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
//