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Database: UniProt
Entry: B3S1W3_TRIAD
LinkDB: B3S1W3_TRIAD
Original site: B3S1W3_TRIAD 
ID   B3S1W3_TRIAD            Unreviewed;       569 AA.
AC   B3S1W3;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV23262.1};
GN   ORFNames=TRIADDRAFT_58361 {ECO:0000313|EMBL:EDV23262.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV23262.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV23262.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV23262.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; DS985247; EDV23262.1; -; Genomic_DNA.
DR   RefSeq; XP_002114172.1; XM_002114136.1.
DR   AlphaFoldDB; B3S1W3; -.
DR   STRING; 10228.B3S1W3; -.
DR   EnsemblMetazoa; TriadT58361; TriadP58361; TriadG58361.
DR   GeneID; 6755385; -.
DR   KEGG; tad:TRIADDRAFT_58361; -.
DR   CTD; 6755385; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   HOGENOM; CLU_000022_59_2_1; -.
DR   InParanoid; B3S1W3; -.
DR   OMA; KASYKWL; -.
DR   OrthoDB; 3031167at2759; -.
DR   PhylomeDB; B3S1W3; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR24096:SF426; BCDNA.GH02901; 1.
DR   PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT   DOMAIN          28..421
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          472..550
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   569 AA;  62743 MW;  BBBFB7DC2F6A6A60 CRC64;
     MTSVRSPYPD VHIPDNVSFF EYVTGNFKNF GNKPAMTDGI TGASYTFHQL DDAIKRVASA
     LVKRGLKKGE VVAIISPNCI EWPVLFFAVI SVGGIITTCN HGYKETELSS QLSNAGAVYL
     VAAKSSVRTV SKMRYKVRER FIIGDADGYT SYSELIRDDG SRFPSFVKIN SKTDICVLPY
     SSGTTGVSKG VMISHYNLVA NLEQTRPVRI RNRKNNCSLA VLPFYHIYGM VVIMSSCLRY
     GNHCVTLPGF EPKSFLRTIE KYKDSLLSTV VASMENIHIC SARKSYVRNI SVRDVSPSKV
     ARLSLVPPLA LFLLKSPLVD KYDLSSLEDA GSGAAPLGDE VMQQFLRKMK VKRFVQGYGM
     TEASPTITLV SPDENHNLGS VGRPVPNTQC KFIDPDSGKV LPPNVPGEIL VKGPQVMLGY
     LNRPKATAET IDKDGWLHTG DVGYYDENGI CYIVDRIKEL IKYKGYQVAP AELESLLKSH
     PDISDAAIIG IPDERAGEIP RAYIILKDSG NGKITTEKIQ EYVTSKVAPH KRLRGGIAIV
     TEIPKSASGK ILRRLIRDQY KKSIAKSKL
//
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