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Database: UniProt
Entry: C4A099_BRAFL
LinkDB: C4A099_BRAFL
Original site: C4A099_BRAFL 
ID   C4A099_BRAFL            Unreviewed;       257 AA.
AC   C4A099;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=PABS domain-containing protein {ECO:0000259|PROSITE:PS51006};
DE   Flags: Fragment;
GN   ORFNames=BRAFLDRAFT_257362 {ECO:0000313|EMBL:EEN41780.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN41780.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN41780.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN41780.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000256|ARBA:ARBA00007867}.
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DR   EMBL; GG666795; EEN41780.1; -; Genomic_DNA.
DR   RefSeq; XP_002585769.1; XM_002585723.1.
DR   AlphaFoldDB; C4A099; -.
DR   STRING; 7739.C4A099; -.
DR   eggNOG; KOG1562; Eukaryota.
DR   InParanoid; C4A099; -.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0016768; F:spermine synthase activity; IBA:GO_Central.
DR   GO; GO:0006597; P:spermine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 2.30.140.10; Spermidine synthase, tetramerisation domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR030374; PABS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR035246; Spermidine_synt_N.
DR   InterPro; IPR037163; Spermidine_synt_N_sf.
DR   InterPro; IPR015576; Spermine_synthase_animal.
DR   PANTHER; PTHR46315; SPERMINE SYNTHASE; 1.
DR   PANTHER; PTHR46315:SF1; SPERMINE SYNTHASE; 1.
DR   Pfam; PF17284; Spermine_synt_N; 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   Polyamine biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00354};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00354}.
FT   DOMAIN          14..255
FT                   /note="PABS"
FT                   /evidence="ECO:0000259|PROSITE:PS51006"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EEN41780.1"
SQ   SEQUENCE   257 AA;  29620 MW;  897C488AA6D01300 CRC64;
     LSRLPFLKRG MRLDPYITTT SEQIVEYDFD RVVYEENSPY QNIKILHSPQ YGNLLLLDDD
     QNLAESDVAY TYAMTGNGRE DFTDKDVLIL GGGDGGILYH LLQQSPKFVT MLEISFLYQM
     VIDAATKYLR GICHDCFDSL SGDNYLVRVE DCVPVLEQYA RDGRTFDYVI NDLTDIPISQ
     EPTDDHLDLP QKILDLSLKV LKTSGKYWTH GANTNDVPQK FEEQLKQLPK PVDFLKEVIA
     IPSYHELWVF YTIWKKS
//
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