ID J9H249_9ZZZZ Unreviewed; 479 AA.
AC J9H249;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE SubName: Full=Cardiolipin synthetase 2 {ECO:0000313|EMBL:EJX09918.1};
GN ORFNames=EVA_01972 {ECO:0000313|EMBL:EJX09918.1};
OS gut metagenome.
OC unclassified sequences; metagenomes; organismal metagenomes.
OX NCBI_TaxID=749906 {ECO:0000313|EMBL:EJX09918.1};
RN [1] {ECO:0000313|EMBL:EJX09918.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23251564; DOI=10.1371/journal.pone.0051521;
RA Alcaide M., Messina E., Richter M., Bargiela R., Peplies J., Huws S.A.,
RA Newbold C.J., Golyshin P.N., Simon M.A., Lopez G., Yakimov M.M., Ferrer M.;
RT "Gene sets for utilization of primary and secondary nutrition supplies in
RT the distal gut of endangered iberian lynx.";
RL PLoS ONE 7:E51521-E51521(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EJX09918.1}.
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DR EMBL; AMCI01000291; EJX09918.1; -; Genomic_DNA.
DR AlphaFoldDB; J9H249; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR CDD; cd09110; PLDc_CLS_1; 1.
DR CDD; cd09112; PLDc_CLS_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR HAMAP; MF_01916; Cardiolipin_synth_Cls; 1.
DR InterPro; IPR030874; Cardiolipin_synth_Firmi.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR027379; CLS_N.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR NCBIfam; TIGR04265; bac_cardiolipin; 1.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR Pfam; PF13396; PLDc_N; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 217..244
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 392..419
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 479 AA; 55693 MW; C9151C4D55636EF2 CRC64;
MIDWNLFFSQ LATIAFDLLY FGAIIGTIVV IILDNRNPVK TLAWILVLMF LPVVGLVFYF
FFGRSQRRER LIEKKLYSRL MKKSMLAYRE QERCEVPEHY ERLISLFQLT NQAYPFEGNH
VEVFTEGSSM LQALLAHLQK ATKHIHLEFY IFEDDAVGRM VRDVLMEKAR AGVEVRVIYD
DVGCWHVPHH FFEKMCEAGI EVRSFLKVRF PQFTSKVNYR NHRKIVVIDG EIGFVGGMNL
AERYLKGFSW GIWRDTHLML QGKAVHGLQT AFLLDWYFVD RSLITAASYF PKIEPKGTAL
AQVVTSEPVG LWREIMLGFM KALSNSRKYF YIQTPYFLPT EAILQALQQA ALSGVDVRLM
LPLRADSKLT HLASCSYLAD VLRAGVKVYF YKKGFLHSKL IVSDDEFSTV GSTNFDFRSF
EHNFEVNAFI YDVETALQMR EIFLQDQRDA VRVLLKNWRK RSWYRKAAES LVRLLAPLL
//