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Conserved domains on  [gi|504697879|ref|WP_014884981|]
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MULTISPECIES: metal ABC transporter permease [Enterobacter]

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 1.37e-54

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


:

Pssm-ID: 440725  Cd Length: 260  Bit Score: 177.55  E-value: 1.37e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  13 YGFMRRALVVCLALSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLLSgmslLAMSIGGFIAGITVALVAGLVSRR 92
Cdd:COG1108    1 YDFMQRALLAGLLVGLACGLLGVFLVLRRMSLIGDALSHAALPGVALAFLLG----LSPLLGALVAGLLAALLIGLLRRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  93 TPLKEDASFAGFYLGSLALGVTLVSL-RGSNVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDTAW 171
Cdd:COG1108   77 SRLKEDTAIGIVFSGGFALGVLLISLvPGSAVDLMSYLFGSILAVSRSDLLLLAVLAAVVLLLLLLFYRELLLVSFDPEL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 172 LQvnARGLPGLLH-GLFLALLVLNLVAGFQVLGTLMAVGLMMLPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLSWAI 250
Cdd:COG1108  157 AR--ASGLPVRLLhLLLLVLLALTVVAALQAVGALLVSALLIIPAATARLLTRSLRRMLLLAVLIGVLSSVLGLYLSYYL 234
                        250       260
                 ....*....|....*....|....*
gi 504697879 251 SLPAGPSIVLTASALFFISVLFGTR 275
Cdd:COG1108  235 DLPTGPTIVLVAGLLFLLSLLFSPR 259
 
Name Accession Description Interval E-value
ZnuB COG1108
ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and ...
13-275 1.37e-54

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


Pssm-ID: 440725  Cd Length: 260  Bit Score: 177.55  E-value: 1.37e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  13 YGFMRRALVVCLALSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLLSgmslLAMSIGGFIAGITVALVAGLVSRR 92
Cdd:COG1108    1 YDFMQRALLAGLLVGLACGLLGVFLVLRRMSLIGDALSHAALPGVALAFLLG----LSPLLGALVAGLLAALLIGLLRRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  93 TPLKEDASFAGFYLGSLALGVTLVSL-RGSNVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDTAW 171
Cdd:COG1108   77 SRLKEDTAIGIVFSGGFALGVLLISLvPGSAVDLMSYLFGSILAVSRSDLLLLAVLAAVVLLLLLLFYRELLLVSFDPEL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 172 LQvnARGLPGLLH-GLFLALLVLNLVAGFQVLGTLMAVGLMMLPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLSWAI 250
Cdd:COG1108  157 AR--ASGLPVRLLhLLLLVLLALTVVAALQAVGALLVSALLIIPAATARLLTRSLRRMLLLAVLIGVLSSVLGLYLSYYL 234
                        250       260
                 ....*....|....*....|....*
gi 504697879 251 SLPAGPSIVLTASALFFISVLFGTR 275
Cdd:COG1108  235 DLPTGPTIVLVAGLLFLLSLLFSPR 259
AztB NF040871
zinc ABC transporter permease AztB;
12-262 4.03e-52

zinc ABC transporter permease AztB;


Pssm-ID: 468808  Cd Length: 254  Bit Score: 170.93  E-value: 4.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  12 EYGFMRRALVVCLALSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLLSGmsllAMSIGGFIAGITVALVAGLVSR 91
Cdd:NF040871   8 EVDFVQRALVGGVLVSLVCAPVGTWVVLRGMAFLGDAMSHGMLPGVALAFLLGG----PLTLGAAVSAAAMALGVGALSR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  92 RTPLKEDASFAGFYLGSLALGVTLVSLRGS-NVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDTA 170
Cdd:NF040871  84 SRRLSEDTSIGLLFVGMLALGVIIVSHSGSfAVDLTGFLFGDVLAVRDADLALLAGALAVTLAVAALFHRAFVALAFDPR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 171 wlQVNARGL-PGLLHGLFLALLVLNLVAGFQVLGTLMAVGLMMLPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLSWA 249
Cdd:NF040871 164 --KASTLGLrPRLAHAALLGLVTLAVVASFQAVGTLLVVGLLIAPAAAARLWARRIPTMMALAALLGAAAVVGGLLISWH 241
                        250
                 ....*....|...
gi 504697879 250 ISLPAGPSIVLTA 262
Cdd:NF040871 242 ASTAAGATIAASA 254
ABC-3 pfam00950
ABC 3 transport family;
13-273 5.99e-36

ABC 3 transport family;


Pssm-ID: 334323  Cd Length: 258  Bit Score: 129.27  E-value: 5.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879   13 YGFMRRALVVCLALSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLLSGmsllAMSIGGFIAGITVALVAGLVSRR 92
Cdd:pfam00950   2 YEFMQRALLASILVSLACGILGSFLVLRRQSLMGDALSHAALPGVALAYFLGI----NPAIGAFVFGLIAAVAMGYLKRK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879   93 TPLKEDASFAGFYLGSLALGVTLVSL-RGSNVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDTAW 171
Cdd:pfam00950  78 TRLKEDTAIGIVFSTFLALGLVLISLiPGSAVDLDSYLFGNILTISQQDLIQIAIITAVILILLLLFWKELLLITFDPDH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  172 LQVnaRGLP-GLLHGLFLALLVLNLVAGFQVLGTLMAVGLMMLPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLSWAI 250
Cdd:pfam00950 158 AKV--IGLPvQFLYLLLLALIALTIVVALQAVGAILVIALLIIPAATARRLTRSFDSMLIIAILIGMVSCVAGLYLSYYF 235
                         250       260
                  ....*....|....*....|...
gi 504697879  251 SLPAGPSIVLTASALFFISVLFG 273
Cdd:pfam00950 236 DTSTGPVIVLIATLLFLISLAFA 258
TM_ABC_iron-siderophores_like cd06550
Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
16-270 8.54e-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: 72.20  E-value: 8.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  16 MRRALVVCLALSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLL---SGMSLLAMSIGGFIAGITVALVAGLVSRR 92
Cdd:cd06550    1 LLAALLVGAALAVSGAILQSLTRNRLASPSILGISHGALLGVVLALLLgigLSNYALGAFAFAGALAIALLVLLLASRGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  93 TPLKEDASFAGFYLGSLALGVTLVSLRGS--NVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDta 170
Cdd:cd06550   81 LSPSKLILIGIVLSAFFSAGVILISLLSDdsLQDLNIWLFGSILGVTWEDLLILLIILLLVLLLLLLLSRKLNLLTFD-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 171 wlQVNARGL---PGLLHGLFLALLVLNLVAGFQVLGTLMAVGLMMlPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLS 247
Cdd:cd06550  159 --EDLAKSLginVNLLRLLLLLLVALLVVAAVALVGVILFVGLIA-PHLARRLFGRSHRYLLPLSALLGAILLLLGDLLS 235
                        250       260
                 ....*....|....*....|....*.
gi 504697879 248 WAIS---LPAGPSIVLTASALFFISV 270
Cdd:cd06550  236 RTLLpseLPVGPVTALLGAPYFLYLL 261
znuB PRK09543
zinc ABC transporter permease subunit ZnuB;
26-271 8.89e-14

zinc ABC transporter permease subunit ZnuB;


Pssm-ID: 181938  Cd Length: 261  Bit Score: 69.33  E-value: 8.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  26 LSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLLSGMSLLAmsiggfIAGITVALVAGLV--SRRTPLKEDASFAG 103
Cdd:PRK09543  15 LACAAGPLGSFVVWRRMSYFGDTLAHASLLGVAFGLLLDVNPFYA------VIAVTLLLAGGLVwlEKRPQLAIDTLLGI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 104 FYLGSLALGVTLVSLRGS-NVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDTAWLQVNARGLpGL 182
Cdd:PRK09543  89 MAHSALSLGLVVVSLMSNvRVDLMAYLFGDLLAVTPEDLISIAIGVVIVLAILFWQWRNLLSMTISPDLAFVDGVKL-QR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 183 LHGLFLALLVLNLVAGFQVLGTLMAVGLMMLPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLSWAISLPAGPSIVLTA 262
Cdd:PRK09543 168 VKLLLMLVTALTIGVAMKFVGALIITSLLIIPAATARRFARTPEQMAGVAVLVGMLAVTGGLTFSAFYDTPAGPSVVLCA 247

                 ....*....
gi 504697879 263 SALFFISVL 271
Cdd:PRK09543 248 ALLFILSMM 256
 
Name Accession Description Interval E-value
ZnuB COG1108
ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and ...
13-275 1.37e-54

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


Pssm-ID: 440725  Cd Length: 260  Bit Score: 177.55  E-value: 1.37e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  13 YGFMRRALVVCLALSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLLSgmslLAMSIGGFIAGITVALVAGLVSRR 92
Cdd:COG1108    1 YDFMQRALLAGLLVGLACGLLGVFLVLRRMSLIGDALSHAALPGVALAFLLG----LSPLLGALVAGLLAALLIGLLRRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  93 TPLKEDASFAGFYLGSLALGVTLVSL-RGSNVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDTAW 171
Cdd:COG1108   77 SRLKEDTAIGIVFSGGFALGVLLISLvPGSAVDLMSYLFGSILAVSRSDLLLLAVLAAVVLLLLLLFYRELLLVSFDPEL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 172 LQvnARGLPGLLH-GLFLALLVLNLVAGFQVLGTLMAVGLMMLPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLSWAI 250
Cdd:COG1108  157 AR--ASGLPVRLLhLLLLVLLALTVVAALQAVGALLVSALLIIPAATARLLTRSLRRMLLLAVLIGVLSSVLGLYLSYYL 234
                        250       260
                 ....*....|....*....|....*
gi 504697879 251 SLPAGPSIVLTASALFFISVLFGTR 275
Cdd:COG1108  235 DLPTGPTIVLVAGLLFLLSLLFSPR 259
AztB NF040871
zinc ABC transporter permease AztB;
12-262 4.03e-52

zinc ABC transporter permease AztB;


Pssm-ID: 468808  Cd Length: 254  Bit Score: 170.93  E-value: 4.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  12 EYGFMRRALVVCLALSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLLSGmsllAMSIGGFIAGITVALVAGLVSR 91
Cdd:NF040871   8 EVDFVQRALVGGVLVSLVCAPVGTWVVLRGMAFLGDAMSHGMLPGVALAFLLGG----PLTLGAAVSAAAMALGVGALSR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  92 RTPLKEDASFAGFYLGSLALGVTLVSLRGS-NVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDTA 170
Cdd:NF040871  84 SRRLSEDTSIGLLFVGMLALGVIIVSHSGSfAVDLTGFLFGDVLAVRDADLALLAGALAVTLAVAALFHRAFVALAFDPR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 171 wlQVNARGL-PGLLHGLFLALLVLNLVAGFQVLGTLMAVGLMMLPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLSWA 249
Cdd:NF040871 164 --KASTLGLrPRLAHAALLGLVTLAVVASFQAVGTLLVVGLLIAPAAAARLWARRIPTMMALAALLGAAAVVGGLLISWH 241
                        250
                 ....*....|...
gi 504697879 250 ISLPAGPSIVLTA 262
Cdd:NF040871 242 ASTAAGATIAASA 254
ABC-3 pfam00950
ABC 3 transport family;
13-273 5.99e-36

ABC 3 transport family;


Pssm-ID: 334323  Cd Length: 258  Bit Score: 129.27  E-value: 5.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879   13 YGFMRRALVVCLALSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLLSGmsllAMSIGGFIAGITVALVAGLVSRR 92
Cdd:pfam00950   2 YEFMQRALLASILVSLACGILGSFLVLRRQSLMGDALSHAALPGVALAYFLGI----NPAIGAFVFGLIAAVAMGYLKRK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879   93 TPLKEDASFAGFYLGSLALGVTLVSL-RGSNVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDTAW 171
Cdd:pfam00950  78 TRLKEDTAIGIVFSTFLALGLVLISLiPGSAVDLDSYLFGNILTISQQDLIQIAIITAVILILLLLFWKELLLITFDPDH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  172 LQVnaRGLP-GLLHGLFLALLVLNLVAGFQVLGTLMAVGLMMLPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLSWAI 250
Cdd:pfam00950 158 AKV--IGLPvQFLYLLLLALIALTIVVALQAVGAILVIALLIIPAATARRLTRSFDSMLIIAILIGMVSCVAGLYLSYYF 235
                         250       260
                  ....*....|....*....|...
gi 504697879  251 SLPAGPSIVLTASALFFISVLFG 273
Cdd:pfam00950 236 DTSTGPVIVLIATLLFLISLAFA 258
TM_ABC_iron-siderophores_like cd06550
Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
16-270 8.54e-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: 72.20  E-value: 8.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  16 MRRALVVCLALSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLL---SGMSLLAMSIGGFIAGITVALVAGLVSRR 92
Cdd:cd06550    1 LLAALLVGAALAVSGAILQSLTRNRLASPSILGISHGALLGVVLALLLgigLSNYALGAFAFAGALAIALLVLLLASRGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  93 TPLKEDASFAGFYLGSLALGVTLVSLRGS--NVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDta 170
Cdd:cd06550   81 LSPSKLILIGIVLSAFFSAGVILISLLSDdsLQDLNIWLFGSILGVTWEDLLILLIILLLVLLLLLLLSRKLNLLTFD-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 171 wlQVNARGL---PGLLHGLFLALLVLNLVAGFQVLGTLMAVGLMMlPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLS 247
Cdd:cd06550  159 --EDLAKSLginVNLLRLLLLLLVALLVVAAVALVGVILFVGLIA-PHLARRLFGRSHRYLLPLSALLGAILLLLGDLLS 235
                        250       260
                 ....*....|....*....|....*.
gi 504697879 248 WAIS---LPAGPSIVLTASALFFISV 270
Cdd:cd06550  236 RTLLpseLPVGPVTALLGAPYFLYLL 261
znuB PRK09543
zinc ABC transporter permease subunit ZnuB;
26-271 8.89e-14

zinc ABC transporter permease subunit ZnuB;


Pssm-ID: 181938  Cd Length: 261  Bit Score: 69.33  E-value: 8.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879  26 LSVSTTALGVFLQLRRMSLMGDALSHAILPGVAVGYLLSGMSLLAmsiggfIAGITVALVAGLV--SRRTPLKEDASFAG 103
Cdd:PRK09543  15 LACAAGPLGSFVVWRRMSYFGDTLAHASLLGVAFGLLLDVNPFYA------VIAVTLLLAGGLVwlEKRPQLAIDTLLGI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 104 FYLGSLALGVTLVSLRGS-NVDLLHLLFGSILAVDNDAALFVTGVCMFTLITLAIFYRGLVTEAFDTAWLQVNARGLpGL 182
Cdd:PRK09543  89 MAHSALSLGLVVVSLMSNvRVDLMAYLFGDLLAVTPEDLISIAIGVVIVLAILFWQWRNLLSMTISPDLAFVDGVKL-QR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697879 183 LHGLFLALLVLNLVAGFQVLGTLMAVGLMMLPAVAARCWVRTLPGLLLMAGISGIFCAWLGLSLSWAISLPAGPSIVLTA 262
Cdd:PRK09543 168 VKLLLMLVTALTIGVAMKFVGALIITSLLIIPAATARRFARTPEQMAGVAVLVGMLAVTGGLTFSAFYDTPAGPSVVLCA 247

                 ....*....
gi 504697879 263 SALFFISVL 271
Cdd:PRK09543 248 ALLFILSMM 256
 
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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