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Database: UniProt
Entry: A0A091P4D3_9PASS
LinkDB: A0A091P4D3_9PASS
Original site: A0A091P4D3_9PASS 
ID   A0A091P4D3_9PASS        Unreviewed;       701 AA.
AC   A0A091P4D3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 30.
DE   SubName: Full=Protein-glutamine gamma-glutamyltransferase 6 {ECO:0000313|EMBL:KFP86420.1};
DE   Flags: Fragment;
GN   ORFNames=N310_12903 {ECO:0000313|EMBL:KFP86420.1};
OS   Acanthisitta chloris (rifleman).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC   Acanthisitta.
OX   NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP86420.1, ECO:0000313|Proteomes:UP000053537};
RN   [1] {ECO:0000313|EMBL:KFP86420.1, ECO:0000313|Proteomes:UP000053537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP86420.1};
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; KK844544; KFP86420.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091P4D3; -.
DR   Proteomes; UP000053537; 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:UP000053537};
KW   Transferase {ECO:0000313|EMBL:KFP86420.1}.
FT   DOMAIN          265..357
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          466..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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:KFP86420.1"
FT   NON_TER         701
FT                   /evidence="ECO:0000313|EMBL:KFP86420.1"
SQ   SEQUENCE   701 AA;  78952 MW;  5DC97A493079D384 CRC64;
     FLAPKITSVN WQSKLNKAAH HTSDYSSTKA ILRRGQAFSI TLNLKTPVQP WDSFTFIAST
     GPSPAESQQT KAIFTLSEEA ECGWSAAREP GEPDCMNITI LSPADAVIGR YKLKLQIVSG
     NKVSSKSLGQ FVLLFNPWCP DDDVYMAKEK EREEYVLNDS GIIFQGLEKD IQEEAWNYGQ
     FEEDILDISL AILDRSLNHR EDAAADVSNR CSPVYVSRVV SAMVNSNDEK GVVEGKWTGK
     YRSGTNPLQW SGSVSILRKW YRTRYRPVRY GQCWVFAGVT CTVLRCLGIP TRVITNFNSA
     HDKNINLSID KYVDTSGKTL HLSEDSVWNF HVWNESWFIR RDLGSFYDGW QVLDATPQEK
     SKGIYQCGPA STRAIKEGDV DLDYDSPFVF AAVNADYVTW IYHSKKRKER IYSDTRRIGK
     CISTKAVGTN SRVDVTANYK YPEGSLKERK VYKKALKLLG VRRTGKKPKI TRPRRPFSRP
     GRQPAQTPSI SGKLSLDESP VIGQDILLTL ALRNLISDFK TIKVKLRASA VLYTRKPKAD
     ILELYRTIKL GSEEAKEISF RISYSQYKNS LMDDRKILVT AVCQTKKGAS LLIEKDIVLQ
     DPFLTIKVLG PAVVHEPVNV EVTFTNPLSD VVTDCVLRAE GSGLLREQLR INVARMDPME
     SSTVQFEIIP YRSGTRQLQV DLVCIHFSDI KGFVMLDVAP A
//
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