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Database: UniProt
Entry: A0A367L6Y7_9HYPO
LinkDB: A0A367L6Y7_9HYPO
Original site: A0A367L6Y7_9HYPO 
ID   A0A367L6Y7_9HYPO        Unreviewed;       588 AA.
AC   A0A367L6Y7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=PABS domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L249_8667 {ECO:0000313|EMBL:RCI10193.1};
OS   Ophiocordyceps polyrhachis-furcata BCC 54312.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI10193.1, ECO:0000313|Proteomes:UP000253664};
RN   [1] {ECO:0000313|EMBL:RCI10193.1, ECO:0000313|Proteomes:UP000253664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI10193.1,
RC   ECO:0000313|Proteomes:UP000253664};
RX   PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA   Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA   Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT   "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT   pathogenicity and host specificity in insect fungi.";
RL   BMC Genomics 16:881-881(2015).
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:RCI10193.1}.
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DR   EMBL; LKCN02000013; RCI10193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367L6Y7; -.
DR   Proteomes; UP000253664; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; NF037959; MFS_SpdSyn; 1.
DR   PANTHER; PTHR43317:SF9; POLYAMINE AMINOPROPYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR   Pfam; PF01564; Spermine_synth; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253664};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        53..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  64777 MW;  353EBD2DECA1C51B CRC64;
     MSSKRTTTTP DMAAKRSSTA AGGFTPEHFE AELKDLAAKA RDDSSGKHVV EQLALYAKAV
     VLLALLGIYS VVSPLNLSPV YGTLPASLWH PQLLMIGCFI GWAGNVAFRN LLPVKTAHLL
     PLVALYIPTM QWFLFGYSSL LGPRWAPIVT ESLTFVPLSA LTVAAVADLV EGTRLPLLPG
     FVADAAPGLG SWAWLKFVEL LAGRHLPPNM GRFFLLTRIG LELMLGGLYA LFARSRLLLY
     VLPPLLHTLF LNAHLASPAA TSSLVSSMLS DNWLLLDRRE SVTGYVSVLQ SMEQGFRAMR
     CDHSFLGGDW IGERGRTLSE PIYGVFAMLE AVRLVERASP LPDQEARALV VGLGVGTMPS
     ALVTHGINTT VVEIDPVIYE FAVKYFDLKE NNAPVLEDAV SYTSALAAAA PESYDYIIHD
     VFTGGAEPVQ LFTLEFIQGL HKLLKPDGVI AINYAGDLLL PAPAVIFRTI KRVFPTCRVF
     REVPLDAKAI ESDGADFANM VIFCTKSDAP LMFRKPTAAD YLESLTRKQF LRLDHEMLEA
     EFLSTYEDDD TILRRNDTSA VEKWHEKSAL GHWAVMRRML PASVWERW
//
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