ID A0A1F3P048_9BACT Unreviewed; 533 AA.
AC A0A1F3P048;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=PABS domain-containing protein {ECO:0000259|PROSITE:PS51006};
GN ORFNames=A3G23_15030 {ECO:0000313|EMBL:OFY71119.1};
OS Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_37_12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797365 {ECO:0000313|EMBL:OFY71119.1, ECO:0000313|Proteomes:UP000176497};
RN [1] {ECO:0000313|EMBL:OFY71119.1, ECO:0000313|Proteomes:UP000176497}
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: 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:OFY71119.1}.
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DR EMBL; MEPC01000019; OFY71119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3P048; -.
DR STRING; 1797365.A3G23_15030; -.
DR Proteomes; UP000176497; 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; IPR036259; MFS_trans_sf.
DR InterPro; IPR030374; PABS.
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; SSF103473; MFS general substrate transporter; 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 16..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 321..450
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 533 AA; 59880 MW; 7D9046F92D9F841F CRC64;
MSKPLPRPAL PEKTSLFAIA FLEGAMVLSV EILGAKMLAP FFGTSLIVWS SVIGITLTSL
TAGYYFGGYL SKKQNPATIL FTVLLLATFT IVLMPTLAYS YIGSFSEWSI YTGSFFSALL
LLGPPLFLLG TTSPILIQVM TQSVTESGRL AGTLYAISTV GGILMTFLQG FLLVPLFGIS
IPLLFCALIL LITTLGILYT SRRLIYSLPV FLILLFQFNN LSNWDKPKRS TKVSIPYSSE
GLLGQLKVVD FEDPNSKNPL RHLLINGIGQ TRIINNPTAI SFWKYIHLLS VYSSLQKGKK
EALLFGFGAG SMSNELNRLG MHVDAVEIDE RMMGLAKKYF YFSDTATRFV VDDARHFIRT
EKKKYDLIIF DIANGEVQPS YVYTKECFTE VKNMLNENGL ILFEFQELMV PDRELVFPSI
CKTLKSTGYE PYYHLDSPNG LNDVMILASP QPIDFANLKK ENMTGCCAMQ PWVPALIEHP
FNPWKNELDN ARVFTDNQPM LDHLHAASLK SWRESMLAYV VRREMIEGYK LFK
//
