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Conserved domains on  [gi|1307852808|gb|AUD73425|]
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phosphotransferase family [Bifidobacterium breve]

Protein Classification

phosphotransferase enzyme family protein( domain architecture ID 11457111)

phosphotransferase enzyme family protein such as serine/threonine protein kinase RdoA, type II homoserine kinase, N-acetylhexosamine 1-kinase, hydroxylysine kinase, and amicoumacin kinase, all of which play crucial roles in transferring phosphate groups to specific substrates

CATH:  1.10.510.10
Gene Ontology:  GO:0016301|GO:0005524|GO:0016310
PubMed:  16244704
SCOP:  3000066

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
6-312 2.54e-29

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: 114.64  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808   6 ETLFDIASHFALeGNIISVEPYGDGhINTTYLVVT-DGPHYILQRMNTSiFPDTVNLMRNVELvTSALKARGKETLDIVP 84
Cdd:COG2334     1 DELAAALERYGL-GPLSSLKPLNSG-ENRNYRVETeDGRRYVLKLYRPG-RWSPEEIPFELAL-LAHLAAAGLPVPAPVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  85 TTSGATWEEIDGGAWRVYKFIE-HTVSynlVPNPDVFREAGRAFGDFQNFLSGFDagqltetIAHFHDTPHRFEDFKAAL 163
Cdd:COG2334    77 TRDGETLLELEGRPAALFPFLPgRSPE---EPSPEQLEELGRLLARLHRALADFP-------RPNARDLAWWDELLERLL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808 164 AADKL--GRAASCQPEIDFYLAHADQYAtvmdglkdGSIPLRVTHNDTKLNNILMDatTGKARAIIDLDTIMPGSMLFDF 241
Cdd:COG2334   147 GPLLPdpEDRALLEELLDRLEARLAPLL--------GALPRGVIHGDLHPDNVLFD--GDGVSGLIDFDDAGYGPRLYDL 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307852808 242 GDSIRFGAstalEDEKDLDKVHfstELFRAYAEgfVGELrgsiTEREAELLafsgNLLTMECGMRFLADYL 312
Cdd:COG2334   217 AIALNGWA----DGPLDPARLA---ALLEGYRA--VRPL----TEAELAAL----PPLLRLRALRFLAWRL 270
 
Name Accession Description Interval E-value
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
6-312 2.54e-29

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: 114.64  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808   6 ETLFDIASHFALeGNIISVEPYGDGhINTTYLVVT-DGPHYILQRMNTSiFPDTVNLMRNVELvTSALKARGKETLDIVP 84
Cdd:COG2334     1 DELAAALERYGL-GPLSSLKPLNSG-ENRNYRVETeDGRRYVLKLYRPG-RWSPEEIPFELAL-LAHLAAAGLPVPAPVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  85 TTSGATWEEIDGGAWRVYKFIE-HTVSynlVPNPDVFREAGRAFGDFQNFLSGFDagqltetIAHFHDTPHRFEDFKAAL 163
Cdd:COG2334    77 TRDGETLLELEGRPAALFPFLPgRSPE---EPSPEQLEELGRLLARLHRALADFP-------RPNARDLAWWDELLERLL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808 164 AADKL--GRAASCQPEIDFYLAHADQYAtvmdglkdGSIPLRVTHNDTKLNNILMDatTGKARAIIDLDTIMPGSMLFDF 241
Cdd:COG2334   147 GPLLPdpEDRALLEELLDRLEARLAPLL--------GALPRGVIHGDLHPDNVLFD--GDGVSGLIDFDDAGYGPRLYDL 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307852808 242 GDSIRFGAstalEDEKDLDKVHfstELFRAYAEgfVGELrgsiTEREAELLafsgNLLTMECGMRFLADYL 312
Cdd:COG2334   217 AIALNGWA----DGPLDPARLA---ALLEGYRA--VRPL----TEAELAAL----PPLLRLRALRFLAWRL 270
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
23-248 2.96e-18

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: 82.93  E-value: 2.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  23 SVEPYGDGHINTTYLVVTDGPHYILQRMNTSIFPDTVNLMRNvelVTSALKARGKETldiVPTT-SGATWEEIDGGAWRV 101
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDGRYVLRLPPPGRAAEELRRELA---LLRHLAAAGVPP---VPRVlAGCTDAELLGLPFLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808 102 YKFIEHTVSYNlVPNPDVFREAGRAFGDFQNFLSGFDAGQLTETiahfHDTPHRFEDFKAALAADKLGRAASCQPEIdfy 181
Cdd:pfam01636  75 MEYLPGEVLAR-PLLPEERGALLEALGRALARLHAVDPAALPLA----GRLARLLELLRQLEAALARLLAAELLDRL--- 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1307852808 182 LAHADQYATVMDGLKDGSIPLRVTHNDTKLNNILMDAtTGKARAIIDLDTIMPGSMLFDFGDSIRFG 248
Cdd:pfam01636 147 EELEERLLAALLALLPAELPPVLVHGDLHPGNLLVDP-GGRVSGVIDFEDAGLGDPAYDLAILLNSW 212
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
6-292 1.17e-12

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: 67.67  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808   6 ETLFDIASHFALeGNIISVEPYGDGHINTTYLVVTDGPHYILqrmntSIFPDTVN---LMRNVELvTSALKARGKETLDI 82
Cdd:cd05153     2 EELAEFLAHYDL-GELLSFEGIAAGIENTNYFVTTTDGRYVL-----TLFEKRRSaaeLPFELEL-LDHLAQAGLPVPRP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  83 VPTTSGATWEEIDGGAWRVYKFIEHTVSYNlvPNPDVFREAGRAFGDFQNFLSGFDAGQLTE-TIAHFHDTPHRFEDFKA 161
Cdd:cd05153    75 LADKDGELLGELNGKPAALFPFLPGESLTT--PTPEQCRAIGAALARLHLALAGFPPPRPNPrGLAWWKPLAERLKARLD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808 162 ALAADKLGRAAScqpEIDFYLAHADQyatvmdglkdgSIPLRVTHNDTKLNNILMDAttGKARAIIDLDTIMPGSMLFDF 241
Cdd:cd05153   153 LLAADDRALLED---ELARLQALAPS-----------DLPRGVIHADLFRDNVLFDG--DRLSGIIDFYDACYDPLLYDL 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1307852808 242 GDSIRFGAStalEDEKDLDKVHFSTeLFRAYAEgfvgelRGSITEREAELL 292
Cdd:cd05153   217 AIALNDWCF---DDDGKLDPERAKA-LLAGYQS------VRPLTEEEKAAL 257
PRK06148 PRK06148
hypothetical protein; Provisional
12-246 1.86e-03

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 40.39  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808   12 ASHFALEGNIISVepygDGHINTTYLVVT-DGPHYILQRMNTSIfPDTvnlmrNVELVTSALKARGKETLD-----IVPT 85
Cdd:PRK06148    21 AQHFGISATATPL----DGERDLNFRLTTdDGADYILKIVNPSE-PRV-----ESDFQTAALDHLAAVAPDlpvprLIPS 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808   86 TSGATWEEI--DGGAWRVYKFIEH---TVSYNLVPNPD-VFREAGRAFGDFQNFLSGFDagqltetiahfHDTPHRfeDF 159
Cdd:PRK06148    91 LSGASLASAqdPDGEPRLLRLLSWlpgTPLAEAAPRTEaLLDNLGRALGRLDRALQGFM-----------HPGALR--DL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  160 K-----AALAADKLgrAASCQPEIDFYLAHA-DQY-ATVMDGLKdgSIPLRVTHNDTKLNNILMDATTGkaraiidlDTI 232
Cdd:PRK06148   158 DwdlrhAGRARDRL--HFIDDPEDRALVERFlARFeRNVAPRLA--ALPAQVIHNDANDYNILVDADDG--------ERI 225
                          250
                   ....*....|....
gi 1307852808  233 mpgSMLFDFGDSIR 246
Cdd:PRK06148   226 ---SGLIDFGDAVH 236
 
Name Accession Description Interval E-value
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
6-312 2.54e-29

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: 114.64  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808   6 ETLFDIASHFALeGNIISVEPYGDGhINTTYLVVT-DGPHYILQRMNTSiFPDTVNLMRNVELvTSALKARGKETLDIVP 84
Cdd:COG2334     1 DELAAALERYGL-GPLSSLKPLNSG-ENRNYRVETeDGRRYVLKLYRPG-RWSPEEIPFELAL-LAHLAAAGLPVPAPVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  85 TTSGATWEEIDGGAWRVYKFIE-HTVSynlVPNPDVFREAGRAFGDFQNFLSGFDagqltetIAHFHDTPHRFEDFKAAL 163
Cdd:COG2334    77 TRDGETLLELEGRPAALFPFLPgRSPE---EPSPEQLEELGRLLARLHRALADFP-------RPNARDLAWWDELLERLL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808 164 AADKL--GRAASCQPEIDFYLAHADQYAtvmdglkdGSIPLRVTHNDTKLNNILMDatTGKARAIIDLDTIMPGSMLFDF 241
Cdd:COG2334   147 GPLLPdpEDRALLEELLDRLEARLAPLL--------GALPRGVIHGDLHPDNVLFD--GDGVSGLIDFDDAGYGPRLYDL 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307852808 242 GDSIRFGAstalEDEKDLDKVHfstELFRAYAEgfVGELrgsiTEREAELLafsgNLLTMECGMRFLADYL 312
Cdd:COG2334   217 AIALNGWA----DGPLDPARLA---ALLEGYRA--VRPL----TEAELAAL----PPLLRLRALRFLAWRL 270
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
23-248 2.96e-18

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: 82.93  E-value: 2.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  23 SVEPYGDGHINTTYLVVTDGPHYILQRMNTSIFPDTVNLMRNvelVTSALKARGKETldiVPTT-SGATWEEIDGGAWRV 101
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDGRYVLRLPPPGRAAEELRRELA---LLRHLAAAGVPP---VPRVlAGCTDAELLGLPFLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808 102 YKFIEHTVSYNlVPNPDVFREAGRAFGDFQNFLSGFDAGQLTETiahfHDTPHRFEDFKAALAADKLGRAASCQPEIdfy 181
Cdd:pfam01636  75 MEYLPGEVLAR-PLLPEERGALLEALGRALARLHAVDPAALPLA----GRLARLLELLRQLEAALARLLAAELLDRL--- 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1307852808 182 LAHADQYATVMDGLKDGSIPLRVTHNDTKLNNILMDAtTGKARAIIDLDTIMPGSMLFDFGDSIRFG 248
Cdd:pfam01636 147 EELEERLLAALLALLPAELPPVLVHGDLHPGNLLVDP-GGRVSGVIDFEDAGLGDPAYDLAILLNSW 212
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
6-292 1.17e-12

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: 67.67  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808   6 ETLFDIASHFALeGNIISVEPYGDGHINTTYLVVTDGPHYILqrmntSIFPDTVN---LMRNVELvTSALKARGKETLDI 82
Cdd:cd05153     2 EELAEFLAHYDL-GELLSFEGIAAGIENTNYFVTTTDGRYVL-----TLFEKRRSaaeLPFELEL-LDHLAQAGLPVPRP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  83 VPTTSGATWEEIDGGAWRVYKFIEHTVSYNlvPNPDVFREAGRAFGDFQNFLSGFDAGQLTE-TIAHFHDTPHRFEDFKA 161
Cdd:cd05153    75 LADKDGELLGELNGKPAALFPFLPGESLTT--PTPEQCRAIGAALARLHLALAGFPPPRPNPrGLAWWKPLAERLKARLD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808 162 ALAADKLGRAAScqpEIDFYLAHADQyatvmdglkdgSIPLRVTHNDTKLNNILMDAttGKARAIIDLDTIMPGSMLFDF 241
Cdd:cd05153   153 LLAADDRALLED---ELARLQALAPS-----------DLPRGVIHADLFRDNVLFDG--DRLSGIIDFYDACYDPLLYDL 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1307852808 242 GDSIRFGAStalEDEKDLDKVHFSTeLFRAYAEgfvgelRGSITEREAELL 292
Cdd:cd05153   217 AIALNDWCF---DDDGKLDPERAKA-LLAGYQS------VRPLTEEEKAAL 257
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
11-242 9.58e-08

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 52.81  E-value: 9.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  11 IASHFALEGNIISVEPYGDGHINTTYLVvTDGPHYILqRMNTSIFPDTVNLMRNVElVTSALKARgketLDI-VPTT--S 87
Cdd:COG3173    12 LAAQLPGLAGLPEVEPLSGGWSNLTYRL-DTGDRLVL-RRPPRGLASAHDVRREAR-VLRALAPR----LGVpVPRPlaL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  88 GATwEEIDGGAWRVYKFIEHTVSYNLVP--NPDVFREAGRAFGDFQNFLSGFDAgqltetiAHFHDTPHRFEDFKAALA- 164
Cdd:COG3173    85 GED-GEVIGAPFYVMEWVEGETLEDALPdlSPAERRALARALGEFLAALHAVDP-------AAAGLADGRPEGLERQLAr 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1307852808 165 -ADKLGRAASCQPEIDfylAHADQYATVMDGLKDGSIPLRVTHNDTKLNNILMDATTGKARAIIDLDTIMPGSMLFDFG 242
Cdd:COG3173   157 wRAQLRRALARTDDLP---ALRERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDPDDGRLTAVIDWELATLGDPAADLA 232
PRK06148 PRK06148
hypothetical protein; Provisional
12-246 1.86e-03

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 40.39  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808   12 ASHFALEGNIISVepygDGHINTTYLVVT-DGPHYILQRMNTSIfPDTvnlmrNVELVTSALKARGKETLD-----IVPT 85
Cdd:PRK06148    21 AQHFGISATATPL----DGERDLNFRLTTdDGADYILKIVNPSE-PRV-----ESDFQTAALDHLAAVAPDlpvprLIPS 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808   86 TSGATWEEI--DGGAWRVYKFIEH---TVSYNLVPNPD-VFREAGRAFGDFQNFLSGFDagqltetiahfHDTPHRfeDF 159
Cdd:PRK06148    91 LSGASLASAqdPDGEPRLLRLLSWlpgTPLAEAAPRTEaLLDNLGRALGRLDRALQGFM-----------HPGALR--DL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307852808  160 K-----AALAADKLgrAASCQPEIDFYLAHA-DQY-ATVMDGLKdgSIPLRVTHNDTKLNNILMDATTGkaraiidlDTI 232
Cdd:PRK06148   158 DwdlrhAGRARDRL--HFIDDPEDRALVERFlARFeRNVAPRLA--ALPAQVIHNDANDYNILVDADDG--------ERI 225
                          250
                   ....*....|....
gi 1307852808  233 mpgSMLFDFGDSIR 246
Cdd:PRK06148   226 ---SGLIDFGDAVH 236
 
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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