ID A0A365H8X6_9ACTN Unreviewed; 663 AA.
AC A0A365H8X6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:RAY15468.1};
GN ORFNames=DPM19_10935 {ECO:0000313|EMBL:RAY15468.1};
OS Actinomadura craniellae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2231787 {ECO:0000313|EMBL:RAY15468.1, ECO:0000313|Proteomes:UP000251891};
RN [1] {ECO:0000313|EMBL:RAY15468.1, ECO:0000313|Proteomes:UP000251891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW63021 {ECO:0000313|EMBL:RAY15468.1,
RC ECO:0000313|Proteomes:UP000251891};
RA Li L., Xu Q.H., Lin H.W., Lu Y.H.;
RT "Actinomadura craniellae sp. nov. isolated from marine sponge Craniella
RT sp.";
RL Submitted (JUN-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:RAY15468.1}.
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DR EMBL; QLYX01000004; RAY15468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365H8X6; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000251891; 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.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000251891};
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 64..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 643..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 100..147
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 164..433
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 663 AA; 68254 MW; 4DC749BD622AACCF CRC64;
MILLPFLAAF AGFLAGPRLT RALGGPGPAP GGVWVPGGGP RASARSWAVA AGTAARVPLR
NGPALLACVP TGLAALLSLV TLIVHWADPG VRSGVLTRVP TGGVDIVIGV QTTGPAVAVG
LMVCCVALAV QVYSIAYMAE DPRYSSYAAF VSLFTAAMLL VVFAGDLLLL YVGWEVMGVC
SYFLIGHHWE ERANSRAAVK AFLVTRLGDV GFLLGILVLG AGAGTFWIDD VLARVPQLPD
GTVLAAALLL LAGVAGKSAQ FPLHTWLPDA MAGPTPISAL IHAATMVAAG IYVVVRLYPV
FSAAPAALAV LGVLAAISML GAALAALAQD DLKRVLAYST ISQLAYMAAG LAVGAREAAT
FHLLTHGAFK ALLFLAAGCV ILVTGSNLLR DHGGLRRAMP ITFWSMTVGF AALAGLPPAS
GFFSKDAIIE AAQHAALHPA DASPGAGVVL SEPYPAVAVA QHSVDVPGWV AWVVYLSLLA
TVAVTAAYAT RAWLMTFFGE PRSDFRPREA PVLMSWPVAA CAVPAALLGL LGLGDAALRP
HLGSALLSLL LVAAGAGAVY LLWNRDPALD PARALGPLRA PFARAFYLDE LYALVIVRPV
RALAGLVVET DDRVIDSAVR GAAPASRGLG GLLRRPQDGN PQTYLTGLLA GVVVIAVTVA
VLQ
//
