ID A0A026W319_OOCBI Unreviewed; 360 AA.
AC A0A026W319;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Spermine synthase {ECO:0000313|EMBL:EZA50418.1};
GN ORFNames=X777_10611 {ECO:0000313|EMBL:EZA50418.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA50418.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA50418.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867}.
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DR EMBL; KK107455; EZA50418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026W319; -.
DR STRING; 2015173.A0A026W319; -.
DR OMA; SGCLVEY; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR GO; GO:0016768; F:spermine synthase activity; IEA:InterPro.
DR GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro.
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; IPR030373; PABS_CS.
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; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Polyamine biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00354};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 104..360
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 360 AA; 40288 MW; 04EA8DF5D4E92D45 CRC64;
MVAHTVLLDF TVSSSVIADM EKRSGLKSAI ANVLAEHFTG LKPLIESNID GNLLILYTGP
RGSLITVRGY TEGLITLNIE YYKQDDQEAL LTFESEGAKG SGLERCKPAQ QAFTANERLL
EYDIDKLVFE ARSPYQKVQI VHSKSLGNLL VLDELQILQL ARDPFADMSE ADLIYTETLM
QRGKEDYAGK EIVILGGGDG GLLWELLKEK PKFVTMLEID DIVMKACSQH MRSICGDCLD
KRKGDNYEII VGDCVKALAH MIEEGRQFDY VFGDLTDIPI STTPHGDAWD FIRLILNSSV
KVLKPTGKYM THGNGASCPE SLKMYEEVLS QLCVPITFTK DRAFVPSFFE DWIFYQVSLK
//
