296
Cdd:smart00090 162 RKLYKEGeLVHGDLSEYNILVH-------DGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELDE---EEL 231


                   ....*.
gi 6324122     297 TEGFGD 302
Cdd:smart00090 232 FERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 108-292 1.35e-43

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: 150.46  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122    108 DIYKVSDKNGNPRVMKIHRLGRTSFHSVRNNRDYLKKSNQG-ANWMHLSRLAANKEYQFMSMLYSKGFKVPEPFDNSRHI 186
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFRDRkTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNRHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122    187 VVMELI--EGYPMRRLR--KHKNIPKLYSDLM-CFIVDLANSGLIHCDFNEFNIMIKDKledendcGFVVIDFPQCISIQ 261
Cdd:pfam01163  81 LVMEFIgkDGVPAPKLKdvELEEAEEIYDEIIrEMRRLYQEAGLVHGDLSEYNILVHDD-------KPVIIDVPQAVETD 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 6324122    262 HQDADYYFQRDVDCIRRFFKKKLKYEPKPDS 292
Cdd:pfam01163 154 HPNALEFLERDVENIINFFRRKGVDEVDERK 184
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 116-285 1.40e-39

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: 140.04  E-value: 1.40e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  116 NGNPRVMKIHRLGRTSFHSVRNNRDYLKKSNqganWMHLSRLAANKEYQFMSMLYSKGFKVPEPFDNSRHIVVMELIEGY 195
Cdd:COG0478   7 GGGPVALKFHREGRTSFRKVRRERADKEHYS----WLYAARTRAEREFRALERLYPAGLPVPRPIAANRHAIVMERIEGV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  196 PMRRLRKHkNIPKLYSDLMCFIVDLANSGLIHCDFNEFNIMIkdkleDENDcGFVVIDFPQCISIQHQDADYYFQRDVDC 275
Cdd:COG0478  83 ELARLKLE-DPEEVLDKILEEIRRAHDAGIVHADLSEYNILV-----DDDG-GVWIIDWPQAVPRDHPNAEELLERDLEN 155

                       170
                ....*....|
gi 6324122  276 IRRFFKKKLK 285
Cdd:COG0478 156 LLRSFRKKYG 165
Rio2_N pfam09202
Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to ...
 8-91 2.42e-38

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: 133.44  E-value: 2.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122      8 MRYLTTDDFRVLQAVEQGSRSHEVVPTPLIHQISGMRSqSGTNRAISDLAKLSLISKmRNVKYDGYRLTYNGIDYLALKT 87
Cdd:pfam09202   1 MRYLSKEDFRVLTAVEMGMRNHEVVPTELITSISRLRH-GGVNKRLSRLAKRKLISR-KNAKYDGYRLTYLGYDYLALRT 78


                  ....
gi 6324122     88 MLNR 91
Cdd:pfam09202  79 LVKR 82
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
82-283 1.60e-31

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 120.68  E-value: 1.60e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   82 YLALKTMLNRDTVYSVGNTIGVGKESDIYKVSDKNGNPRVMKIHRlgrTSFHSVRNNRDYL--------KKS----NQGA 149
Cdd:COG1718  35 PKALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGGELVAAKIYR---TATSSFKRMAQYIegdprfmgKGSfgrrQLIF 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  150 NWmhlsrlaANKEYQFMSMLYSKGFKVPEPFDNSRHIVVMELI--EGYPMRRLR----KHKNIPKLYSDLMCFIVDLANS 223
Cdd:COG1718 112 AW-------ARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIgdDGVPAPRLKdvelEPEEAEELYEQLIEYIVRLYKA 184

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  224 GLIHCDFNEFNIMIKDKledendcGFVVIDFPQCISIQHQDADYYFQRDVDCIRRFFKKK 283
Cdd:COG1718 185 GLVHGDLSEYNILVDDG-------GPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARF 237
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
 97-283 1.15e-27

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: 108.41  E-value: 1.15e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   97 VGNTIGVGKESDIYKVSDKNGNPRVMKIHRLGRTSFhsvRNNRDYLK-----KSNQGANWMHLSRLAANKEYQFMSMLYS 171
Cdd:cd05145   1 LGGVISTGKEANVYLARGGDGEPVAVKIYRTSTSSF---KKMAKYIEgdprfESRRRGNRRKLIFAWARKEFRNLKRLYE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  172 KGFKVPEPFDNSRHIVVMELI--EGYPMRRLR----KHKNIPKLYSDLMCFIVDL-ANSGLIHCDFNEFNIMIKDKlede 244
Cdd:cd05145  78 AGVRVPEPIAVYRNVLVMEFIgdDGSPAPRLKdvelEEEDAEELYEQVVEQMRRMyCKAGLVHGDLSEYNILYYDG---- 153

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6324122  245 ndcGFVVIDFPQCISIQHQDADYYFQRDVDCIRRFFKKK 283
Cdd:cd05145 154 ---KPVIIDVSQAVTLDHPNAEEFLRRDIRNINRFFSRK 189
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
 97-282 2.62e-17

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: 79.68  E-value: 2.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   97 VGNTIGVGKESDI---YKVSDKNGNPRVMKIHRLGRTSFHSVRNNRDYLKKSNQGAnwMHLSRLA---ANKEYQFMSMLY 170
Cdd:cd05119   1 IGGVISTGKEANVfyaDGVFDGKPVACAVKIYRIETSEFDKVDEYLYGDERFDYRR--ISPKEKVfiwTEKEFRNLERAK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  171 SKGFKVPEPFDNSRHIVVMELI--------EGYPMRRLRKHKNIPKLYSDLMCFIVDL-ANSGLIHCDFNEFNIMIKDKL 241
Cdd:cd05119  79 EAGVSVPQPYTYEKNVLL*EFIgedelpapTLVELGRELKELDVEGIFNDVVENVKRLyQEAELVHADLSEYNILYIDKV 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6324122  242 edendcgfVVIDFPQCISIQHQDADYYFQRDVDCIRRFFKK 282
Cdd:cd05119 159 --------YFIDFGQAVTLRHPGAESYLERDVRNIIRFFSK 191
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 161-309 7.42e-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: 68.83  E-value: 7.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  161 KEYQFMSMLYSKGFKVPEP--FDNSRHIVVMELIEGYPMR-RLRKHKNIPKLYSDLMCFIVDLANSGLIHCDFNEFNIMI 237
Cdd:COG3642   5 REARLLRELREAGVPVPKVldVDPDDADLVMEYIEGETLAdLLEEGELPPELLRELGRLLARLHRAGIVHGDLTTSNILV 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324122  238 KDKledendcGFVVIDFPQCisiQHQDADYYFQRDVDCIRRFFKKKlkyepKPDSSMLDTEGFGDGYKYAYP 309
Cdd:COG3642  85 DDG-------GVYLIDFGLA---RYSDPLEDKAVDLAVLKRSLEST-----HPDPAEELWEAFLEGYREVGP 141
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 100-283 1.60e-10

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: 59.89  E-value: 1.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  100 TIGVGKESDIYKVSDKNGNPRVMKIHRlgrTS---FHSvRNN--------RDYLKKSNQganwMHLSRLAANKEYQFMSM 168
Cdd:cd05147   4 CISTGKEANVYHATTKNGGELAIKVYK---TSilvFKD-RDKyvsgefrfRHGYCKHNP----RKMVKTWAEKEMRNLKR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  169 LYSKGFKVPEPFDNSRHIVVMELI--EGYPMRRLRKHKNIP----KLYSDLMCFIVDLAN-SGLIHCDFNEFNIMI-KDK 240
Cdd:cd05147  76 LNQAGIPCPEPILLRSHVLVMEFIgkDGWPAPRLKDAKLSEskwrELYLQVIKIMRRMYQkCRLVHADLSEYNLLYhKGK 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 6324122  241 LedendcgfVVIDFPQCISIQHQDADYYFQRDVDCIRRFFKKK 283
Cdd:cd05147 156 V--------YIIDVSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 97-283 2.37e-08

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: 53.91  E-value: 2.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   97 VGNTIGVGKESDIYKVSDKNGNPRVM------KIHRlgrTSFHSVRNNRDYLKK--------SNQgaNWMHLSRLAANKE 162
Cdd:cd05146   1 VNGCISTGKEAVVFHANGGSMEEVLLppecaiKVFK---TTLNEFKNRDKYIKDdyrfkdrfSKQ--NPRKIIRLWAEKE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  163 YQFMSMLYSKGFKVPEPFDNSRHIVVMELI--EGYPMRRLRKHK----NIPKLYS---DLMCFIVDLANsgLIHCDFNEF 233
Cdd:cd05146  76 MHNLKRMQKAGIPCPEVVLLKKHVLVMSFIgkDQVPAPKLKDAKlssaDLKLAYEqvvQMMKTMYNECH--LVHADLSEY 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6324122  234 NImikdkLEDENDCGFvvIDFPQCISIQHQDADYYFQRDVDCIRRFFKKK 283
Cdd:cd05146 154 NI-----LWHEGKVWF--IDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
43-254 7.21e-05

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


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 43.86  E-value: 7.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   43 MRSQSGTNRAISDLAKLSLISKMRNvkydgyRLTYNGIDYLalktmLNRDTVYSVGNTIGVGKESDIYKVSDKNGNpRVM 122
Cdd:COG2112   1 MDSDEELIRLLCYPRSESELEERLE------ELKSLGITSI-----YSGGTLIGGLRLLGKGYRGVVFLGKLGGKK-VAL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  123 KIHRLGrtsfhSVRNNrdylkksnqganwmhlsrlaANKEYQFMSMLYSKGFkVPEPFDNSRHIVVMELIEGYPMRRLRK 202
Cdd:COG2112  69 KIRRTD-----SPRPS--------------------LKKEAEILKKANGAGV-GPKLYDYGRDFLVMEYIEGEPLKDWLE 122

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6324122  203 ---HKNIPKLYSDLM--CFIVDLAnsGLIHCDFN--EFNIMIKDKledendcGFVVIDF 254
Cdd:COG2112 123 nldKEELRKVIRELLeaAYLLDRI--GIDHGELSrpGKHVIVDKG-------RPYIIDF 172
DNA_pol_phi pfam04931
DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7. ...
 355-407 1.87e-04

DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7.7. Pol5p is localized exclusively to the nucleolus and binds near or at the enhancer region of rRNA-encoding DNA repeating units.


Pssm-ID: 461488  Cd Length: 765  Bit Score: 43.77  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6324122    355 DDDMSNDEAEEENGEGDYSEEDEYyDSELDNESSEDDSEDAQEEEN--ERIIEAL 407
Cdd:pfam04931 642 DEEDDDEEEDDDDEDDEDSEEDDD-EDDDDEDEEDDDDEDVDEIDElrAKLAEAL 695
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
 95-270 2.90e-04

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 42.26  E-value: 2.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   95 YSVGNTIGVGKESDIYKVSDKNGNPRV-MKIhrlgrtsfhsVRNNRDYLKKSNQGANWMH-LSRLAANKEYQFMSMLysk 172
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGEEVaLKI----------IKNNKDYLDQSLDEIRLLElLNKKDKADKYHIVRLK--- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  173 gfkvpEPFDNSRHI-VVMELIE-------------GYPMRRLRKhknIPKLYSDLMCFivdLANSGLIHCDFNEFNIMIK 238
Cdd:cd14133  68 -----DVFYFKNHLcIVFELLSqnlyeflkqnkfqYLSLPRIRK---IAQQILEALVF---LHSLGLIHCDLKPENILLA 136

                       170       180       190
                ....*....|....*....|....*....|..
gi 6324122  239 dkleDENDCGFVVIDFPQCISIqHQDADYYFQ 270
Cdd:cd14133 137 ----SYSRCQIKIIDFGSSCFL-TQRLYSYIQ 163
PRK14879 PRK14879
Kae1-associated kinase Bud32;
161-254 3.18e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 41.82  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122   161 KEYQFMSMLYSKGFKVPEP--FDNSRHIVVMELIEGYPMRRL--RKHKNIPKLYSDLMCFIVDLANSGLIHCDFNEFNIM 236
Cdd:PRK14879  48 REARIMSRARKAGVNVPAVyfVDPENFIIVMEYIEGEPLKDLinSNGMEELELSREIGRLVGKLHSAGIIHGDLTTSNMI 127

                         90
                 ....*....|....*...
gi 6324122   237 IKDKledendcGFVVIDF 254
Cdd:PRK14879 128 LSGG-------KIYLIDF 138
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 322-408 1.85e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.75  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122     322 DELVQASGFSKKHPGDRGLETAVESMRNAVYNSDDDMSNDEAEEENGEGD--YSEEDEYYDSELDNESSEDDSEDAQEEE 399
Cdd:TIGR00927  810 GEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDggDSEEEEEEEEEEEEEEEEEEEEEEEEEE 889


                   ....*....
gi 6324122     400 NEriiEALS 408
Cdd:TIGR00927  890 NE---EPLS 895
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
 353-401 3.28e-03

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 39.78  E-value: 3.28e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6324122  353 NSDDDMSNDEAEEENGEGDYSEEDEYYDSElDNESSEDDSEDAQEEENE 401
Cdd:COG4547 221 DDEDDSGEQEEDEEDGEDEDEESDEGAEAE-DAEASGDDAEEGESEAAE 268
Taf7 COG5414
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ...
 319-425 7.08e-03

TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];


Pssm-ID: 227701  Cd Length: 392  Bit Score: 38.53  E-value: 7.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324122  319 DNLDELVQASGFSKKHPGDRGLETAVESMRNAvynSDDDMSNDEAEEENGEGDYSEEDEYYDSELDNESSEDDSEDAQEE 398
Cdd:COG5414 258 KKEKQGAEEEGEEGMSEEDLDVGAAEIENKEV---SEGDKEQQQEEVENAEAHKEEVQSDRPDEIGEEKEEDDENEENER 334

                        90       100       110
                ....*....|....*....|....*....|..
gi 6324122  399 ENERI---IEALSSGVENLK--MDKLGNYILE 425
Cdd:COG5414 335 HTELLadeLNELEKGIEEKRrqMESATNPILQ 366
DNA_pol_phi pfam04931
DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7. ...
 362-401 9.66e-03

DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7.7. Pol5p is localized exclusively to the nucleolus and binds near or at the enhancer region of rRNA-encoding DNA repeating units.


Pssm-ID: 461488  Cd Length: 765  Bit Score: 38.37  E-value: 9.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 6324122    362 EAEEENGEGDYSEEDEyyDSELDNESSEDDSEDAQEEENE 401
Cdd:pfam04931 637 EDEDEDEEDDDEEEDD--DDEDDEDSEEDDDEDDDDEDEE 674
 
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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