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Database: UniProt
Entry: A0A0T6BAH3_9SCAR
LinkDB: A0A0T6BAH3_9SCAR
Original site: A0A0T6BAH3_9SCAR 
ID   A0A0T6BAH3_9SCAR        Unreviewed;       719 AA.
AC   A0A0T6BAH3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   08-NOV-2023, entry version 23.
DE   RecName: Full=Transglutaminase-like domain-containing protein {ECO:0000259|SMART:SM00460};
DE   Flags: Fragment;
GN   ORFNames=AMK59_767 {ECO:0000313|EMBL:KRT84321.1};
OS   Oryctes borbonicus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC   Scarabaeidae; Dynastinae; Oryctes.
OX   NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT84321.1, ECO:0000313|Proteomes:UP000051574};
RN   [1] {ECO:0000313|EMBL:KRT84321.1, ECO:0000313|Proteomes:UP000051574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB123 {ECO:0000313|EMBL:KRT84321.1};
RC   TISSUE=Whole animal {ECO:0000313|EMBL:KRT84321.1};
RA   Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA   Roedelsperger C.;
RT   "Draft genome of the scarab beetle Oryctes borbonicus.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000459-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000459-2};
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
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:KRT84321.1}.
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DR   EMBL; LJIG01002619; KRT84321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6BAH3; -.
DR   OrthoDB; 5344745at2759; -.
DR   Proteomes; UP000051574; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   InterPro; IPR023608; Transglutaminase_animal.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR036238; Transglutaminase_C_sf.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11590:SF69; RE08173P; 1.
DR   Pfam; PF00927; Transglut_C; 1.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   PIRSF; PIRSF000459; TGM_EBP42; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051574}.
FT   DOMAIN          286..382
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        379
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         419
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         421
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         469
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         474
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRT84321.1"
SQ   SEQUENCE   719 AA;  82166 MW;  DC62630C79691A40 CRC64;
     DETVDLPYID ADKESDILIV REIDPCIAEN GQTHHTGKYE LMTRAVERQL VVRRAQHFKI
     VLTLSRPYKE DMDGISFIFF VEDEQKPSLG QGTLVAVPLL KRADQKSTGW SAIVDKVDDA
     LLTVLITPAH DCIVAKWRVE VDTKVIDDGA YRYSWDTFIY IIFNPWNKKD QAYMKSDEWR
     DEAILNDVGL IWRGTFDTVR PTIWKYSQFD ENILECVLYL IGHVGKLSGK ARSDPVHISR
     ILAATVNNID DEGVLMGNWS NNYSGGTAPT KWMGSADILQ TYYKKKKPVK FAQCWVFAGV
     LTTTCRAIGL PSRVVTNYSS AHDTHSSLTV DYFMDADGCG MRDLNSDSIW TFHVWNEVWM
     RRPDLSSRTE EYDGWQVVDA TPQEPSEKMY RCGPASVEAC KQGEVLRPYD TSFLFAEVNA
     DKVYWRYDGK TQPLKLLGKD IQGIGKLICT KAAGRFERED ITDDYKHTEK SKEERVTMLK
     ALKQAESIFS RYYINEDFSD IHFRLRLQDS IQIGDPFTVV LEMKNRTRIK DYNVNITLRV
     ESIHYIGKIK DLVKKDEYKV MVKMESIHEV KLDVKYEEYC KKLTEQGAFV MSCMATVADT
     KFDFFTQNDF KVTKPNIKIT LPDQVIQGQE TIADVELENP LPVPLKKAEF LIDAPGKKQF
     KIKIKGAVLD KQKAVAQFKF TPPDVGKQTI AAKFTSKELS DVDGFVNFVV SQKVEENGA
//
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