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Database: UniProt
Entry: B3RYC4_TRIAD
LinkDB: B3RYC4_TRIAD
Original site: B3RYC4_TRIAD 
ID   B3RYC4_TRIAD            Unreviewed;       491 AA.
AC   B3RYC4;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Macro domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIADDRAFT_56509 {ECO:0000313|EMBL:EDV24574.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV24574.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV24574.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV24574.1,
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 GDAP2 family.
CC       {ECO:0000256|ARBA:ARBA00008355}.
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DR   EMBL; DS985245; EDV24574.1; -; Genomic_DNA.
DR   RefSeq; XP_002112464.1; XM_002112428.1.
DR   AlphaFoldDB; B3RYC4; -.
DR   STRING; 10228.B3RYC4; -.
DR   EnsemblMetazoa; TriadT56509; TriadP56509; TriadG56509.
DR   GeneID; 6754117; -.
DR   KEGG; tad:TRIADDRAFT_56509; -.
DR   CTD; 6754117; -.
DR   eggNOG; KOG2633; Eukaryota.
DR   HOGENOM; CLU_026877_0_0_1; -.
DR   InParanoid; B3RYC4; -.
DR   OMA; VHLFRYV; -.
DR   OrthoDB; 1105329at2759; -.
DR   PhylomeDB; B3RYC4; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   CDD; cd02905; Macro_GDAP2-like; 1.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR035793; Macro_GDAP2.
DR   PANTHER; PTHR11106; GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED; 1.
DR   PANTHER; PTHR11106:SF72; GANGLIOSIDE-INDUCED DIFFERENTIATION-ASSOCIATED PROTEIN 2; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   Pfam; PF01661; Macro; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT   DOMAIN          39..220
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          321..475
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
SQ   SEQUENCE   491 AA;  56324 MW;  070C075B06D376A6 CRC64;
     MAASIDPLGV AKNLIEVSVL KTWHESIVPS YPDIQPSKQS PFQYCSNINQ KLVLWTGDIT
     TLKVDAIVNP TNENLSVMSP INQKIFEIAG PSLHRDIRDE IGKCATGESK LSKGYNLPSR
     YVIHTVGPKY NPRYLSAVEN ALYRSYRSSL LIAGEYKVRS IAIPTVHLHQ RGFPVSEGAH
     IALRTVRRYL EHQSCTLETV ILILDDTEME IYKRLAVLYF PRSNEEEAYA FENLPEDIGN
     EFGEPTIKER SIRIQDKIVN SEDEKTFTKS DSAAFRAFSK MAGDHDIARS ELIQSKSKKT
     SQLQQNAKRY QTWLKLARTL DTKDIIKLKA LYKSGVDQYG RSVIVFIGNN FPAHLTDLNK
     AISYYAYLMD DMVDNDYIAI YFHTLTNAEQ RPPANFLKLV YQTLDPKYHK NLKAFYVVHP
     SWWLKWSFWS FCTFTAPELK SKLQYIDDLK DLLKFIPRDQ FSIPQYLFDE NRKMNGNSVT
     TPNAASQPDE L
//
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