ID A0A1H5DEX8_9ACTN Unreviewed; 664 AA.
AC A0A1H5DEX8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:SED77290.1};
GN ORFNames=SAMN05216489_04400 {ECO:0000313|EMBL:SED77290.1};
OS Streptomyces sp. 3213.3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855348 {ECO:0000313|EMBL:SED77290.1, ECO:0000313|Proteomes:UP000198754};
RN [1] {ECO:0000313|EMBL:SED77290.1, ECO:0000313|Proteomes:UP000198754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3213 {ECO:0000313|EMBL:SED77290.1,
RC ECO:0000313|Proteomes:UP000198754};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNTK01000001; SED77290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5DEX8; -.
DR STRING; 1855348.SAMN05216489_04400; -.
DR Proteomes; UP000198754; 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:UP000198754};
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 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 642..661
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..115
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 132..403
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 664 AA; 68263 MW; 162C654200200AAF CRC64;
MTTTTLAVLV PLLPFLGAAA GLLLGRTAPG FVRPLAVLPT LAALALAAIV AVRQGGYAAV
DSATELTPTG SVPVELALHI DGFAALVAVL VAFVATCVQI YSTGYLRDDP RYPSYAALVS
LFTSAMLLVV YSGDLIVLLV GWEVMGICSY FLVGHYWETP EARAASMKAF LVTKLGDVPF
LIGLFALATD AGSFRITKVL GTVASGGLHH PTLIALLLLA GVAGKSAQFP LHTWLPDAMA
GPTPVSALIH AATMVAAGVY FVARLLPVFE ASSAAMVVLA VMAAVTMAGS GLAALAQDDI
KRVLAYSTIG QLGYMTGALA VGDRGAAVFH LLSHGAFKAL LFLAAGVIIH ASGTNSLAAM
SRMGNLRARV PDAFWTMTVA LLALAAIPPF SGFFSKESVL GAAEHTATEH TSHIPGAAGW
IVLVAGLLTA LLTAAYATRL WLLAFHGKGV EAPDHGRQPV AMNAVLWVLA VPSLALGGLA
YRVLPDWFDG RDLTPTLTTS VLGTGVALVG GIVTYGAWRH TTALAARAPM GAVAAHPEGD
AGLVEAEAIA SHTPAYGDVA SAADPADPGR LLLGPLHRHA ATGFHLDAVY GALFVRPVLA
AASLVRFLDR EVVDTYVQGA GTLPRLLGAA VRRAQTGNLQ TYVSALLAGT VVLTVAVLLV
ATGA
//