NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1131742486|ref|NP_001335122|]
View 

serine/threonine-protein kinase RIO3 isoform 2 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase RIO3( domain architecture ID 10142321)

serine/threonine-protein kinase RIO3 is an atypical protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 237-437 4.70e-151

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: 429.09  E-value: 4.70e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 237 ITGCISTGKESVVFHAYGGSMEDekedsKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 316
Cdd:cd05146     1 VNGCISTGKEAVVFHANGGSMEE-----VLLPPECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 317 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNM 396
Cdd:cd05146    76 MHNLKRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNI 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1131742486 397 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 437
Cdd:cd05146   156 LWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
 
Name Accession Description Interval E-value
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 237-437 4.70e-151

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: 429.09  E-value: 4.70e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 237 ITGCISTGKESVVFHAYGGSMEDekedsKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 316
Cdd:cd05146     1 VNGCISTGKEAVVFHANGGSMEE-----VLLPPECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 317 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNM 396
Cdd:cd05146    76 MHNLKRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNI 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1131742486 397 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 437
Cdd:cd05146   156 LWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
RIO smart00090
RIO-like kinase;
206-454 7.10e-119

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 348.91  E-value: 7.10e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486  206 EKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAYggsmedekeDSKVIPTECAIKVFKTTLNEFKN 285
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHAL---------DFDGSGKERAVKIYRTGTLEFKR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486  286 RDKYIKDDFRFKdrFSKLNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEE 365
Cdd:smart00090  72 RDRYVDGDFRFK--YRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486  366 MKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSE 445
Cdd:smart00090 150 EFELYDDILEEMRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDE-LDE 228


                   ....*....
gi 1131742486  446 RELFNAVSG 454
Cdd:smart00090 229 EELFERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 248-447 7.36e-89

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: 269.87  E-value: 7.36e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 248 VVFHAYGgsmEDEKEdskvipteCAIKVFKTTLNEFKNRDKYIKDDFRFKDRfsKLNPRKIIRMWAEKEMHNLARMQRAG 327
Cdd:pfam01163   1 NVYHAVS---EDGKE--------VAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 328 IPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLnsEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLID 407
Cdd:pfam01163  68 VPVPKPIDVNRHVLVMEFIGKDGVPAPKLKDVEL--EEAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIID 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1131742486 408 VSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSERE 447
Cdd:pfam01163 146 VPQAVETDHPNALEFLERDVENIINFFRRKGVDE-VDERK 184
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
198-452 8.85e-70

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 223.14  E-value: 8.85e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 198 ERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAyggsmedEKEDSKVIptecAIKVFK 277
Cdd:COG1718    11 DKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLA-------RRPGGELV----AAKIYR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 278 TTLNEFKNRDKYIKDDFRFKDRFSKlNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLK 357
Cdd:COG1718    80 TATSSFKRMAQYIEGDPRFMGKGSF-GRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 358 EVKLNSEEMKEAYYQTLHLMRQLYhECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 437
Cdd:COG1718   159 DVELEPEEAEELYEQLIEYIVRLY-KAGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARF 237

                         250
                  ....*....|....*
gi 1131742486 438 GVKeaLSERELFNAV 452
Cdd:COG1718   238 GPE--LDPEELLKEI 250
PRK14879 PRK14879
Kae1-associated kinase Bud32;
286-425 3.72e-10

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 59.54  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 286 RDKYIKDDFRFKDRFSK--LNPR---KIIRMWAEKEMHNLARMQRAGIPCPTVVL--LKKHILVMSFIghdqvPAPKLKE 358
Cdd:PRK14879   14 LGDFLGIKAVIKWRIPKryRHPEldeRIRRERTRREARIMSRARKAGVNVPAVYFvdPENFIIVMEYI-----EGEPLKD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 359 VkLNSEEMKEA-YYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP--------------THPH 418
Cdd:PRK14879   89 L-INSNGMEELeLSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDfglaeFSKDLEDravdlhvllrslesTHPD 167


                  ....*..
gi 1131742486 419 GLEFLFR 425
Cdd:PRK14879  168 WAEELFE 174
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 306-414 2.38e-07

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


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 51.06  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 306 RKIIRMWAEKEMHNLARMQRAGIPCPTV--VLLKKHILVMSFIghdqvPAPKLKEVklnSEEMKEAYYQTLHLMRQLYHE 383
Cdd:TIGR03724  37 ERLRKERTRREARLLSRARKAGVNTPVIydVDPDNKTIVMEYI-----EGKPLKDV---IEENGDELAREIGRLVGKLHK 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1131742486 384 CTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP 414
Cdd:TIGR03724 109 AGIVHGDLTTSNIIVRDDKVYLIDfglgkYSDEIED 144
 
Name Accession Description Interval E-value
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 237-437 4.70e-151

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: 429.09  E-value: 4.70e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 237 ITGCISTGKESVVFHAYGGSMEDekedsKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 316
Cdd:cd05146     1 VNGCISTGKEAVVFHANGGSMEE-----VLLPPECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 317 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNM 396
Cdd:cd05146    76 MHNLKRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNI 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1131742486 397 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 437
Cdd:cd05146   156 LWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
RIO smart00090
RIO-like kinase;
206-454 7.10e-119

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 348.91  E-value: 7.10e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486  206 EKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAYggsmedekeDSKVIPTECAIKVFKTTLNEFKN 285
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHAL---------DFDGSGKERAVKIYRTGTLEFKR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486  286 RDKYIKDDFRFKdrFSKLNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEE 365
Cdd:smart00090  72 RDRYVDGDFRFK--YRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486  366 MKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSE 445
Cdd:smart00090 150 EFELYDDILEEMRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDE-LDE 228


                   ....*....
gi 1131742486  446 RELFNAVSG 454
Cdd:smart00090 229 EELFERITG 237
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 237-436 2.27e-103

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: 307.19  E-value: 2.27e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 237 ITGCISTGKESVVFHAYGGSmedekedskviPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 316
Cdd:cd05147     1 INGCISTGKEANVYHATTKN-----------GGELAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 317 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNM 396
Cdd:cd05147    70 MRNLKRLNQAGIPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNL 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1131742486 397 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 436
Cdd:cd05147   150 LYHKGKVYIIDVSQSVEHDHPHALEFLRRDCVNVNDFFRK 189
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
 237-436 1.79e-98

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: 294.84  E-value: 1.79e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 237 ITGCISTGKESVVFHAYGGSmedekedskviPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRfSKLNPRKIIRMWAEKE 316
Cdd:cd05145     1 LGGVISTGKEANVYLARGGD-----------GEPVAVKIYRTSTSSFKKMAKYIEGDPRFESR-RRGNRRKLIFAWARKE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 317 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNM 396
Cdd:cd05145    69 FRNLKRLYEAGVRVPEPIAVYRNVLVMEFIGDDGSPAPRLKDVELEEEDAEELYEQVVEQMRRMYCKAGLVHGDLSEYNI 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1131742486 397 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 436
Cdd:cd05145   149 LYYDGKPVIIDVSQAVTLDHPNAEEFLRRDIRNINRFFSR 188
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 248-447 7.36e-89

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: 269.87  E-value: 7.36e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 248 VVFHAYGgsmEDEKEdskvipteCAIKVFKTTLNEFKNRDKYIKDDFRFKDRfsKLNPRKIIRMWAEKEMHNLARMQRAG 327
Cdd:pfam01163   1 NVYHAVS---EDGKE--------VAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 328 IPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLnsEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLID 407
Cdd:pfam01163  68 VPVPKPIDVNRHVLVMEFIGKDGVPAPKLKDVEL--EEAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIID 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1131742486 408 VSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSERE 447
Cdd:pfam01163 146 VPQAVETDHPNALEFLERDVENIINFFRRKGVDE-VDERK 184
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
198-452 8.85e-70

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 223.14  E-value: 8.85e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 198 ERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAyggsmedEKEDSKVIptecAIKVFK 277
Cdd:COG1718    11 DKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLA-------RRPGGELV----AAKIYR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 278 TTLNEFKNRDKYIKDDFRFKDRFSKlNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLK 357
Cdd:COG1718    80 TATSSFKRMAQYIEGDPRFMGKGSF-GRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 358 EVKLNSEEMKEAYYQTLHLMRQLYhECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 437
Cdd:COG1718   159 DVELEPEEAEELYEQLIEYIVRLY-KAGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARF 237

                         250
                  ....*....|....*
gi 1131742486 438 GVKeaLSERELFNAV 452
Cdd:COG1718   238 GPE--LDPEELLKEI 250
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
 237-436 1.05e-37

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: 137.08  E-value: 1.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 237 ITGCISTGKESVVFHAYGgsmedeKEDSKviPTECAIKVFKTTLNEFKNRDKYIKDDFRFKdrFSKLNPRKIIRMWAEKE 316
Cdd:cd05119     1 IGGVISTGKEANVFYADG------VFDGK--PVACAVKIYRIETSEFDKVDEYLYGDERFD--YRRISPKEKVFIWTEKE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 317 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVK--LNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEY 394
Cdd:cd05119    71 FRNLERAKEAGVSVPQPYTYEKNVLL*EFIGEDELPAPTLVELGreLKELDVEGIFNDVVENVKRLYQEAELVHADLSEY 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1131742486 395 NMLWhAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 436
Cdd:cd05119   151 NILY-IDKVYFIDFGQAVTLRHPGAESYLERDVRNIIRFFSK 191
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 234-436 8.63e-24

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: 98.35  E-value: 8.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 234 LETITGCISTGKESVVFHAYGGSMEdekedskviptECAIKV-------FKTTLNefkNRDkYIKDdfrfKDRFSKLNpr 306
Cdd:cd05144     1 ISSVGNQIGVGKESDVYLALDEDGN-----------PVVLKFhrlgrtsFRKVKR---KRD-YLKH----RKHASWLY-- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 307 kIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIghdqvPAPKLKEVKLNsEEMKEAYYQTLHLMRQLYhECTL 386
Cdd:cd05144    60 -LSRLAAEKEFAALKALYEEGFPVPKPIDWNRHAVVMELI-----DGYPLYQVRLL-EDPEEVLDEILELIVKLA-KHGL 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1131742486 387 VHADLSEYN-MLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 436
Cdd:cd05144   132 IHGDFSEFNiLVDEDEKITVIDFPQMVSTSHPNAEEYFDRDVECIIKFFRR 182
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 288-436 2.35e-22

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: 94.20  E-value: 2.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 288 KYIKDDFRFKDRFSKLN-PRKIirmwAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIghdqvPAPKLKEVKLNSEEm 366
Cdd:COG0478    24 RKVRRERADKEHYSWLYaARTR----AEREFRALERLYPAGLPVPRPIAANRHAIVMERI-----EGVELARLKLEDPE- 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742486 367 kEAYYQTLHLMRQLyHECTLVHADLSEYN-MLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 436
Cdd:COG0478    94 -EVLDKILEEIRRA-HDAGIVHADLSEYNiLVDDDGGVWIIDWPQAVPRDHPNAEELLERDLENLLRSFRK 162
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 310-411 8.52e-13

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: 66.14  E-value: 8.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 310 RMWAEKEMhnLARMQRAGIPCPTVVLLKKH--ILVMSFIghdqvPAPKLKEVKLNSEEMKEAYYQTLHLMRQLyHECTLV 387
Cdd:COG3642     2 RTRREARL--LRELREAGVPVPKVLDVDPDdaDLVMEYI-----EGETLADLLEEGELPPELLRELGRLLARL-HRAGIV 73

                          90       100
                  ....*....|....*....|....
gi 1131742486 388 HADLSEYNMLWHAGKVWLIDVSQS 411
Cdd:COG3642    74 HGDLTTSNILVDDGGVYLIDFGLA 97
PRK14879 PRK14879
Kae1-associated kinase Bud32;
286-425 3.72e-10

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 59.54  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 286 RDKYIKDDFRFKDRFSK--LNPR---KIIRMWAEKEMHNLARMQRAGIPCPTVVL--LKKHILVMSFIghdqvPAPKLKE 358
Cdd:PRK14879   14 LGDFLGIKAVIKWRIPKryRHPEldeRIRRERTRREARIMSRARKAGVNVPAVYFvdPENFIIVMEYI-----EGEPLKD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 359 VkLNSEEMKEA-YYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP--------------THPH 418
Cdd:PRK14879   89 L-INSNGMEELeLSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDfglaeFSKDLEDravdlhvllrslesTHPD 167


                  ....*..
gi 1131742486 419 GLEFLFR 425
Cdd:PRK14879  168 WAEELFE 174
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 306-414 2.38e-07

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


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 51.06  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 306 RKIIRMWAEKEMHNLARMQRAGIPCPTV--VLLKKHILVMSFIghdqvPAPKLKEVklnSEEMKEAYYQTLHLMRQLYHE 383
Cdd:TIGR03724  37 ERLRKERTRREARLLSRARKAGVNTPVIydVDPDNKTIVMEYI-----EGKPLKDV---IEENGDELAREIGRLVGKLHK 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1131742486 384 CTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP 414
Cdd:TIGR03724 109 AGIVHGDLTTSNIIVRDDKVYLIDfglgkYSDEIED 144
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
285-413 9.95e-06

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 47.96  E-value: 9.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 285 NRDKYIKDDFRFKDRFSKL--NP---RKIIRMWAEKEMHNLARMQRAGIPCPTV--VLLKKHILVMSFIGhdqvpAPKLK 357
Cdd:PRK09605  350 KKGEYLGRDAVIKERVPKGyrHPeldERLRTERTRAEARLLSEARRAGVPTPVIydVDPEEKTIVMEYIG-----GKDLK 424

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742486 358 EVKLNSEEMKEAYYQTLHLMrqlyHECTLVHADLSEYNMLWHAGKVWLID-----VSQSVE 413
Cdd:PRK09605  425 DVLEGNPELVRKVGEIVAKL----HKAGIVHGDLTTSNFIVRDDRLYLIDfglgkYSDLIE 481
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 310-407 2.49e-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: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 310 RMWAEKEMHNLARMQRAGIPCPTVVLLKK----HILVMSFIGHDQVPAPkLKEVKLNSEEMKEAYYQTLHLMRQLyHECT 385
Cdd:cd13968    34 GEDLESEMDILRRLKGLELNIPKVLVTEDvdgpNILLMELVKGGTLIAY-TQEEELDEKDVESIMYQLAECMRLL-HSFH 111

                          90       100
                  ....*....|....*....|...
gi 1131742486 386 LVHADLSEYN-MLWHAGKVWLID 407
Cdd:cd13968   112 LIHRDLNNDNiLLSEDGNVKLID 134
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 316-407 4.28e-05

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily 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: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 43.70  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 316 EMHNLARMQRAGIpCPTVVLL--KKHILVMSFIghdqVPAPKLKEVKLNSEEMKEAyyqtLHLMRQLYH----ECTLVHA 389
Cdd:cd05151    42 EKANSKAAAELGI-APEVIYFdpETGVKITEFI----EGATLLTNDFSDPENLERI----AALLRKLHSspleDLVLCHN 112

                          90
                  ....*....|....*...
gi 1131742486 390 DLSEYNMLWHAGKVWLID 407
Cdd:cd05151   113 DLVPGNFLLDDDRLYLID 130
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
 277-431 6.99e-05

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: 43.92  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 277 KTTLNEFkNRDKYikddfrfkdRFSKLNPRkiirmwAEKEMHNLARMQRAGIPCPTVV--------LLKKHILVMSFIGH 348
Cdd:pfam06293  37 GGMWGHL-NRDLY---------RYPLGRTR------AFREFRLIRRLREAGLPVPKPVaagevkvgGGYRADLLTERLEG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 349 DQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAG-----KVWLIDVSQSVEPTHP-----H 418
Cdd:pfam06293 101 AQSLADWLADWAVPSGELRRAIWEAVGRLIRQMHRAGVQHGDLYAHHILLQQEgdegfEAWLIDLDKGRLRLPArrwrnK 180

                         170
                  ....*....|...
gi 1131742486 419 GLEFLFRDCRNVS 431
Cdd:pfam06293 181 DLARLLRSFLNIG 193
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
 310-407 1.80e-03

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


Pssm-ID: 234975  Cd Length: 239  Bit Score: 39.87  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742486 310 RMWAEkeMHNLARMQRAGIPCPTVV--------LLKKHILVMSFIGHDQVPAPKLKEVKLnSEEMkeaYYQTLHLMRQLy 381
Cdd:PRK01723   86 RAFAE--FRLLAQLYEAGLPVPRPIaarvvrhgLFYRADILIERIEGARDLVALLQEAPL-SEEQ---WQAIGQLIARF- 158

                          90       100
                  ....*....|....*....|....*..
gi 1131742486 382 HECTLVHADLSEYNMLW-HAGKVWLID 407
Cdd:PRK01723  159 HDAGVYHADLNAHNILLdPDGKFWLID 185
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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