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Database: UniProt
Entry: A0A091PES3_LEPDC
LinkDB: A0A091PES3_LEPDC
Original site: A0A091PES3_LEPDC 
ID   A0A091PES3_LEPDC        Unreviewed;       705 AA.
AC   A0A091PES3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   SubName: Full=Protein-glutamine gamma-glutamyltransferase 6 {ECO:0000313|EMBL:KFQ05866.1};
DE   Flags: Fragment;
GN   ORFNames=N330_10332 {ECO:0000313|EMBL:KFQ05866.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ05866.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ05866.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ05866.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KK672149; KFQ05866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091PES3; -.
DR   PhylomeDB; A0A091PES3; -.
DR   Proteomes; UP000053001; 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; IPR013808; Transglutaminase_AS.
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:SF50; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 6; 1.
DR   Pfam; PF00927; Transglut_C; 2.
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.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
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:UP000053001};
KW   Transferase {ECO:0000313|EMBL:KFQ05866.1}.
FT   DOMAIN          265..357
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         394
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         396
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         443
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         448
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:KFQ05866.1"
FT   NON_TER         705
FT                   /evidence="ECO:0000313|EMBL:KFQ05866.1"
SQ   SEQUENCE   705 AA;  79570 MW;  CDB4CA4E13EB1DF7 CRC64;
     FLALKIANVN WQSKLNKAAH HTSDYSSTEA ILRRGQPFNI TLNLQTTVQP GDNFTFIAST
     GPCPAESQQT KAVFNLLEED ASGWSATQEP SEPGCMNFTI FSPANAVIGR YKLKLQIVSG
     NKVSSTLLGQ FVLLFNPWCP NDDVYMANEK ERQEYVLNDS GIIFQGLEKY IQQEAWNYGQ
     FEEDILDISL AILDRSLNHR QDPAVDVSNR NNPIYVSRVV SAMVNSNDEK GVVEGKWNGN
     YCSGTNPLQW SGSVTILRKW YRGRYKPVRY GQCWVFAGVM CTVLRSLGIP TRVITNFNSA
     HDRNINLSID NYIDISGKTL HLTEDSVWNF HVWNESWFIR RDLGSFYDGW QVLDATPQER
     SKGIYRCGPA STRAIKEGDV NLDYDSSFLF AAVNADYVTW IHYSNKRKER IYSDSRKIGK
     FISTKAVGTN CRVDVTANYK YPEGSLKERQ VYKKARKLLG VRSTGKRTKI ARPRRRSSVA
     WRQNMAQPAQ KPSISAKLIL DAPPVIGQDI LFTLALRNLI SDFKTIKVKL RASAILYTRK
     PKAEILQLSR SIKLGSEEVK EISFKISYSQ YKNSLKDDRK ILVTAVCETT QEASLLVEKD
     IVLQDPFLTI EVLGPTVVHK AVNVQVTLTN PLSEVVTDCE LRAEGSGLLK EQLRINVARM
     APMESLTVQF EIIPYKSGTR LLQVDFVCIH FSDIKGFVML DVAPA
//
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