ID A0A1V8SLW0_9PEZI Unreviewed; 692 AA.
AC A0A1V8SLW0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=EF-hand domain-containing protein {ECO:0000259|PROSITE:PS50222};
GN ORFNames=B0A48_13934 {ECO:0000313|EMBL:OQO00147.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO00147.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00004137}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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:OQO00147.1}.
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DR EMBL; NAJO01000036; OQO00147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8SLW0; -.
DR STRING; 1507870.A0A1V8SLW0; -.
DR InParanoid; A0A1V8SLW0; -.
DR OrthoDB; 48029at2759; -.
DR Proteomes; UP000192596; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR Gene3D; 3.50.50.100; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR43706:SF50; NADH DEHYDROGENASE (UBIQUINONE)-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SMART; SM00054; EFh; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000192596};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 91..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 539..574
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 692 AA; 76845 MW; EB90702E8A62D943 CRC64;
MASTPRAFNG LARSSVARQF FRATRSNASQ CQQRTLTSAV RQQLPQTWRR RTAMPMSRLV
LIRAESTAAA VDNALKTKVK AVKSKSRIVR FAARAFATLG FVVVVAGVVV VGFFIYDATT
YSSLGADADI PVSELALNPR RGGPKNLPIA EYYLSDDDCE DSKDTKHKPK LVILGTGWAS
VALLKQLNAG DYHVTVISPE NHFLFTPMLP SATVGTLELR SLVEPIRRIV MRVRGHFLKA
SAVDVEFSEK LVEVSSVGPT GEDQRFYVPY DKLVVGVGSQ TNPHGVKGLE NCHFLKNIAD
AGNIRNKIIK NLEIACLPTT TDSERRRLLS FVVSGGGPTG VEFAAELYDM LNEDLCKYYP
RLLRNEISVH VIQSRGHILN TYDEALSKYA EARFAHDGLD IQTNARVKEV RPDKILFSQK
DETGQIVTKE LPHGFCLWST GVAQTDFSQM LAKKLGDSQT NRHALETDTH LRLSGTPLGD
VYCVGDCSTV QNNVSDHIMT FLRTLAWEKG KDPEAMKITF ADWRGVAKRV KSRFPQAGDH
LRRLDKLFEA YDTDRSGTLD FSELNELLKQ IDSKLTSLPA TAQRANQQGV YLGHKFNKLA
HAAPGMAIND MADGDIDEAV YKAFEYHHMG SLAYIGNGAI FDINGYNFGG GLFAAYLWRG
AYFAQSVSMR TRVLLAMDWG KRTLFGRDMM NY
//
