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Conserved domains on  [gi|523691561|ref|WP_020810427|]
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MULTISPECIES: NAD(P)(+) transhydrogenase (Re/Si-specific) subunit beta [Agrobacterium tumefaciens complex]

Protein Classification

NAD(P)(+) transhydrogenase (Re/Si-specific) subunit beta( domain architecture ID 10003429)

NAD(P)(+) transhydrogenase (Re/Si-specific) subunit beta is part of a tetrameric membrane-bound proton pump (composed of two alpha and two beta subunits) that catalyzes the reversible transfer of a hydride ion equivalent between NAD and NADP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PntB COG1282
NAD/NADP transhydrogenase beta subunit [Energy production and conversion];
16-473 0e+00

NAD/NADP transhydrogenase beta subunit [Energy production and conversion];


:

Pssm-ID: 440893  Cd Length: 458  Bit Score: 716.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  16 LFILSLGGLSGQESAKRAVWYGITGMGLAIVATVFGPDVGNWFIVLLMLVGGSVLGYFVANRVQMTEMPQLVAALHSFVG 95
Cdd:COG1282   16 LFILGLKGLSSPETARRGNLLGAVGMLIAVVATLLLPGIVNYGLILAAIAIGGAIGAVLARKVEMTAMPQLVALFNGFGG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  96 LAAVFIGFNAHIEeahvasldetarslltgfsalLAHKTPVELAIMKVEVFLGVFIGAVTFTGSVVAFGKLAGKVDGKAK 175
Cdd:COG1282   96 LAAALVAAAELLE---------------------PGALAGALPAIHLIEIVLGVLIGAVTFTGSLIAFGKLQGLISGKPI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 176 KLPGGHVLNASAAILSLVLLLMYC-NGAGAWTLVLMTLAAFFIGYHLIMGIGGADMPVVVSMLNSYSGWAAAAIGFTLGN 254
Cdd:COG1282  155 TFPGQHLLNLLLLLAIVALGVLFVvSPGSLLLLLLLTVLALLLGVLLVLPIGGADMPVVISLLNSYSGLAAAAAGFVLGN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 255 DLLIVTGALVGSSGAILSYIMCKAMNRSFVSVILGGFGGTTGPA--MEIDGEQVAIDAEGVASALNDADSVIIVPGYGMA 332
Cdd:COG1282  235 DLLIIAGALVGASGAILTYIMCKAMNRSLINVLFGGFGGGGAAAagAAEQGEVKEISAEDAAILLAYASSVIIVPGYGMA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 333 VAQAQSAVSELTRKLRADGKTVRFAIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFPNTDVVIVIGSNDIVNPAA 412
Cdd:COG1282  315 VAQAQHAVRELADLLEERGVEVKFAIHPVAGRMPGHMNVLLAEANVPYDQLLEMDEINPEFAQTDVALVIGANDVVNPAA 394
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523691561 413 QDDPNSPIAGMPVLEVWKSKLVIVSKRGQGTGYSGIENPLFYKDNTRMFYGDAKKSINDLL 473
Cdd:COG1282  395 RTDPGSPIYGMPILEVDKAKTVIVIKRSMGPGYAGVENPLFYKDNTRMLFGDAKKSVEELV 455
 
Name Accession Description Interval E-value
PntB COG1282
NAD/NADP transhydrogenase beta subunit [Energy production and conversion];
16-473 0e+00

NAD/NADP transhydrogenase beta subunit [Energy production and conversion];


Pssm-ID: 440893  Cd Length: 458  Bit Score: 716.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  16 LFILSLGGLSGQESAKRAVWYGITGMGLAIVATVFGPDVGNWFIVLLMLVGGSVLGYFVANRVQMTEMPQLVAALHSFVG 95
Cdd:COG1282   16 LFILGLKGLSSPETARRGNLLGAVGMLIAVVATLLLPGIVNYGLILAAIAIGGAIGAVLARKVEMTAMPQLVALFNGFGG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  96 LAAVFIGFNAHIEeahvasldetarslltgfsalLAHKTPVELAIMKVEVFLGVFIGAVTFTGSVVAFGKLAGKVDGKAK 175
Cdd:COG1282   96 LAAALVAAAELLE---------------------PGALAGALPAIHLIEIVLGVLIGAVTFTGSLIAFGKLQGLISGKPI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 176 KLPGGHVLNASAAILSLVLLLMYC-NGAGAWTLVLMTLAAFFIGYHLIMGIGGADMPVVVSMLNSYSGWAAAAIGFTLGN 254
Cdd:COG1282  155 TFPGQHLLNLLLLLAIVALGVLFVvSPGSLLLLLLLTVLALLLGVLLVLPIGGADMPVVISLLNSYSGLAAAAAGFVLGN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 255 DLLIVTGALVGSSGAILSYIMCKAMNRSFVSVILGGFGGTTGPA--MEIDGEQVAIDAEGVASALNDADSVIIVPGYGMA 332
Cdd:COG1282  235 DLLIIAGALVGASGAILTYIMCKAMNRSLINVLFGGFGGGGAAAagAAEQGEVKEISAEDAAILLAYASSVIIVPGYGMA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 333 VAQAQSAVSELTRKLRADGKTVRFAIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFPNTDVVIVIGSNDIVNPAA 412
Cdd:COG1282  315 VAQAQHAVRELADLLEERGVEVKFAIHPVAGRMPGHMNVLLAEANVPYDQLLEMDEINPEFAQTDVALVIGANDVVNPAA 394
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523691561 413 QDDPNSPIAGMPVLEVWKSKLVIVSKRGQGTGYSGIENPLFYKDNTRMFYGDAKKSINDLL 473
Cdd:COG1282  395 RTDPGSPIYGMPILEVDKAKTVIVIKRSMGPGYAGVENPLFYKDNTRMLFGDAKKSVEELV 455
PNTB pfam02233
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP ...
16-473 0e+00

NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP transhydrogenase in prokaryotes, and either the protein N- or C terminal in eukaryotes. The domain is often found in conjunction with pfam01262. Pyridine nucleotide transhydrogenase catalyzes the reduction of NAD+ to NADPH. A complete loss of activity occurs upon mutation of Gly314 in E. coli.


Pssm-ID: 460502  Cd Length: 454  Bit Score: 678.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561   16 LFILSLGGLSGQESAKRAVWYGITGMGLAIVATV---FGPDVGNWFIVLLMLVGGSVLGYFVANRVQMTEMPQLVAALHS 92
Cdd:pfam02233   9 LFILGLKGLSSPKTARRGNLLGAIGMALAIVATLllgALADSLPYGLILIAIAIGGVIGLYIARRVKMTAMPQLVALFHS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561   93 FVGLAAVFIGFNAHIEEAHVASLDETarslltgfsallahktpvelaIMKVEVFLGVFIGAVTFTGSVVAFGKLAGKVDG 172
Cdd:pfam02233  89 LGGLAAVLVAIAEYLAPEAFGAGISA---------------------FHLVEIVLGVLIGAVTFTGSLIAFGKLQGLLSS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  173 KAKKLPGGHVLNASAAILSLVLLLMYCNGAGAWTLVLMTLAAFFIGYHLIMGIGGADMPVVVSMLNSYSGWAAAAIGFTL 252
Cdd:pfam02233 148 KPLTLPGRHLLNLLLLLAIVVLGVLFVAAPSSPGLWLLTALALLLGVLLVLPIGGADMPVVISLLNSYSGWAAAAAGFVL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  253 GNDLLIVTGALVGSSGAILSYIMCKAMNRSFVSVILGGFGGTTGPA----MEIDGEQVAIDAEGVASALNDADSVIIVPG 328
Cdd:pfam02233 228 GNPLLIIAGALVGASGAILTYIMCKAMNRSLTNVLFGGFGAAASAGaagaAAADGEVKEISAEDAAELLAYASSVIIVPG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  329 YGMAVAQAQSAVSELTRKLRADGKTVRFAIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFPNTDVVIVIGSNDIV 408
Cdd:pfam02233 308 YGMAVAQAQHAVAELADLLEERGVEVRFAIHPVAGRMPGHMNVLLAEADVPYDIVLEMDEINDDFADTDVALVIGANDVV 387
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523691561  409 NPAAQDDPNSPIAGMPVLEVWKSKLVIVSKRGQGTGYSGIENPLFYKDNTRMFYGDAKKSINDLL 473
Cdd:pfam02233 388 NPAARTDPGSPIYGMPILEVWKAKTVIVIKRSMGPGYAGVDNPLFYKDNTRMLFGDAKKSLEELV 452
pntB PRK09444
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;
1-473 0e+00

Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;


Pssm-ID: 236520  Cd Length: 462  Bit Score: 671.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561   1 MTIGIVSAAYVAAAVLFILSLGGLSGQESAKRAVWYGITGMGLAIVATVFGPDVGNWFIVLLMLVGGSVLGYFVANRVQM 80
Cdd:PRK09444   1 MSGGLVTAAYIVAAILFIFSLAGLSKHETSRQGNNFGIAGMAIALIATIFGPDTGNVGWIIIAMVIGGAIGIRLAKKVEM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  81 TEMPQLVAALHSFVGLAAVFIGFNAHIEEAHVAsldetarslltgfsallahkTPVELAIMKVEVFLGVFIGAVTFTGSV 160
Cdd:PRK09444  81 TEMPELVAILHSFVGLAAVLVGFNSYLDHDAGM--------------------APVLVNIHLTEVFLGIFIGAVTFTGSI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 161 VAFGKLAGKVDGKAKKLPGGHVLNASAAILSLVLLLMYCN----GAGAWTLVLMTLAAFFIGYHLIMGIGGADMPVVVSM 236
Cdd:PRK09444 141 VAFGKLRGKISSKPLMLPHRHKLNLAALVVSFLLLIVFVRtdsvGLQVFALLLMTLIALAFGWHLVASIGGADMPVVVSM 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 237 LNSYSGWAAAAIGFTLGNDLLIVTGALVGSSGAILSYIMCKAMNRSFVSVILGGFG--GTTGPAMEIDGEQVAIDAEGVA 314
Cdd:PRK09444 221 LNSYSGWAAAAAGFMLSNDLLIVTGALVGSSGAILSYIMCKAMNRSFISVIAGGFGtdGSSTGDDEEVGEHRETTAEEVA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 315 SALNDADSVIIVPGYGMAVAQAQSAVSELTRKLRADGKTVRFAIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFP 394
Cdd:PRK09444 301 EMLKNSHSVIITPGYGMAVAQAQYPVAEITEKLRARGINVRFGIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFA 380
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523691561 395 NTDVVIVIGSNDIVNPAAQDDPNSPIAGMPVLEVWKSKLVIVSKRGQGTGYSGIENPLFYKDNTRMFYGDAKKSINDLL 473
Cdd:PRK09444 381 DTDTVLVIGANDTVNPAAQEDPNSPIAGMPVLEVWKAQNVIVFKRSMNTGYAGVQNPLFFKENTQMLFGDAKASVDAIL 459
MFS_ShiA_like cd17369
Shikimate transporter and similar proteins of the Major Facilitator Superfamily; This ...
138-272 8.78e-03

Shikimate transporter and similar proteins of the Major Facilitator Superfamily; This subfamily is composed of Escherichia coli shikimate transporter (ShiA), inner membrane metabolite transport protein YhjE, and other putative metabolite transporters. ShiA is involved in the uptake of shikimate, an aromatic compound involved in siderophore biosynthesis. It has been suggested that YhjE may mediate the uptake of osmoprotectants. The ShiA-like subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340927 [Multi-domain]  Cd Length: 408  Bit Score: 38.28  E-value: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 138 LAIMKVEVFLGVFIGAVTFTGSVVAFGKLAGKVdGKAKKLPGGhvlnASAAILSLVLLLMYCNGAGAWTLVLMTLAAFFI 217
Cdd:cd17369  259 LGVDRSTVLLAVLIASVVAAITIPLFGWLSDRV-GRRPVYLAG----ALLAALFAFPFFWLLDTGSTWLIVLAAVVVLGV 333
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 218 GYHLIMGIGGADMPVVVSMLNSYSGwaaAAIGFTLGNDL-----LIVTGALVGSSGAILS 272
Cdd:cd17369  334 LHGMMYGPQAAFLAELFPTRVRYTG---ASLGYQLGAILgggfaPLIATALVAATGSWWP 390
 
Name Accession Description Interval E-value
PntB COG1282
NAD/NADP transhydrogenase beta subunit [Energy production and conversion];
16-473 0e+00

NAD/NADP transhydrogenase beta subunit [Energy production and conversion];


Pssm-ID: 440893  Cd Length: 458  Bit Score: 716.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  16 LFILSLGGLSGQESAKRAVWYGITGMGLAIVATVFGPDVGNWFIVLLMLVGGSVLGYFVANRVQMTEMPQLVAALHSFVG 95
Cdd:COG1282   16 LFILGLKGLSSPETARRGNLLGAVGMLIAVVATLLLPGIVNYGLILAAIAIGGAIGAVLARKVEMTAMPQLVALFNGFGG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  96 LAAVFIGFNAHIEeahvasldetarslltgfsalLAHKTPVELAIMKVEVFLGVFIGAVTFTGSVVAFGKLAGKVDGKAK 175
Cdd:COG1282   96 LAAALVAAAELLE---------------------PGALAGALPAIHLIEIVLGVLIGAVTFTGSLIAFGKLQGLISGKPI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 176 KLPGGHVLNASAAILSLVLLLMYC-NGAGAWTLVLMTLAAFFIGYHLIMGIGGADMPVVVSMLNSYSGWAAAAIGFTLGN 254
Cdd:COG1282  155 TFPGQHLLNLLLLLAIVALGVLFVvSPGSLLLLLLLTVLALLLGVLLVLPIGGADMPVVISLLNSYSGLAAAAAGFVLGN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 255 DLLIVTGALVGSSGAILSYIMCKAMNRSFVSVILGGFGGTTGPA--MEIDGEQVAIDAEGVASALNDADSVIIVPGYGMA 332
Cdd:COG1282  235 DLLIIAGALVGASGAILTYIMCKAMNRSLINVLFGGFGGGGAAAagAAEQGEVKEISAEDAAILLAYASSVIIVPGYGMA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 333 VAQAQSAVSELTRKLRADGKTVRFAIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFPNTDVVIVIGSNDIVNPAA 412
Cdd:COG1282  315 VAQAQHAVRELADLLEERGVEVKFAIHPVAGRMPGHMNVLLAEANVPYDQLLEMDEINPEFAQTDVALVIGANDVVNPAA 394
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523691561 413 QDDPNSPIAGMPVLEVWKSKLVIVSKRGQGTGYSGIENPLFYKDNTRMFYGDAKKSINDLL 473
Cdd:COG1282  395 RTDPGSPIYGMPILEVDKAKTVIVIKRSMGPGYAGVENPLFYKDNTRMLFGDAKKSVEELV 455
PNTB pfam02233
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP ...
16-473 0e+00

NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP transhydrogenase in prokaryotes, and either the protein N- or C terminal in eukaryotes. The domain is often found in conjunction with pfam01262. Pyridine nucleotide transhydrogenase catalyzes the reduction of NAD+ to NADPH. A complete loss of activity occurs upon mutation of Gly314 in E. coli.


Pssm-ID: 460502  Cd Length: 454  Bit Score: 678.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561   16 LFILSLGGLSGQESAKRAVWYGITGMGLAIVATV---FGPDVGNWFIVLLMLVGGSVLGYFVANRVQMTEMPQLVAALHS 92
Cdd:pfam02233   9 LFILGLKGLSSPKTARRGNLLGAIGMALAIVATLllgALADSLPYGLILIAIAIGGVIGLYIARRVKMTAMPQLVALFHS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561   93 FVGLAAVFIGFNAHIEEAHVASLDETarslltgfsallahktpvelaIMKVEVFLGVFIGAVTFTGSVVAFGKLAGKVDG 172
Cdd:pfam02233  89 LGGLAAVLVAIAEYLAPEAFGAGISA---------------------FHLVEIVLGVLIGAVTFTGSLIAFGKLQGLLSS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  173 KAKKLPGGHVLNASAAILSLVLLLMYCNGAGAWTLVLMTLAAFFIGYHLIMGIGGADMPVVVSMLNSYSGWAAAAIGFTL 252
Cdd:pfam02233 148 KPLTLPGRHLLNLLLLLAIVVLGVLFVAAPSSPGLWLLTALALLLGVLLVLPIGGADMPVVISLLNSYSGWAAAAAGFVL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  253 GNDLLIVTGALVGSSGAILSYIMCKAMNRSFVSVILGGFGGTTGPA----MEIDGEQVAIDAEGVASALNDADSVIIVPG 328
Cdd:pfam02233 228 GNPLLIIAGALVGASGAILTYIMCKAMNRSLTNVLFGGFGAAASAGaagaAAADGEVKEISAEDAAELLAYASSVIIVPG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  329 YGMAVAQAQSAVSELTRKLRADGKTVRFAIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFPNTDVVIVIGSNDIV 408
Cdd:pfam02233 308 YGMAVAQAQHAVAELADLLEERGVEVRFAIHPVAGRMPGHMNVLLAEADVPYDIVLEMDEINDDFADTDVALVIGANDVV 387
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523691561  409 NPAAQDDPNSPIAGMPVLEVWKSKLVIVSKRGQGTGYSGIENPLFYKDNTRMFYGDAKKSINDLL 473
Cdd:pfam02233 388 NPAARTDPGSPIYGMPILEVWKAKTVIVIKRSMGPGYAGVDNPLFYKDNTRMLFGDAKKSLEELV 452
pntB PRK09444
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;
1-473 0e+00

Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;


Pssm-ID: 236520  Cd Length: 462  Bit Score: 671.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561   1 MTIGIVSAAYVAAAVLFILSLGGLSGQESAKRAVWYGITGMGLAIVATVFGPDVGNWFIVLLMLVGGSVLGYFVANRVQM 80
Cdd:PRK09444   1 MSGGLVTAAYIVAAILFIFSLAGLSKHETSRQGNNFGIAGMAIALIATIFGPDTGNVGWIIIAMVIGGAIGIRLAKKVEM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561  81 TEMPQLVAALHSFVGLAAVFIGFNAHIEEAHVAsldetarslltgfsallahkTPVELAIMKVEVFLGVFIGAVTFTGSV 160
Cdd:PRK09444  81 TEMPELVAILHSFVGLAAVLVGFNSYLDHDAGM--------------------APVLVNIHLTEVFLGIFIGAVTFTGSI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 161 VAFGKLAGKVDGKAKKLPGGHVLNASAAILSLVLLLMYCN----GAGAWTLVLMTLAAFFIGYHLIMGIGGADMPVVVSM 236
Cdd:PRK09444 141 VAFGKLRGKISSKPLMLPHRHKLNLAALVVSFLLLIVFVRtdsvGLQVFALLLMTLIALAFGWHLVASIGGADMPVVVSM 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 237 LNSYSGWAAAAIGFTLGNDLLIVTGALVGSSGAILSYIMCKAMNRSFVSVILGGFG--GTTGPAMEIDGEQVAIDAEGVA 314
Cdd:PRK09444 221 LNSYSGWAAAAAGFMLSNDLLIVTGALVGSSGAILSYIMCKAMNRSFISVIAGGFGtdGSSTGDDEEVGEHRETTAEEVA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 315 SALNDADSVIIVPGYGMAVAQAQSAVSELTRKLRADGKTVRFAIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFP 394
Cdd:PRK09444 301 EMLKNSHSVIITPGYGMAVAQAQYPVAEITEKLRARGINVRFGIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFA 380
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523691561 395 NTDVVIVIGSNDIVNPAAQDDPNSPIAGMPVLEVWKSKLVIVSKRGQGTGYSGIENPLFYKDNTRMFYGDAKKSINDLL 473
Cdd:PRK09444 381 DTDTVLVIGANDTVNPAAQEDPNSPIAGMPVLEVWKAQNVIVFKRSMNTGYAGVQNPLFFKENTQMLFGDAKASVDAIL 459
MFS_ShiA_like cd17369
Shikimate transporter and similar proteins of the Major Facilitator Superfamily; This ...
138-272 8.78e-03

Shikimate transporter and similar proteins of the Major Facilitator Superfamily; This subfamily is composed of Escherichia coli shikimate transporter (ShiA), inner membrane metabolite transport protein YhjE, and other putative metabolite transporters. ShiA is involved in the uptake of shikimate, an aromatic compound involved in siderophore biosynthesis. It has been suggested that YhjE may mediate the uptake of osmoprotectants. The ShiA-like subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340927 [Multi-domain]  Cd Length: 408  Bit Score: 38.28  E-value: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 138 LAIMKVEVFLGVFIGAVTFTGSVVAFGKLAGKVdGKAKKLPGGhvlnASAAILSLVLLLMYCNGAGAWTLVLMTLAAFFI 217
Cdd:cd17369  259 LGVDRSTVLLAVLIASVVAAITIPLFGWLSDRV-GRRPVYLAG----ALLAALFAFPFFWLLDTGSTWLIVLAAVVVLGV 333
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 523691561 218 GYHLIMGIGGADMPVVVSMLNSYSGwaaAAIGFTLGNDL-----LIVTGALVGSSGAILS 272
Cdd:cd17369  334 LHGMMYGPQAAFLAELFPTRVRYTG---ASLGYQLGAILgggfaPLIATALVAATGSWWP 390
 
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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