ID A0A3R7SK51_PENVA Unreviewed; 150 AA.
AC A0A3R7SK51;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 05-FEB-2025, entry version 14.
DE SubName: Full=Spermine synthase {ECO:0000313|EMBL:ROT64417.1};
GN ORFNames=C7M84_017651 {ECO:0000313|EMBL:ROT64417.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT64417.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT64417.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT64417.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT64417.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT64417.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:ROT64417.1}.
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DR EMBL; QCYY01003255; ROT64417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7SK51; -.
DR STRING; 6689.A0A3R7SK51; -.
DR OrthoDB; 5953636at2759; -.
DR Proteomes; UP000283509; 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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 64..150
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
SQ SEQUENCE 150 AA; 16702 MW; 658D5A8061F6B49E CRC64;
MTLSVKLYSN GLVTATVEYY TDQVNEHKIA NDHGRALEKQ LMAKFDCSVA KVLPAIKRAP
PVNPYFTSSD DRLLEYDTDG IVFEEQSKFQ KVQIYSTKSF GNLLVLDDLQ NLAEQDLPYT
HGLMNKDKED FAGKEILILG GGDGPFCGSC
//
