ID A0A3N2JV10_9CELL Unreviewed; 674 AA.
AC A0A3N2JV10;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=NADH dehydrogenase subunit L {ECO:0000313|EMBL:ROS76719.1};
GN ORFNames=EDF32_1540 {ECO:0000313|EMBL:ROS76719.1};
OS Cellulomonas sp. PhB143.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2485186 {ECO:0000313|EMBL:ROS76719.1, ECO:0000313|Proteomes:UP000276333};
RN [1] {ECO:0000313|EMBL:ROS76719.1, ECO:0000313|Proteomes:UP000276333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PhB143 {ECO:0000313|EMBL:ROS76719.1,
RC ECO:0000313|Proteomes:UP000276333};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (NOV-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:ROS76719.1}.
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DR EMBL; RKIJ01000011; ROS76719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2JV10; -.
DR Proteomes; UP000276333; 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:UP000276333};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..674
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039626423"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 506..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 548..570
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 654..673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 100..150
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 166..438
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 674 AA; 71623 MW; 042F2F4278FB8F27 CRC64;
MFLAQSPSVM PFGPLASLPA QASAVSTDVP SSLQLAPLVI LLPLVGAAVL LLVGRRGDRW
GHWLGVLTTA GAFVVGLVLL VGLTGLDAAE RVYDQHLYRW IPAGTLDVSA GLRIDPLSVT
FVLLVTFVGA LIHVYSVAYM EHDPNRRRFF GYLNLFVAAM LVLVLADSYL LLFVGWEGVG
LASYLLIGFW YHERPNAVAA KKAFVMNRVG DIGLIVAMML MLSTFGSVDF ATVFDQAPTA
GTGILTAMGL VLLLAACGKS AQVPLQAWLG DAMAGPTPVS ALIHAATMVT AGVYLVVRSA
PVFDGAPDAR LVVVVVGALT LLFGAVVGSA KDDLKKALAA STMSQIGYMV LAAGLGPIGY
AFAIFHLVTH GFFKAGLFLG AGSVMHGMDD GVDMRRFGGL SRFMKVTFVT FGLGWLAILG
VPPFSGFWSK DKIIEAAFVP VDGQEWRAWV FGLVALLGAG ITAFYMSRLF FMTFTGRRRW
NDGSGSVGGA GPQDGPVRHP HESPRLMTVP MVVLAVGSVA LGGLLAWGDT FVTWLEPVTG
HAEHGEPVLP VWLLVVLTLL LVLAGIALAW RQYTVADVPV TPPHGSVLTR AARRDLYQDA
VNEDVVMRPG QYLTRTLVYA DRELVDGSFL GIGSALTWAS GAWRKAQNGY VRSYAAIMLG
GLIVIVVVAL ALAS
//
