ID A0A3D8IC39_9HELI Unreviewed; 624 AA.
AC A0A3D8IC39;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:RDU62605.1};
GN ORFNames=CQA53_09210 {ECO:0000313|EMBL:RDU62605.1};
OS Helicobacter didelphidarum.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=2040648 {ECO:0000313|EMBL:RDU62605.1, ECO:0000313|Proteomes:UP000256379};
RN [1] {ECO:0000313|EMBL:RDU62605.1, ECO:0000313|Proteomes:UP000256379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 17-337 {ECO:0000313|EMBL:RDU62605.1,
RC ECO:0000313|Proteomes:UP000256379};
RA Mannion A.J., Shen Z., Fox J.G.;
RT "Novel Campyloabacter and Helicobacter Species and Strains.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDU62605.1}.
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DR EMBL; NXLQ01000030; RDU62605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8IC39; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000256379; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR Gene3D; 1.20.5.2700; -; 1.
DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR NCBIfam; TIGR01974; NDH_I_L; 1.
DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
DR PRINTS; PR01435; NPOXDRDTASE5.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000256379};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 77..126
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 143..430
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 624 AA; 70198 MW; 09D8D641FB775517 CRC64;
MLDFILLHKE ILLTIVVFLP FISAILAGFN ATLRPSKILG YICSIFITSS FLLTCLLIYI
LVKTDIQSFH VFLWDFIATG QFQVSFSLMF DKINAIMFLV VTLVSTMVHF YSIGYMEHDA
GFNRFFSYLG GFVFSMLLLV GGDNLLILFI GWEGVGTCSY LLIGFWYKRK KANEASIEAF
VMNRIADLGM LLGIFLTYWT LGSLSYHDIF LTLANNPPKD SVMTWIAILL FIGAMGKSAQ
FPLHTWLANA MEGPTPVSAL IHAATMVTAG VYLVVRLAPI YNVVPHVAYF IASLGAFVAI
FASLMAIVNR DLKRIIAYST LSQLGYMFVA TGLGAYWIAL FHLFTHAFFK SLLFLGAGNV
MHAMHDKLDI TKMGALAKPL KTSMVFMLIG SIALCGIPPL AGYYSKDKIL EVAYAQHEYI
IWTILLIGAV CTAFYSFRLF TLVFIAPKNH NEHPHEASKV MLFAMTPLAI LACIAGIFHI
QFETFLSSAL VPLIIHIKEQ TLLIILTLGL IIVSIISAYF IYKKGYQEKH RYNILHKILS
NEYYIPKLYN MLFVKPFSLC SEFLYHIVDM GIIDKMVDSI GKFIVFLSYL LRPIQNGNLS
SMLRLMSLGV IVLLFITLLY FILL
//
