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Database: UniProt
Entry: A0A3D8QGN3_9HELO
LinkDB: A0A3D8QGN3_9HELO
Original site: A0A3D8QGN3_9HELO 
ID   A0A3D8QGN3_9HELO        Unreviewed;      1474 AA.
AC   A0A3D8QGN3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Protein SERAC1 {ECO:0000256|ARBA:ARBA00040991};
DE   AltName: Full=Serine active site-containing protein 1 {ECO:0000256|ARBA:ARBA00041701};
GN   ORFNames=BP6252_11957 {ECO:0000313|EMBL:RDW60574.1};
OS   Coleophoma cylindrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Coleophoma.
OX   NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW60574.1, ECO:0000313|Proteomes:UP000256645};
RN   [1] {ECO:0000313|EMBL:RDW60574.1, ECO:0000313|Proteomes:UP000256645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP6252 {ECO:0000313|EMBL:RDW60574.1,
RC   ECO:0000313|Proteomes:UP000256645};
RX   PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA   Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA   Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA   De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA   Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA   Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA   Xiong C., Yue Q., Zhang X.;
RT   "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT   Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT   basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT   Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT   and Morchella septimelata.";
RL   IMA Fungus 9:199-223(2018).
CC   -!- FUNCTION: Plays an important role in the phosphatidylglycerol
CC       remodeling that is essential for both mitochondrial function and
CC       intracellular cholesterol trafficking. May catalyze the remodeling of
CC       phosphatidylglycerol and be involved in the transacylation-acylation
CC       reaction to produce phosphatidylglycerol-36:1. May be involved in
CC       bis(monoacylglycerol)phosphate biosynthetic pathway.
CC       {ECO:0000256|ARBA:ARBA00037251}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the SERAC1 family.
CC       {ECO:0000256|ARBA:ARBA00038024}.
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:RDW60574.1}.
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DR   EMBL; PDLM01000015; RDW60574.1; -; Genomic_DNA.
DR   Proteomes; UP000256645; Unassembled WGS sequence.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR026003; Cohesin_HEAT.
DR   InterPro; IPR007111; NACHT_NTPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   PANTHER; PTHR48182; PROTEIN SERAC1; 1.
DR   PANTHER; PTHR48182:SF2; PROTEIN SERAC1; 1.
DR   Pfam; PF12765; Cohesin_HEAT; 1.
DR   Pfam; PF13646; HEAT_2; 4.
DR   Pfam; PF05729; NACHT; 1.
DR   SMART; SM00567; EZ_HEAT; 9.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50837; NACHT; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256645};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1474
FT                   /note="Protein SERAC1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017776055"
FT   DOMAIN          452..582
FT                   /note="NACHT"
FT                   /evidence="ECO:0000259|PROSITE:PS50837"
FT   REGION          33..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1474 AA;  166096 MW;  0EE30E37AA9390EA CRC64;
     MDLIIIILML ILLVAGLITV NFEHRKKNAN TRLATDPQAA SQQDHEPDQT LPPQRGVHLR
     QVYPDKTKET ETDIDIIAIH GLDTKSPETW TWVDQKNPTI RVNWLEDRAM LPSTVDRVRI
     FTCDWPADLL QPSKLIQMEF LELALRLSAG IQSRPPGPSS GASRDRPILF IASCLGGIML
     IKALVDAGKQ DNPLRRATRG IIFLATPFQG TSFEEVATWA VPCMEAWALV QRREVTKLLA
     SVKKLDLDAL VRNFTQLIKQ QDPPCEVFNF YEKRVTSLPS KIFPWLPTRL RQEKLLVDRV
     SATLEMVPDP LPLDQPHVLM NKFKGPECTD YKLVVGQVQR ILGNIRDGSP LEQADVWIRE
     KHYTEDRLKI DRLSGERLMM EQCYINLAIV EQPRVDAASS GEPGNQEISP TSSHSSLRAR
     LRVETPAEDI QVELGTLFDP RKGPNGLIAQ PKRIMIRGRA GVGKTTLCKK IIHDFQQGAW
     NDIFHRILWV PLRKLKTWNA DKYTLGQLFH HEYFPGSPNG KMLSEALWRD IDAGNGKKTL
     FILDGLDEVA GTFDPETNKH QLLITLLNQP NVVITCRPHG ALVSNLHPVS LELETVGFYP
     DQMNDYIEMA LQKRPRHEID EVQSFLKDHF LIQDLMRIPI QLDALCYTWD RDYRIDPQLQ
     TMTAIYHAIE HNLWKKDVVR LGKKDRGDPV TSSQIQSSSA PNVERLVRDE ILFLEGLAFT
     GIYSDVINFD IKQLEDIYET FKPENDFLLE KTLPNLSFLR TSDQSSEYKD QNYHFLHLTI
     QEYFAARYFV RCWKSGKEII CLKLNTGRSF QKEYPATDYL QEQKHNVQYD IVWRFVTGLL
     QGNGSDTQLP RFFYTIEKEP RDLLGPVHQR LIMHCLSEVV IQKEPPSFTP LRKQLEIRLS
     QWVLFECNST GHGSQLAREI ELPEQVLNKI LPNESKDISG LQIKVLRSIA DRNKQPLSIV
     RLANDSLTQS DVSLELKVVA LRILGNLYKG SSSNLGTIVA LLKNNEVYVR MAAVEALAKQ
     PALSPELLET IVALLKDKDS SVRKAAVSAL AKQQALSLEL LEAIVALFKD KYSFVREAAV
     NALAKQQALS PELLEAIVAL LKDNDMFVRM AAVDALAKQQ ALSLERLEAK VAHLKDNDMF
     VRMAAVDALA KQPALSLEPL EAIVALLKDN DMFVRRAAVD ALAKQQALSP ELLEAIVALL
     KDNDIFVRMA AVNALAKQPA LSPKFLEAIV AHLKDKDYSV RRVAVDALAK QPALSSELLE
     AIVALLKDNK ASVRSAAVNA LAKQPALSPE LLEAIVALLK DNEESVREAA LYALAKQPAL
     SPELLEAIVA LLKDNEESVR EAALYALAKQ PALSSELLEA IISLLKDNDM FVRRAAVDAL
     AKQPGLSLEL VGKDIESFYR SWVERSLLGY TSWYIMDKVS YIDMLDSRLY LEGKQDQLRV
     SIKEAQQHLC LKNGGLHGLW TYVSEDSSDS MSIA
//
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