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Database: UniProt
Entry: A0A094HSM3_9PEZI
LinkDB: A0A094HSM3_9PEZI
Original site: A0A094HSM3_9PEZI 
ID   A0A094HSM3_9PEZI        Unreviewed;       582 AA.
AC   A0A094HSM3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=PABS domain-containing protein {ECO:0000259|PROSITE:PS51006};
GN   ORFNames=V501_01245 {ECO:0000313|EMBL:KFZ18405.1};
OS   Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ18405.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ18405.1, ECO:0000313|Proteomes:UP000029315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000256|ARBA:ARBA00007867}.
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:KFZ18405.1}.
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DR   EMBL; JPKD01000407; KFZ18405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HSM3; -.
DR   HOGENOM; CLU_017511_2_0_1; -.
DR   Proteomes; UP000029315; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR030374; PABS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; NF037959; MFS_SpdSyn; 1.
DR   PANTHER; PTHR43317:SF12; POLYAMINE AMINOPROPYLTRANSFERASE; 1.
DR   PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR   Pfam; PF01564; Spermine_synth; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polyamine biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00354};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00354}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        112..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          364..494
FT                   /note="PABS"
FT                   /evidence="ECO:0000259|PROSITE:PS51006"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        414
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ   SEQUENCE   582 AA;  64172 MW;  AC2F2E6C44B2E539 CRC64;
     MAKPKSQKRE ANVSNASPPL TQENFEKELK ELAKKAKEET FFNHAVDWAG TTVRAVVILA
     LAAASSSVSQ LTLSPVYGAI PASIWHDKLV NAACFLGWSG SFWLRRNVRW RLIDLLPLIA
     FYIPAVQYFL FNYSNTFGAT YGPLITELLT VAPLLLFSAS AVGLVLEEFG ITGKWQSVPG
     IASFVFLKIT SAWSANVIQS TSYKSVLLSR VSWQVQLAAS YALLAPSKLL LYAVPALLHT
     AIFNAHSQTP WATQALNLSL QAEGYRLIAR QDSNTGYISV LESVSNQFRV LRCDHSLLGG
     VWTMDQSHNP VVGEPVYAIF TMLEAVRLIE APVSVPDSEA QALVIGAGIG TSPGALMAHG
     INTTIVEIDP VVLEFAVKYF DLAPNHHAVI DDAVHYAAQV ANDTTQRYDY IIHDVFTGGA
     EPIALFTDEF LRNLHRALKP DGVIAINYAS DLLQPSTHLI IRTVLAIFPS CRIYRETATP
     TAAELLAAGQ DFTNMVLFCR ARSEAPITFR EPVERDFLRS GARKAYLVPK HEILRGEFDL
     EDMGDVLRAN DTATLEETQR KSAVGHWNVM RTVVPGKVWE LW
//
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