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Database: UniProt
Entry: A0A1F9EZ68_9DELT
LinkDB: A0A1F9EZ68_9DELT
Original site: A0A1F9EZ68_9DELT 
ID   A0A1F9EZ68_9DELT        Unreviewed;      1049 AA.
AC   A0A1F9EZ68;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=PABS domain-containing protein {ECO:0000259|PROSITE:PS51006};
GN   ORFNames=A2138_00120 {ECO:0000313|EMBL:OGQ12295.1};
OS   Deltaproteobacteria bacterium RBG_16_71_12.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1797848 {ECO:0000313|EMBL:OGQ12295.1, ECO:0000313|Proteomes:UP000176731};
RN   [1] {ECO:0000313|EMBL:OGQ12295.1, ECO:0000313|Proteomes:UP000176731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000256|ARBA:ARBA00007867}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00354}.
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:OGQ12295.1}.
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DR   EMBL; MGQY01000337; OGQ12295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F9EZ68; -.
DR   Proteomes; UP000176731; 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   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.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|PROSITE-
KW   ProRule:PRU00354};
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        35..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        220..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        322..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        367..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          540..708
FT                   /note="PABS"
FT                   /evidence="ECO:0000259|PROSITE:PS51006"
SQ   SEQUENCE   1049 AA;  109559 MW;  15D1940B6A49B575 CRC64;
     MICALVFGSG LCALIYQAMW FRALRTIFGA STPSNAAVLA IFMAGLGLGG ALFGRRAERT
     TRPLALYANL ELGVAISAAL SPFLVDGVRF VYFAAGGSSV LGSTGATIAR LVLATIALGV
     PATLMGGTFP AVARAVITRD DAGRRTLALV YGANTLGAVA GTALATFLLL DVLGVRQSIW
     AACAINALVA MAARSLSQGA AGHVPAAATP PAPSSSSRPV LFAAFATGFA FFLLELVWYR
     MCSPLLGGST YSFGVVLVLA LFGVGIGGAL YAFFGPRAAT PGHFAVTCAL EAALLLVPFA
     LGDDVARFAF HARELGQATF GGLALSWIAT AAILVLPAAI VAGWQFPLLL ALKGRGDEGA
     GKDSGDVYAA NTLGAIVGSL LGGFGALPWL GATGAWRLAA FVLIAAGTWF ALRALAAGGT
     GPAGVVAEPA GTATGERVRF AAFLSLAAIT IAIAFGATGP TSMWRHSPIG AGRADLHAPT
     WNARMQRSND GRRFVLESSD GVESSIAFKA TTGISLFVSG KSDGGTIGDA PTQVGSGVLA
     ALLHGNVKNA FVIGLGTGQT AGWLGMLPGI ERVDVVEIEP NVLRFGEVCA DTNGDVMKNP
     KVHVIVGDGR EALATTRETY DLILSEPSNP YRAGVSSFYA TELYQDAYAR LKDDGIFAQW
     LQAYEIDSVA VQTAVATLSA TFPEISAWRL TPGDMFLLAT KRPQLIDVER VRALLDVEPY
     RTVALRVLRA HGVEGVLALH QASPPFMRRL ASSSPTINSD DRPTLELSFA RNVGRSSENP
     LGAIFALAQP RGEHVPALTA PVVPSLVEMQ RARPWIAVGR TVSAGVSGDP VEAAWTAGEF
     ERAIALMHAA DAEGQTPEPR VDDATGRMIR LHLRALDTGA VDEAAIDALA HDLPCDAAVV
     RLEAANRRGE PSAAHVVAAL AAARADPWCN VRLLRSGLRR LAVLDGIAPA AAASMLDAFV
     AGRFAGYTCE VDRVQVAGAL ARRAGFPPKC VEAYGGIEPY PFWERVWLED RLACYARHAP
     DRVPIAEREL RDMITHQAAS LADLMSTPP
//
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