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Conserved domains on  [gi|490251413|ref|WP_004149458|]
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MULTISPECIES: metal ABC transporter permease [Klebsiella]

Protein Classification

metal ABC transporter permease( domain architecture ID 11437853)

metal ABC transporter permease is the transmembrane subunit (TM) of a Periplasmic Binding Protein (PBP)-dependent ABC transporter complex that facilitates the ABC transport of specific metal ions such as manganese or zinc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZnuB COG1108
ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and ...
13-275 3.49e-56

ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and metabolism];


:

Pssm-ID: 440725  Cd Length: 260  Bit Score: 181.78  E-value: 3.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  13 FGFMRRALVVCLALSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLSgmslLAMTLGGFIAGIVVALVAGWVSRR 92
Cdd:COG1108    1 YDFMQRALLAGLLVGLACGLLGVFLVLRRMSLIGDALSHAALPGVALAFLLG----LSPLLGALVAGLLAALLIGLLRRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  93 TPLKEDASFAGFYLGSLALGVTLVSL-RGSSVDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFDSAW 171
Cdd:COG1108   77 SRLKEDTAIGIVFSGGFALGVLLISLvPGSAVDLMSYLFGSILAVSRSDLLLLAVLAAVVLLLLLLFYRELLLVSFDPEL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 172 LQVNHRRlPALLHGLFLALLVLNLVAGFQVLGTLMAVGVMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSWAIS 251
Cdd:COG1108  157 ARASGLP-VRLLHLLLLVLLALTVVAALQAVGALLVSALLIIPAATARLLTRSLRRMLLLAVLIGVLSSVLGLYLSYYLD 235
                        250       260
                 ....*....|....*....|....
gi 490251413 252 LPAGPAIVLTASALFFVSLFFGTR 275
Cdd:COG1108  236 LPTGPTIVLVAGLLFLLSLLFSPR 259
 
Name Accession Description Interval E-value
ZnuB COG1108
ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and ...
13-275 3.49e-56

ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and metabolism];


Pssm-ID: 440725  Cd Length: 260  Bit Score: 181.78  E-value: 3.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  13 FGFMRRALVVCLALSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLSgmslLAMTLGGFIAGIVVALVAGWVSRR 92
Cdd:COG1108    1 YDFMQRALLAGLLVGLACGLLGVFLVLRRMSLIGDALSHAALPGVALAFLLG----LSPLLGALVAGLLAALLIGLLRRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  93 TPLKEDASFAGFYLGSLALGVTLVSL-RGSSVDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFDSAW 171
Cdd:COG1108   77 SRLKEDTAIGIVFSGGFALGVLLISLvPGSAVDLMSYLFGSILAVSRSDLLLLAVLAAVVLLLLLLFYRELLLVSFDPEL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 172 LQVNHRRlPALLHGLFLALLVLNLVAGFQVLGTLMAVGVMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSWAIS 251
Cdd:COG1108  157 ARASGLP-VRLLHLLLLVLLALTVVAALQAVGALLVSALLIIPAATARLLTRSLRRMLLLAVLIGVLSSVLGLYLSYYLD 235
                        250       260
                 ....*....|....*....|....
gi 490251413 252 LPAGPAIVLTASALFFVSLFFGTR 275
Cdd:COG1108  236 LPTGPTIVLVAGLLFLLSLLFSPR 259
AztB NF040871
zinc ABC transporter permease AztB;
12-262 6.45e-55

zinc ABC transporter permease AztB;


Pssm-ID: 468808  Cd Length: 254  Bit Score: 178.25  E-value: 6.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  12 EFGFMRRALVVCLALSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLSGmsllAMTLGGFIAGIVVALVAGWVSR 91
Cdd:NF040871   8 EVDFVQRALVGGVLVSLVCAPVGTWVVLRGMAFLGDAMSHGMLPGVALAFLLGG----PLTLGAAVSAAAMALGVGALSR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  92 RTPLKEDASFAGFYLGSLALGVTLVSLRGS-SVDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFDSA 170
Cdd:NF040871  84 SRRLSEDTSIGLLFVGMLALGVIIVSHSGSfAVDLTGFLFGDVLAVRDADLALLAGALAVTLAVAALFHRAFVALAFDPR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 171 WLQVNHRRlPALLHGLFLALLVLNLVAGFQVLGTLMAVGVMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSWAI 250
Cdd:NF040871 164 KASTLGLR-PRLAHAALLGLVTLAVVASFQAVGTLLVVGLLIAPAAAARLWARRIPTMMALAALLGAAAVVGGLLISWHA 242
                        250
                 ....*....|..
gi 490251413 251 SLPAGPAIVLTA 262
Cdd:NF040871 243 STAAGATIAASA 254
ABC-3 pfam00950
ABC 3 transport family;
15-273 5.04e-37

ABC 3 transport family;


Pssm-ID: 334323  Cd Length: 258  Bit Score: 131.97  E-value: 5.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413   15 FMRRALVVCLALSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLSGmsllAMTLGGFIAGIVVALVAGWVSRRTP 94
Cdd:pfam00950   4 FMQRALLASILVSLACGILGSFLVLRRQSLMGDALSHAALPGVALAYFLGI----NPAIGAFVFGLIAAVAMGYLKRKTR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413   95 LKEDASFAGFYLGSLALGVTLVSL-RGSSVDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFDSAWLQ 173
Cdd:pfam00950  80 LKEDTAIGIVFSTFLALGLVLISLiPGSAVDLDSYLFGNILTISQQDLIQIAIITAVILILLLLFWKELLLITFDPDHAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  174 VNHRRlPALLHGLFLALLVLNLVAGFQVLGTLMAVGVMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSWAISLP 253
Cdd:pfam00950 160 VIGLP-VQFLYLLLLALIALTIVVALQAVGAILVIALLIIPAATARRLTRSFDSMLIIAILIGMVSCVAGLYLSYYFDTS 238
                         250       260
                  ....*....|....*....|
gi 490251413  254 AGPAIVLTASALFFVSLFFG 273
Cdd:pfam00950 239 TGPVIVLIATLLFLISLAFA 258
TM_ABC_iron-siderophores_like cd06550
Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
16-270 1.94e-15

Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters involved in the uptake of siderophores, heme, vitamin B12, or the divalent cations Mg2+ and Zn2+. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The TMs are bundles of alpha helices that transverse the cytoplasmic membrane multiple times. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Each TM has a prominent cytoplasmic loop which contacts an ABC and represents a conserved motif. The two TMs form either a homodimer (e.g. in the case of the BtuC subunits of the Escherichia coli BtuCD vitamin B12 transporter), a heterodimer (e.g. the TroC and TroD subunits of the Treponema pallidum general transition metal transporter, TroBCD), or a pseudo-heterodimer (e.g. the FhuB protein of the E. coli ferrichrome transporter, FhuBC). FhuB contains two tandem TMs which associate to form the pseudo-heterodimer. Both FhuB TMs are found in this hierarchy.


Pssm-ID: 119348 [Multi-domain]  Cd Length: 261  Bit Score: 74.13  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  16 MRRALVVCLALSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLSG----MSLLAMTLGGFIAGIVVALVAGWVSR 91
Cdd:cd06550    1 LLAALLVGAALAVSGAILQSLTRNRLASPSILGISHGALLGVVLALLLGIglsnYALGAFAFAGALAIALLVLLLASRGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  92 RTPLKEdaSFAGFYLGS-LALGVTLVSLRGSS--VDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFD 168
Cdd:cd06550   81 LSPSKL--ILIGIVLSAfFSAGVILISLLSDDslQDLNIWLFGSILGVTWEDLLILLIILLLVLLLLLLLSRKLNLLTFD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 169 SAWLQVNHRRlPALLHGLFLALLVLNLVAGFQVLGTLMAVGvMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSW 248
Cdd:cd06550  159 EDLAKSLGIN-VNLLRLLLLLLVALLVVAAVALVGVILFVG-LIAPHLARRLFGRSHRYLLPLSALLGAILLLLGDLLSR 236
                        250       260
                 ....*....|....*....|....*
gi 490251413 249 AIS---LPAGPAIVLTASALFFVSL 270
Cdd:cd06550  237 TLLpseLPVGPVTALLGAPYFLYLL 261
znuB PRK09543
zinc ABC transporter permease subunit ZnuB;
26-270 6.72e-15

zinc ABC transporter permease subunit ZnuB;


Pssm-ID: 181938  Cd Length: 261  Bit Score: 72.80  E-value: 6.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  26 LSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLS---GMSLLAMTLggfiagiVVALVAGWVSRRTPLKEDASFA 102
Cdd:PRK09543  15 LACAAGPLGSFVVWRRMSYFGDTLAHASLLGVAFGLLLDvnpFYAVIAVTL-------LLAGGLVWLEKRPQLAIDTLLG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 103 GFYLGSLALGVTLVSLRGS-SVDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFDSAWLQVNHRRLpA 181
Cdd:PRK09543  88 IMAHSALSLGLVVVSLMSNvRVDLMAYLFGDLLAVTPEDLISIAIGVVIVLAILFWQWRNLLSMTISPDLAFVDGVKL-Q 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 182 LLHGLFLALLVLNLVAGFQVLGTLMAVGVMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSWAISLPAGPAIVLT 261
Cdd:PRK09543 167 RVKLLLMLVTALTIGVAMKFVGALIITSLLIIPAATARRFARTPEQMAGVAVLVGMLAVTGGLTFSAFYDTPAGPSVVLC 246

                 ....*....
gi 490251413 262 ASALFFVSL 270
Cdd:PRK09543 247 AALLFILSM 255
 
Name Accession Description Interval E-value
ZnuB COG1108
ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and ...
13-275 3.49e-56

ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and metabolism];


Pssm-ID: 440725  Cd Length: 260  Bit Score: 181.78  E-value: 3.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  13 FGFMRRALVVCLALSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLSgmslLAMTLGGFIAGIVVALVAGWVSRR 92
Cdd:COG1108    1 YDFMQRALLAGLLVGLACGLLGVFLVLRRMSLIGDALSHAALPGVALAFLLG----LSPLLGALVAGLLAALLIGLLRRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  93 TPLKEDASFAGFYLGSLALGVTLVSL-RGSSVDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFDSAW 171
Cdd:COG1108   77 SRLKEDTAIGIVFSGGFALGVLLISLvPGSAVDLMSYLFGSILAVSRSDLLLLAVLAAVVLLLLLLFYRELLLVSFDPEL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 172 LQVNHRRlPALLHGLFLALLVLNLVAGFQVLGTLMAVGVMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSWAIS 251
Cdd:COG1108  157 ARASGLP-VRLLHLLLLVLLALTVVAALQAVGALLVSALLIIPAATARLLTRSLRRMLLLAVLIGVLSSVLGLYLSYYLD 235
                        250       260
                 ....*....|....*....|....
gi 490251413 252 LPAGPAIVLTASALFFVSLFFGTR 275
Cdd:COG1108  236 LPTGPTIVLVAGLLFLLSLLFSPR 259
AztB NF040871
zinc ABC transporter permease AztB;
12-262 6.45e-55

zinc ABC transporter permease AztB;


Pssm-ID: 468808  Cd Length: 254  Bit Score: 178.25  E-value: 6.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  12 EFGFMRRALVVCLALSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLSGmsllAMTLGGFIAGIVVALVAGWVSR 91
Cdd:NF040871   8 EVDFVQRALVGGVLVSLVCAPVGTWVVLRGMAFLGDAMSHGMLPGVALAFLLGG----PLTLGAAVSAAAMALGVGALSR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  92 RTPLKEDASFAGFYLGSLALGVTLVSLRGS-SVDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFDSA 170
Cdd:NF040871  84 SRRLSEDTSIGLLFVGMLALGVIIVSHSGSfAVDLTGFLFGDVLAVRDADLALLAGALAVTLAVAALFHRAFVALAFDPR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 171 WLQVNHRRlPALLHGLFLALLVLNLVAGFQVLGTLMAVGVMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSWAI 250
Cdd:NF040871 164 KASTLGLR-PRLAHAALLGLVTLAVVASFQAVGTLLVVGLLIAPAAAARLWARRIPTMMALAALLGAAAVVGGLLISWHA 242
                        250
                 ....*....|..
gi 490251413 251 SLPAGPAIVLTA 262
Cdd:NF040871 243 STAAGATIAASA 254
ABC-3 pfam00950
ABC 3 transport family;
15-273 5.04e-37

ABC 3 transport family;


Pssm-ID: 334323  Cd Length: 258  Bit Score: 131.97  E-value: 5.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413   15 FMRRALVVCLALSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLSGmsllAMTLGGFIAGIVVALVAGWVSRRTP 94
Cdd:pfam00950   4 FMQRALLASILVSLACGILGSFLVLRRQSLMGDALSHAALPGVALAYFLGI----NPAIGAFVFGLIAAVAMGYLKRKTR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413   95 LKEDASFAGFYLGSLALGVTLVSL-RGSSVDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFDSAWLQ 173
Cdd:pfam00950  80 LKEDTAIGIVFSTFLALGLVLISLiPGSAVDLDSYLFGNILTISQQDLIQIAIITAVILILLLLFWKELLLITFDPDHAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  174 VNHRRlPALLHGLFLALLVLNLVAGFQVLGTLMAVGVMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSWAISLP 253
Cdd:pfam00950 160 VIGLP-VQFLYLLLLALIALTIVVALQAVGAILVIALLIIPAATARRLTRSFDSMLIIAILIGMVSCVAGLYLSYYFDTS 238
                         250       260
                  ....*....|....*....|
gi 490251413  254 AGPAIVLTASALFFVSLFFG 273
Cdd:pfam00950 239 TGPVIVLIATLLFLISLAFA 258
TM_ABC_iron-siderophores_like cd06550
Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
16-270 1.94e-15

Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters involved in the uptake of siderophores, heme, vitamin B12, or the divalent cations Mg2+ and Zn2+. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The TMs are bundles of alpha helices that transverse the cytoplasmic membrane multiple times. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Each TM has a prominent cytoplasmic loop which contacts an ABC and represents a conserved motif. The two TMs form either a homodimer (e.g. in the case of the BtuC subunits of the Escherichia coli BtuCD vitamin B12 transporter), a heterodimer (e.g. the TroC and TroD subunits of the Treponema pallidum general transition metal transporter, TroBCD), or a pseudo-heterodimer (e.g. the FhuB protein of the E. coli ferrichrome transporter, FhuBC). FhuB contains two tandem TMs which associate to form the pseudo-heterodimer. Both FhuB TMs are found in this hierarchy.


Pssm-ID: 119348 [Multi-domain]  Cd Length: 261  Bit Score: 74.13  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  16 MRRALVVCLALSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLSG----MSLLAMTLGGFIAGIVVALVAGWVSR 91
Cdd:cd06550    1 LLAALLVGAALAVSGAILQSLTRNRLASPSILGISHGALLGVVLALLLGIglsnYALGAFAFAGALAIALLVLLLASRGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  92 RTPLKEdaSFAGFYLGS-LALGVTLVSLRGSS--VDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFD 168
Cdd:cd06550   81 LSPSKL--ILIGIVLSAfFSAGVILISLLSDDslQDLNIWLFGSILGVTWEDLLILLIILLLVLLLLLLLSRKLNLLTFD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 169 SAWLQVNHRRlPALLHGLFLALLVLNLVAGFQVLGTLMAVGvMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSW 248
Cdd:cd06550  159 EDLAKSLGIN-VNLLRLLLLLLVALLVVAAVALVGVILFVG-LIAPHLARRLFGRSHRYLLPLSALLGAILLLLGDLLSR 236
                        250       260
                 ....*....|....*....|....*
gi 490251413 249 AIS---LPAGPAIVLTASALFFVSL 270
Cdd:cd06550  237 TLLpseLPVGPVTALLGAPYFLYLL 261
znuB PRK09543
zinc ABC transporter permease subunit ZnuB;
26-270 6.72e-15

zinc ABC transporter permease subunit ZnuB;


Pssm-ID: 181938  Cd Length: 261  Bit Score: 72.80  E-value: 6.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413  26 LSLSTTMLGVFLLLRRMSLMGDALSHAILPGVAVGYLLS---GMSLLAMTLggfiagiVVALVAGWVSRRTPLKEDASFA 102
Cdd:PRK09543  15 LACAAGPLGSFVVWRRMSYFGDTLAHASLLGVAFGLLLDvnpFYAVIAVTL-------LLAGGLVWLEKRPQLAIDTLLG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 103 GFYLGSLALGVTLVSLRGS-SVDLLHLLFGSILAVDRDAALFVSGVASLTLLCIALCYRGLVSEAFDSAWLQVNHRRLpA 181
Cdd:PRK09543  88 IMAHSALSLGLVVVSLMSNvRVDLMAYLFGDLLAVTPEDLISIAIGVVIVLAILFWQWRNLLSMTISPDLAFVDGVKL-Q 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490251413 182 LLHGLFLALLVLNLVAGFQVLGTLMAVGVMMLPAVAARCWARTLPGILLLAAGMGALCAWLGLSLSWAISLPAGPAIVLT 261
Cdd:PRK09543 167 RVKLLLMLVTALTIGVAMKFVGALIITSLLIIPAATARRFARTPEQMAGVAVLVGMLAVTGGLTFSAFYDTPAGPSVVLC 246

                 ....*....
gi 490251413 262 ASALFFVSL 270
Cdd:PRK09543 247 AALLFILSM 255
 
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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