ID A0A5A9PG35_9TELE Unreviewed; 380 AA.
AC A0A5A9PG35;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 05-FEB-2025, entry version 15.
DE SubName: Full=Spermine synthase {ECO:0000313|EMBL:KAA0720121.1};
GN ORFNames=E1301_Tti008252 {ECO:0000313|EMBL:KAA0720121.1};
OS Triplophysa tibetana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Nemacheilidae; Triplophysa.
OX NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0720121.1, ECO:0000313|Proteomes:UP000324632};
RN [1] {ECO:0000313|EMBL:KAA0720121.1, ECO:0000313|Proteomes:UP000324632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0720121.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA0720121.1};
RX PubMed=30977968;
RA Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA Wang W., Yang R.;
RT "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT to the harsh high-altitude environment of the Tibetan Plateau.";
RL Mol. Ecol. Resour. 19:1027-1036(2019).
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:KAA0720121.1}.
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DR EMBL; SOYY01000006; KAA0720121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A9PG35; -.
DR Proteomes; UP000324632; Chromosome 6.
DR GO; GO:0016768; F:spermine synthase activity; IEA:InterPro.
DR GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro.
DR FunFam; 2.30.140.10:FF:000005; Spermine synthase; 1.
DR FunFam; 3.30.160.110:FF:000002; spermine synthase; 1.
DR Gene3D; 3.30.160.110; Siroheme synthase, domain 2; 1.
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 InterPro; IPR040900; SpmSyn_N.
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 Pfam; PF17950; SpmSyn_N; 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:UP000324632};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 119..379
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 293
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 380 AA; 42990 MW; 6F33E40CD3F79E0F CRC64;
MAVRHYTLDL KLRAPADVSA TVRGLQSIFQ EQEMTETVHD SEGHGYLATF VGKNGRFAIL
RMHSHGLLTF DLQCLEGDEE AQVDNLLNAL EKKLKTLLDG NIQRIKRLPA LVRGSDVDRY
WPTADGRLME YDIDEVVYEK DSDYQNIKIL HSRQFGNMLI LNGDVNLAES DQPYTEAIMG
SGKENYAGKE VLILGGGDGG ILHEAVKLKP KMITMVEISF MRITSTTVAD HQSVPVYIDE
LVINGCRKHM RKTCGNVLDN LKGDCYEILV QDCVPVLKKF VEQGRMFDYV INDLTAVPIS
TAPEEDSTWE FLRLILDLSI RVLRPSGKYF TQGNCANLTD ALSEYENLLG RLSCKVDFSK
EVVCVPSYME LWVFYTIWKK
//
