ID A0A2K8L8L5_9PROT Unreviewed; 935 AA.
AC A0A2K8L8L5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative spermidine synthase with an N-terminal membrane domain {ECO:0000313|EMBL:ATX82589.1};
GN ORFNames=Ga0123462_1742 {ECO:0000313|EMBL:ATX82589.1};
OS Mariprofundus ferrinatatus.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=1921087 {ECO:0000313|EMBL:ATX82589.1, ECO:0000313|Proteomes:UP000231637};
RN [1] {ECO:0000313|EMBL:ATX82589.1, ECO:0000313|Proteomes:UP000231637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP-8 {ECO:0000313|EMBL:ATX82589.1,
RC ECO:0000313|Proteomes:UP000231637};
RA McAllister S.M., Kato S., Chan C.S., Chiu B.K., Field E.K.;
RT "Isolation and genomic insights into novel planktonic Zetaproteobacteria
RT from stratified waters of the Chesapeake Bay.";
RL Submitted (DEC-2016) 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}.
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DR EMBL; CP018800; ATX82589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8L8L5; -.
DR KEGG; mfn:Ga0123462_1742; -.
DR OrthoDB; 5287313at2; -.
DR Proteomes; UP000231637; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat 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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43317:SF9; POLYAMINE AMINOPROPYLTRANSFERASE 2; 1.
DR PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR Pfam; PF13432; TPR_16; 2.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51006; PABS_2; 1.
DR PROSITE; PS50005; TPR; 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}; Reference proteome {ECO:0000313|Proteomes:UP000231637};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
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 35..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 544..661
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT REPEAT 797..830
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 935 AA; 103460 MW; 6E5D3054AB154BD5 CRC64;
MRRNLFFGLM LASGLAGISY EILYGRILGN LIGDQFAVSA AILITFLLGI GVGSRYAWRL
WPWLWLIEAA IGICGAGFVL GGDLIDQLLY AGIPFVPSGL SGTILICIML LIVPAFLIGC
SVPLFAGYMS RLFSGAVFSG VYAVYNVGAA LTALLIEYLL IRWLGITGAT LGFVAVNIVI
ALLLKVAFAD VAQPPALSDQ GRLRLSPRRW QALIPVSMAS AVFQLFMIKL AEMLLGPFRE
SFALVLSIIL LGIAAGSMLV RSFGVRFHTL LLAAMAGLLL LIVTVEPVAY LYAGYYEQAS
ENYITSVLLK WSVLALLMGI PAIAFGATIP ALLGRKRGDV SRESGHLLYV ASLANVTGFL
LMVFVLHRYL DYGIQLVMIA LLVALSWLMY ARLNIQAVTV TLLLLVPMML FEKVKWDEDL
LYVSYTKFRA VDKLERARKE FDFPEKFKGY QDVFSINWIN GTPYFFINGY TSIPLDSPSE
KVVGALSSIH APGLKRALVL GLGSGATASV VGEMFEATDV VEINPVVREN LFRMRKWNLE
IESNPRVNII VDDAIHFSKA SDESYDLILN TVTTPLYFSS AKLYTQDFFD VVKKRLRPDG
VYVTWMDGRV GDRGADIILN TIAGSFNYCA IFYIKSSYFM LIASDKPVLP SQVTSIAANK
KLREHFLKEY GLLVEWMPYQ LLNSRAFDLV GNAGLPLNRA DYPALEFEMA KLSSRGIGEF
KLRLLDEMGM HHFDEASFGQ SVKFSAAVAR QADIMLGDSS ITRRFHAVAE GLDGKTLSLE
MAAHREYVEA VVEAGNVDAL HQYGYKLMRK GRYGLALEVF RQVVLLDANH NNSNFNIAAC
YEYLGNYPLA LSYYQKELSV DAGDFDATYR IGRVYVKSKQ YVKAVGYLQS ILEGAGASYH
GRIYHYLGRA YEGLGRDKDA EKAYEKAERA TASGN
//
