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Conserved domains on  [gi|1958756364|ref|XP_038954326|]
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trimethyllysine dioxygenase, mitochondrial isoform X1 [Rattus norvegicus]

Protein Classification

Fe(II)-2OG oxygenase family protein( domain architecture ID 905)

Fe(II)-2OG oxygenase family protein may catalyze a hydroxylation reaction

Gene Ontology:  GO:0016491

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CAS_like super family cl00184
Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) ...
145-443 1.64e-168

Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) oxygenase carrying out three reactions in the biosynthesis of clavulanic acid, an inhibitor of class A serine beta-lactamases. In general, Fe(II)-2OG oxygenases catalyze a hydroxylation reaction, which leads to the incorporation of an oxygen atom from dioxygen into a hydroxyl group and conversion of 2OG to succinate and CO2


The actual alignment was detected with superfamily member TIGR02410:

Pssm-ID: 444731 [Multi-domain]  Cd Length: 362  Bit Score: 477.73  E-value: 1.64e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 145 PDGHVTRYDLDWLVKNSYEGQKQEVIQPRVLWNAKLYQDAQLPS-VDFQGFLETKEG-----LKKFLQNFLLYGIAFVEN 218
Cdd:TIGR02410  55 PDGHVSKFKEDWLIRHSYEPKKEKNVKALILPNRKIYWLAEFNElKDPSVHFKTTYDhtdstLKSFSKNIYKYGFTFVDN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 219 VPPTQEHTEKLARRVSLIRETIYGRMWYFTSDFSRGDTAYTKLALDRHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDG 298
Cdd:TIGR02410 135 VPVTPEATEKLCERISIIRPTHYGGFWDFTSDLSKNDTAYTSLAIDMHTDGTYWDETPGLQLFHCLTHDGTGGETVLVDG 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 299 FYAAQQVLQRAPEEFDLLSQVPLKHEYIENVGQCHNHMIGVGPILNIYPWNKELYLIRYNNYDRAVINTVP---YDVVRR 375
Cdd:TIGR02410 215 FYCAEQLRKEAPEDFELLTKVPIPHHYSGESDSVFIHPDYPQPVLTLDPSTGELTQIRWNNSDRAVMDCLNwssPYDVPK 294
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958756364 376 WYAAHRTLTTELRRPENELWVKLKPGKVLFIDNWRVLHGRESFTGYRQLCGCYLTRDDVLNTARILGL 443
Cdd:TIGR02410 295 FYKAIRRFNKIITDPDNEIEFKLRPGTVLIFDNWRVLHSRTSFTGYRRMCGCYLTRDDFLARARLLLF 362
 
Name Accession Description Interval E-value
carnitine_TMLD TIGR02410
trimethyllysine dioxygenase; Members of this family with known function act as trimethyllysine ...
145-443 1.64e-168

trimethyllysine dioxygenase; Members of this family with known function act as trimethyllysine dioxygenase, an enzyme in the pathway for carnitine biosynthesis from lysine. This enzyme is homologous to gamma-butyrobetaine,2-oxoglutarate dioxygenase, which catalyzes the last step in carnitine biosynthesis. Members of this family appear to be eukaryotic only.


Pssm-ID: 274119 [Multi-domain]  Cd Length: 362  Bit Score: 477.73  E-value: 1.64e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 145 PDGHVTRYDLDWLVKNSYEGQKQEVIQPRVLWNAKLYQDAQLPS-VDFQGFLETKEG-----LKKFLQNFLLYGIAFVEN 218
Cdd:TIGR02410  55 PDGHVSKFKEDWLIRHSYEPKKEKNVKALILPNRKIYWLAEFNElKDPSVHFKTTYDhtdstLKSFSKNIYKYGFTFVDN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 219 VPPTQEHTEKLARRVSLIRETIYGRMWYFTSDFSRGDTAYTKLALDRHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDG 298
Cdd:TIGR02410 135 VPVTPEATEKLCERISIIRPTHYGGFWDFTSDLSKNDTAYTSLAIDMHTDGTYWDETPGLQLFHCLTHDGTGGETVLVDG 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 299 FYAAQQVLQRAPEEFDLLSQVPLKHEYIENVGQCHNHMIGVGPILNIYPWNKELYLIRYNNYDRAVINTVP---YDVVRR 375
Cdd:TIGR02410 215 FYCAEQLRKEAPEDFELLTKVPIPHHYSGESDSVFIHPDYPQPVLTLDPSTGELTQIRWNNSDRAVMDCLNwssPYDVPK 294
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958756364 376 WYAAHRTLTTELRRPENELWVKLKPGKVLFIDNWRVLHGRESFTGYRQLCGCYLTRDDVLNTARILGL 443
Cdd:TIGR02410 295 FYKAIRRFNKIITDPDNEIEFKLRPGTVLIFDNWRVLHSRTSFTGYRRMCGCYLTRDDFLARARLLLF 362
CAS_like cd00250
Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) ...
166-432 6.30e-95

Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) oxygenase carrying out three reactions in the biosynthesis of clavulanic acid, an inhibitor of class A serine beta-lactamases. In general, Fe(II)-2OG oxygenases catalyze a hydroxylation reaction, which leads to the incorporation of an oxygen atom from dioxygen into a hydroxyl group and conversion of 2OG to succinate and CO2


Pssm-ID: 238154  Cd Length: 262  Bit Score: 286.60  E-value: 6.30e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 166 KQEVIQPRVLWNAKLYqdAQLPSVDFQGFLETKEGLKKFLQNFLLYGIAFVENVPPTQEHTEKLARRVSLIRETIYGRMW 245
Cdd:cd00250     1 LRRFERPAQRLWGSLC--KALPVLSFLEVLELDSPLGKLLLASAGVGFAELEGAPLDPAALLGLAERIGFIRGTLYGDVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 246 YFTSDFSRGDTAYTKLALDRHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAQQVLQRAPEEFDLLSQVPLKHEY 325
Cdd:cd00250    79 PVPGKENAQNGAYTNTLLPLHTDLAYHEYRPGLQILHCLRNTATGGATLLVDGFRVALKLLREDPEAFELLSRVPVRHAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 326 IENVGqCHNHMIGVGPILNIYPwnkELYLIRYNNYDRAvinTVPYDVVRRWYAAHRTLTTELRRPENELWVKLKPGKVLF 405
Cdd:cd00250   159 PGSSG-TMFSSYQLAPVLELDP---EDPVLRYNNYDNF---SVPFDEVKEAYEALAELVALIEDPDNQLTVKLEPGDLLI 231
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958756364 406 IDNWRVLHGRESFTG----YRQLCGCYLTRD 432
Cdd:cd00250   232 FDNRRVLHGRTAFSPryggDRWLKGCYVDRD 262
TauD pfam02668
Taurine catabolism dioxygenase TauD, TfdA family; This family consists of taurine catabolism ...
211-418 7.74e-35

Taurine catabolism dioxygenase TauD, TfdA family; This family consists of taurine catabolism dioxygenases of the TauD, TfdA family. TauD from E. coli is a alpha-ketoglutarate-dependent taurine dioxygenase. This enzyme catalyzes the oxygenolytic release of sulfite from taurine. TfdA from Burkholderia sp. is a 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase. TfdA from Alcaligenes eutrophus JMP134 is a 2,4-dichlorophenoxyacetate monooxygenase. Also included are gamma-Butyrobetaine hydroxylase enzymes EC:1.14.11.1.


Pssm-ID: 367137 [Multi-domain]  Cd Length: 264  Bit Score: 130.26  E-value: 7.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 211 YGIAFVENVPPTQEHTEKLARRVSLIRETI-------YGRMWYFTS---DFSRGDTAYTKLALdrHTDTTYFQEPCGIQV 280
Cdd:pfam02668  37 HGVLLFRGQPLSPEQLLAFARRFGPLYGTPgggrndgYPEVLDVSSvypDADPANTAYTGLPW--HTDLSYLEDPPGIQL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 281 FHCLKHEGTGGRTLLVDGFYAAQQVLQRAPEEFDLLSQVP-----LKHEYIENVGQCHNHMIGVGPILNIYPWNKELYLI 355
Cdd:pfam02668 115 LHCLEAAPEGGETLFADGRAAYNALPEELPELFEGLTAVHsyfryRGEAYPANRPADDKHPPTGHPVVRTHPVTGRKALY 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958756364 356 RYNNYDRAVINtvpyDVVRRWYAAHRTLTTELRRPENELWVKLKPGKVLFIDNWRVLHGRESF 418
Cdd:pfam02668 195 VNPPFATRIVG----LGTPESDEALDALFALATDPEFTYRFKWQPGDLVIWDNRRVLHGRTAF 253
TauD COG2175
Taurine dioxygenase, alpha-ketoglutarate-dependent [Secondary metabolites biosynthesis, ...
184-432 7.92e-15

Taurine dioxygenase, alpha-ketoglutarate-dependent [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441778  Cd Length: 275  Bit Score: 74.22  E-value: 7.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 184 AQLPSVDFQGFLeTKEGLKKFLQNFLLYGIAFVENVPPTQEHTEKLARR------VSLIRETIYGRMWYFTSDfSRGDTA 257
Cdd:COG2175    14 AEITGVDLAAPL-SDATVAELRAALLEHGVLVFRGQPLTDEQQVAFARRfgeleiHPTRPYNLPGHPEIFDVS-NDPADG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 258 YTKLALDRHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAQQVLQRAPEEFDLLSQV-PLKHEYIENVGQCHNHM 336
Cdd:COG2175    92 YTNAGLPWHTDGSFRERPPKGSILYCVEVPPEGGDTLFADMAAAYEALPEELKELLEGLRAVhSFNKDYGRGRPDPEELR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 337 IGVG--------PILNIYPWNKELYLiRYNNYDRAVINTVPYDVVRrwyAAHRTLTTELRRPENELWVKLKPGKVLFIDN 408
Cdd:COG2175   172 EEDDasvppvehPVVRTHPETGRKVL-YVNEGFTTRIVGLSPEESR---ALLDELFAHATRPEFTYRHRWQPGDLVIWDN 247
                         250       260
                  ....*....|....*....|....*.
gi 1958756364 409 WRVLHGRESFTG--YRQLCGCYLTRD 432
Cdd:COG2175   248 RRTLHGATADYGpgRRVLHRVTIAGD 273
 
Name Accession Description Interval E-value
carnitine_TMLD TIGR02410
trimethyllysine dioxygenase; Members of this family with known function act as trimethyllysine ...
145-443 1.64e-168

trimethyllysine dioxygenase; Members of this family with known function act as trimethyllysine dioxygenase, an enzyme in the pathway for carnitine biosynthesis from lysine. This enzyme is homologous to gamma-butyrobetaine,2-oxoglutarate dioxygenase, which catalyzes the last step in carnitine biosynthesis. Members of this family appear to be eukaryotic only.


Pssm-ID: 274119 [Multi-domain]  Cd Length: 362  Bit Score: 477.73  E-value: 1.64e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 145 PDGHVTRYDLDWLVKNSYEGQKQEVIQPRVLWNAKLYQDAQLPS-VDFQGFLETKEG-----LKKFLQNFLLYGIAFVEN 218
Cdd:TIGR02410  55 PDGHVSKFKEDWLIRHSYEPKKEKNVKALILPNRKIYWLAEFNElKDPSVHFKTTYDhtdstLKSFSKNIYKYGFTFVDN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 219 VPPTQEHTEKLARRVSLIRETIYGRMWYFTSDFSRGDTAYTKLALDRHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDG 298
Cdd:TIGR02410 135 VPVTPEATEKLCERISIIRPTHYGGFWDFTSDLSKNDTAYTSLAIDMHTDGTYWDETPGLQLFHCLTHDGTGGETVLVDG 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 299 FYAAQQVLQRAPEEFDLLSQVPLKHEYIENVGQCHNHMIGVGPILNIYPWNKELYLIRYNNYDRAVINTVP---YDVVRR 375
Cdd:TIGR02410 215 FYCAEQLRKEAPEDFELLTKVPIPHHYSGESDSVFIHPDYPQPVLTLDPSTGELTQIRWNNSDRAVMDCLNwssPYDVPK 294
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958756364 376 WYAAHRTLTTELRRPENELWVKLKPGKVLFIDNWRVLHGRESFTGYRQLCGCYLTRDDVLNTARILGL 443
Cdd:TIGR02410 295 FYKAIRRFNKIITDPDNEIEFKLRPGTVLIFDNWRVLHSRTSFTGYRRMCGCYLTRDDFLARARLLLF 362
CAS_like cd00250
Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) ...
166-432 6.30e-95

Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) oxygenase carrying out three reactions in the biosynthesis of clavulanic acid, an inhibitor of class A serine beta-lactamases. In general, Fe(II)-2OG oxygenases catalyze a hydroxylation reaction, which leads to the incorporation of an oxygen atom from dioxygen into a hydroxyl group and conversion of 2OG to succinate and CO2


Pssm-ID: 238154  Cd Length: 262  Bit Score: 286.60  E-value: 6.30e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 166 KQEVIQPRVLWNAKLYqdAQLPSVDFQGFLETKEGLKKFLQNFLLYGIAFVENVPPTQEHTEKLARRVSLIRETIYGRMW 245
Cdd:cd00250     1 LRRFERPAQRLWGSLC--KALPVLSFLEVLELDSPLGKLLLASAGVGFAELEGAPLDPAALLGLAERIGFIRGTLYGDVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 246 YFTSDFSRGDTAYTKLALDRHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAQQVLQRAPEEFDLLSQVPLKHEY 325
Cdd:cd00250    79 PVPGKENAQNGAYTNTLLPLHTDLAYHEYRPGLQILHCLRNTATGGATLLVDGFRVALKLLREDPEAFELLSRVPVRHAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 326 IENVGqCHNHMIGVGPILNIYPwnkELYLIRYNNYDRAvinTVPYDVVRRWYAAHRTLTTELRRPENELWVKLKPGKVLF 405
Cdd:cd00250   159 PGSSG-TMFSSYQLAPVLELDP---EDPVLRYNNYDNF---SVPFDEVKEAYEALAELVALIEDPDNQLTVKLEPGDLLI 231
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958756364 406 IDNWRVLHGRESFTG----YRQLCGCYLTRD 432
Cdd:cd00250   232 FDNRRVLHGRTAFSPryggDRWLKGCYVDRD 262
carnitine_bodg TIGR02409
gamma-butyrobetaine hydroxylase; Members of this protein family are gamma-butyrobetaine ...
145-441 6.57e-64

gamma-butyrobetaine hydroxylase; Members of this protein family are gamma-butyrobetaine hydroxylase, both bacterial and eukarytotic. This enzyme catalyzes the last step in the conversion of lysine to carnitine. Carnitine can serve as a compatible solvent in bacteria and also participates in fatty acid metabolism.


Pssm-ID: 274118 [Multi-domain]  Cd Length: 366  Bit Score: 210.40  E-value: 6.57e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 145 PDGHVTRYDLDWLVKNSYEgqKQEVIQPRV------LWnAKLYQDAQLPSVDFQGFLETKEGLKKFLQNFLLYGIAFVEN 218
Cdd:TIGR02409  66 PDGHLSEFPADWLKKRCYD--KQELRERELffpekqRW-GKATSELSLPTLDFEAVMRDDSVLLDWLSAVRDVGIVVLTG 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 219 VPPTQEHTEKLARRVSLIRETIYGRMWYFTSDFSRGDTAYTKLALDRHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDG 298
Cdd:TIGR02409 143 APTKPGAVSKLGKRIGFIRETNYGHLFEVRDKADANNLAYTNGGLPFHTDNPYRDHPPGLQLLHCLESTVEGGDSEFVDG 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 299 FYAAQQVLQRAPEEFDLLSQVPLKHEYIENVG---QCHNHMIGVGPilniypwNKELYLIRYNNYDRAVINTVPYDVVRR 375
Cdd:TIGR02409 223 FAVAEALRKENPEAFRILSSTPVEFRDIGDDYcdlRSKHPVIELDD-------DGEVVKIRFNNASRDTIFDVPVERVQD 295
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958756364 376 WYAAHRTLTTELRRPENELWVKLKPGKVLFIDNWRVLHGRESF---TGYRQLCGCYLTRDDVLNTARIL 441
Cdd:TIGR02409 296 FYAAYRRFVELIESPRFKFTFKLEPGDLILFDNTRLLHARDAFsatEGKRHLQGCYADWDGLLSRLRAL 364
TauD pfam02668
Taurine catabolism dioxygenase TauD, TfdA family; This family consists of taurine catabolism ...
211-418 7.74e-35

Taurine catabolism dioxygenase TauD, TfdA family; This family consists of taurine catabolism dioxygenases of the TauD, TfdA family. TauD from E. coli is a alpha-ketoglutarate-dependent taurine dioxygenase. This enzyme catalyzes the oxygenolytic release of sulfite from taurine. TfdA from Burkholderia sp. is a 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase. TfdA from Alcaligenes eutrophus JMP134 is a 2,4-dichlorophenoxyacetate monooxygenase. Also included are gamma-Butyrobetaine hydroxylase enzymes EC:1.14.11.1.


Pssm-ID: 367137 [Multi-domain]  Cd Length: 264  Bit Score: 130.26  E-value: 7.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 211 YGIAFVENVPPTQEHTEKLARRVSLIRETI-------YGRMWYFTS---DFSRGDTAYTKLALdrHTDTTYFQEPCGIQV 280
Cdd:pfam02668  37 HGVLLFRGQPLSPEQLLAFARRFGPLYGTPgggrndgYPEVLDVSSvypDADPANTAYTGLPW--HTDLSYLEDPPGIQL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 281 FHCLKHEGTGGRTLLVDGFYAAQQVLQRAPEEFDLLSQVP-----LKHEYIENVGQCHNHMIGVGPILNIYPWNKELYLI 355
Cdd:pfam02668 115 LHCLEAAPEGGETLFADGRAAYNALPEELPELFEGLTAVHsyfryRGEAYPANRPADDKHPPTGHPVVRTHPVTGRKALY 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958756364 356 RYNNYDRAVINtvpyDVVRRWYAAHRTLTTELRRPENELWVKLKPGKVLFIDNWRVLHGRESF 418
Cdd:pfam02668 195 VNPPFATRIVG----LGTPESDEALDALFALATDPEFTYRFKWQPGDLVIWDNRRVLHGRTAF 253
TauD COG2175
Taurine dioxygenase, alpha-ketoglutarate-dependent [Secondary metabolites biosynthesis, ...
184-432 7.92e-15

Taurine dioxygenase, alpha-ketoglutarate-dependent [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441778  Cd Length: 275  Bit Score: 74.22  E-value: 7.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 184 AQLPSVDFQGFLeTKEGLKKFLQNFLLYGIAFVENVPPTQEHTEKLARR------VSLIRETIYGRMWYFTSDfSRGDTA 257
Cdd:COG2175    14 AEITGVDLAAPL-SDATVAELRAALLEHGVLVFRGQPLTDEQQVAFARRfgeleiHPTRPYNLPGHPEIFDVS-NDPADG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 258 YTKLALDRHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAQQVLQRAPEEFDLLSQV-PLKHEYIENVGQCHNHM 336
Cdd:COG2175    92 YTNAGLPWHTDGSFRERPPKGSILYCVEVPPEGGDTLFADMAAAYEALPEELKELLEGLRAVhSFNKDYGRGRPDPEELR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756364 337 IGVG--------PILNIYPWNKELYLiRYNNYDRAVINTVPYDVVRrwyAAHRTLTTELRRPENELWVKLKPGKVLFIDN 408
Cdd:COG2175   172 EEDDasvppvehPVVRTHPETGRKVL-YVNEGFTTRIVGLSPEESR---ALLDELFAHATRPEFTYRHRWQPGDLVIWDN 247
                         250       260
                  ....*....|....*....|....*.
gi 1958756364 409 WRVLHGRESFTG--YRQLCGCYLTRD 432
Cdd:COG2175   248 RRTLHGATADYGpgRRVLHRVTIAGD 273
 
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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