NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1197863592|ref|WP_086790759|]
View 

MULTISPECIES: phosphotransferase [Bacillus cereus group]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
28-319 6.33e-26

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05153:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 300  Bit Score: 104.65  E-value: 6.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  28 KIRNAIPIHRGWLNLKWKLETDAGDFVLKQYNQERykmyNSDLLIQALQQQQRLHNNGVSCPRVLIYKNNVMHISKSDER 107
Cdd:cd05153    15 ELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRR----SAAELPFELELLDHLAQAGLPVPRPLADKDGELLGELNGKP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 108 FIVLEHKEGslVSPGKVNQKEIHSLGQTIGYMHNLLNDgslikgenpkFVPPTKEARLKHWE----DKRREVEKLGKEHI 183
Cdd:cd05153    91 AALFPFLPG--ESLTTPTPEQCRAIGAALARLHLALAG----------FPPPRPNPRGLAWWkplaERLKARLDLLAADD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 184 LPYIKLQQEATQlvnTEQFHNSQRAWVHRDLWVDNFLFLNDKVSAILDFDRMDYDYVELDIGRVVIS-CALSDGVLNKSL 262
Cdd:cd05153   159 RALLEDELARLQ---ALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNDwCFDDDGKLDPER 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1197863592 263 VASFLEGYR-------NEVD-FPVGNIVRAIQM-LWYMestWWIHANMDQHSVPPSRFADEMNWIA 319
Cdd:cd05153   236 AKALLAGYQsvrplteEEKAaLPLLLRAAALRFwLSRL---YDFHLPREGALVTPKDPDEFLRRLR 298
 
Name Accession Description Interval E-value
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
28-319 6.33e-26

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase 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: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 104.65  E-value: 6.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  28 KIRNAIPIHRGWLNLKWKLETDAGDFVLKQYNQERykmyNSDLLIQALQQQQRLHNNGVSCPRVLIYKNNVMHISKSDER 107
Cdd:cd05153    15 ELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRR----SAAELPFELELLDHLAQAGLPVPRPLADKDGELLGELNGKP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 108 FIVLEHKEGslVSPGKVNQKEIHSLGQTIGYMHNLLNDgslikgenpkFVPPTKEARLKHWE----DKRREVEKLGKEHI 183
Cdd:cd05153    91 AALFPFLPG--ESLTTPTPEQCRAIGAALARLHLALAG----------FPPPRPNPRGLAWWkplaERLKARLDLLAADD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 184 LPYIKLQQEATQlvnTEQFHNSQRAWVHRDLWVDNFLFLNDKVSAILDFDRMDYDYVELDIGRVVIS-CALSDGVLNKSL 262
Cdd:cd05153   159 RALLEDELARLQ---ALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNDwCFDDDGKLDPER 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1197863592 263 VASFLEGYR-------NEVD-FPVGNIVRAIQM-LWYMestWWIHANMDQHSVPPSRFADEMNWIA 319
Cdd:cd05153   236 AKALLAGYQsvrplteEEKAaLPLLLRAAALRFwLSRL---YDFHLPREGALVTPKDPDEFLRRLR 298
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
41-322 1.41e-23

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: 98.46  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  41 NLKWKLETDAG-DFVLKQYNQERYkmyNSDLLIQALQQQQRLHNNGVSCPRVLIYKNNVMHISKSDERFIVLEHKEGSlv 119
Cdd:COG2334    26 NRNYRVETEDGrRYVLKLYRPGRW---SPEEIPFELALLAHLAAAGLPVPAPVPTRDGETLLELEGRPAALFPFLPGR-- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 120 SPGKVNQKEIHSLGQTIGYMHNLLNDgslikgenpkFVPPTkEARLKHWedkRREVEKLGKEHIL--PYIKLQQEATQLV 197
Cdd:COG2334   101 SPEEPSPEQLEELGRLLARLHRALAD----------FPRPN-ARDLAWW---DELLERLLGPLLPdpEDRALLEELLDRL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 198 NT---EQFHNSQRAWVHRDLWVDNFLFLNDKVSAILDFDRMDYDYVELDIGrVVIScALSDGVLNKSLVASFLEGYRNEV 274
Cdd:COG2334   167 EArlaPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLA-IALN-GWADGPLDPARLAALLEGYRAVR 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1197863592 275 DFPVGNI--VRAIQMLWYMESTWWIHANMDQHSVPPSRFADEMNWIAENY 322
Cdd:COG2334   245 PLTEAELaaLPPLLRLRALRFLAWRLRRVRAKDPAFERYLRRQIALAWAA 294
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
34-276 1.90e-13

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: 68.68  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  34 PIHRGWLNLKWKLETDAGDFVLKQYNQERYKmynsDLLIQALQQQQRLHNNGVS-CPRVLIYKNNVMHISKsdeRFIVLE 112
Cdd:pfam01636   4 PISSGASNRTYLVTTGDGRYVLRLPPPGRAA----EELRRELALLRHLAAAGVPpVPRVLAGCTDAELLGL---PFLLME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 113 HKEGSLVSPG--KVNQKEIH-SLGQTIGYMHNLlndgslikgenpkfvpPTKEARLKHWEDKRREVEKLGKEHILPYIKL 189
Cdd:pfam01636  77 YLPGEVLARPllPEERGALLeALGRALARLHAV----------------DPAALPLAGRLARLLELLRQLEAALARLLAA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 190 QQEATQLVNTEQFHN---------SQRAWVHRDLWVDNFLFL-NDKVSAILDFDRMDYDYVELDIGRVVIS-CALSDGVL 258
Cdd:pfam01636 141 ELLDRLEELEERLLAallallpaeLPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAILLNSwGRELGAEL 220
                         250
                  ....*....|....*...
gi 1197863592 259 NKSLVASFLEGYRNEVDF 276
Cdd:pfam01636 221 LAAYLAAYGAFGYARLRE 238
PRK05231 PRK05231
homoserine kinase; Provisional
82-270 2.13e-06

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 48.64  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  82 HNNGVSCPRVLIyknnvmhiSKSDERFIVLEHKEGSLVS--PGK----VNQKEIHSLGQTIGYMHNLLNDGSLiKGENPK 155
Cdd:PRK05231   72 AARGVPVPAPVA--------RRDGAALGELAGKPAAIVTflEGKwpraPTAAHCAEVGEMLARMHLAGRDFPL-ERPNLR 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 156 FVPPTKEARLKHWEDKRREVEKLgkehilpyikLQQE-ATQLVNTEQFHNSQ--RAWVHRDLWVDNFLFLNDKVSAILDF 232
Cdd:PRK05231  143 GLAWWRELAPRLLPFLADEQAAL----------LEAElAAQLAFLASAAWPAlpRGVIHADLFRDNVLFEGDRLSGFIDF 212
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1197863592 233 -----DRMDYDyveldigrVVIS----CALSDGVLNKSLVASFLEGY 270
Cdd:PRK05231  213 yfacnDKLLYD--------VAITlndwCFEADGSLDATKARALLAAY 251
 
Name Accession Description Interval E-value
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
28-319 6.33e-26

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase 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: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 104.65  E-value: 6.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  28 KIRNAIPIHRGWLNLKWKLETDAGDFVLKQYNQERykmyNSDLLIQALQQQQRLHNNGVSCPRVLIYKNNVMHISKSDER 107
Cdd:cd05153    15 ELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRR----SAAELPFELELLDHLAQAGLPVPRPLADKDGELLGELNGKP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 108 FIVLEHKEGslVSPGKVNQKEIHSLGQTIGYMHNLLNDgslikgenpkFVPPTKEARLKHWE----DKRREVEKLGKEHI 183
Cdd:cd05153    91 AALFPFLPG--ESLTTPTPEQCRAIGAALARLHLALAG----------FPPPRPNPRGLAWWkplaERLKARLDLLAADD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 184 LPYIKLQQEATQlvnTEQFHNSQRAWVHRDLWVDNFLFLNDKVSAILDFDRMDYDYVELDIGRVVIS-CALSDGVLNKSL 262
Cdd:cd05153   159 RALLEDELARLQ---ALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNDwCFDDDGKLDPER 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1197863592 263 VASFLEGYR-------NEVD-FPVGNIVRAIQM-LWYMestWWIHANMDQHSVPPSRFADEMNWIA 319
Cdd:cd05153   236 AKALLAGYQsvrplteEEKAaLPLLLRAAALRFwLSRL---YDFHLPREGALVTPKDPDEFLRRLR 298
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
41-322 1.41e-23

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: 98.46  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  41 NLKWKLETDAG-DFVLKQYNQERYkmyNSDLLIQALQQQQRLHNNGVSCPRVLIYKNNVMHISKSDERFIVLEHKEGSlv 119
Cdd:COG2334    26 NRNYRVETEDGrRYVLKLYRPGRW---SPEEIPFELALLAHLAAAGLPVPAPVPTRDGETLLELEGRPAALFPFLPGR-- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 120 SPGKVNQKEIHSLGQTIGYMHNLLNDgslikgenpkFVPPTkEARLKHWedkRREVEKLGKEHIL--PYIKLQQEATQLV 197
Cdd:COG2334   101 SPEEPSPEQLEELGRLLARLHRALAD----------FPRPN-ARDLAWW---DELLERLLGPLLPdpEDRALLEELLDRL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 198 NT---EQFHNSQRAWVHRDLWVDNFLFLNDKVSAILDFDRMDYDYVELDIGrVVIScALSDGVLNKSLVASFLEGYRNEV 274
Cdd:COG2334   167 EArlaPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLA-IALN-GWADGPLDPARLAALLEGYRAVR 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1197863592 275 DFPVGNI--VRAIQMLWYMESTWWIHANMDQHSVPPSRFADEMNWIAENY 322
Cdd:COG2334   245 PLTEAELaaLPPLLRLRALRFLAWRLRRVRAKDPAFERYLRRQIALAWAA 294
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
34-276 1.90e-13

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: 68.68  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  34 PIHRGWLNLKWKLETDAGDFVLKQYNQERYKmynsDLLIQALQQQQRLHNNGVS-CPRVLIYKNNVMHISKsdeRFIVLE 112
Cdd:pfam01636   4 PISSGASNRTYLVTTGDGRYVLRLPPPGRAA----EELRRELALLRHLAAAGVPpVPRVLAGCTDAELLGL---PFLLME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 113 HKEGSLVSPG--KVNQKEIH-SLGQTIGYMHNLlndgslikgenpkfvpPTKEARLKHWEDKRREVEKLGKEHILPYIKL 189
Cdd:pfam01636  77 YLPGEVLARPllPEERGALLeALGRALARLHAV----------------DPAALPLAGRLARLLELLRQLEAALARLLAA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 190 QQEATQLVNTEQFHN---------SQRAWVHRDLWVDNFLFL-NDKVSAILDFDRMDYDYVELDIGRVVIS-CALSDGVL 258
Cdd:pfam01636 141 ELLDRLEELEERLLAallallpaeLPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAILLNSwGRELGAEL 220
                         250
                  ....*....|....*...
gi 1197863592 259 NKSLVASFLEGYRNEVDF 276
Cdd:pfam01636 221 LAAYLAAYGAFGYARLRE 238
PRK05231 PRK05231
homoserine kinase; Provisional
82-270 2.13e-06

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 48.64  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  82 HNNGVSCPRVLIyknnvmhiSKSDERFIVLEHKEGSLVS--PGK----VNQKEIHSLGQTIGYMHNLLNDGSLiKGENPK 155
Cdd:PRK05231   72 AARGVPVPAPVA--------RRDGAALGELAGKPAAIVTflEGKwpraPTAAHCAEVGEMLARMHLAGRDFPL-ERPNLR 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 156 FVPPTKEARLKHWEDKRREVEKLgkehilpyikLQQE-ATQLVNTEQFHNSQ--RAWVHRDLWVDNFLFLNDKVSAILDF 232
Cdd:PRK05231  143 GLAWWRELAPRLLPFLADEQAAL----------LEAElAAQLAFLASAAWPAlpRGVIHADLFRDNVLFEGDRLSGFIDF 212
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1197863592 233 -----DRMDYDyveldigrVVIS----CALSDGVLNKSLVASFLEGY 270
Cdd:PRK05231  213 yfacnDKLLYD--------VAITlndwCFEADGSLDATKARALLAAY 251
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
205-271 4.11e-04

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 41.64  E-value: 4.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1197863592 205 SQRAWVHRDLWVDNFLFLND--KVSAILDFDRMDYDYVELDIGRVVISCALSDGVLNKSlvASFLEGYR 271
Cdd:COG3173   190 GPPVLVHGDLRPGNLLVDPDdgRLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPR--AAFLAAYE 256
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
15-273 8.75e-04

Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444583 [Multi-domain]  Cd Length: 331  Bit Score: 40.65  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  15 QELKVECETLFEFKIRNAIPIhRGwlnlKWKLETDAGDFVLKQYNQERYKMYNSDlliqalQQQQRLHNNGVS-CPRVLI 93
Cdd:COG5881     2 EELIEEILENYDLKIESIKPV-RG----VYKIETDQGPKCLKKIKYSPERLLFIY------EAQEHLKKNGFNnIPRIVP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592  94 YKNNVMHISKSDERFIVLEH---KEGSLVSPgkvnqKEIHSLGQTIGYMHNLLndgsliKGENPKFVPPTKEAR---LKH 167
Cdd:COG5881    71 TKDGKPYVKYGGKLYYLTEWiegRECDYKNP-----EDLKKAAETLAEFHKAS------KGFEPPPGSKGRSHLgkwPER 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197863592 168 WEDKRREVEKLGK----------------EHILPYIKLQQEATQLVNTEQFHN----SQRAW--VHRDLWVDNFLFLNDK 225
Cdd:COG5881   140 FEKRLEELEKFKKiaekkknknefdrlflKNIDYFLEQAEKALELLEKSAYYKlvkeAKKEGgfCHHDYAYHNILIDEDG 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1197863592 226 VSAILDFDRMDYDYVELDIGRVVISCaLSDGVLNKSLVASFLEGYRNE 273
Cdd:COG5881   220 KIYIIDFDYCIYDLPVHDLAKLLRRV-MKRGNWDIEKAKEILEAYNKI 266
 
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