ID A0A091L9W4_CATAU Unreviewed; 705 AA.
AC A0A091L9W4;
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:KFP52647.1};
DE Flags: Fragment;
GN ORFNames=N323_04826 {ECO:0000313|EMBL:KFP52647.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP52647.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP52647.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP52647.1};
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; KL308677; KFP52647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091L9W4; -.
DR Proteomes; UP000053745; 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:UP000053745};
KW Transferase {ECO:0000313|EMBL:KFP52647.1}.
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:KFP52647.1"
FT NON_TER 705
FT /evidence="ECO:0000313|EMBL:KFP52647.1"
SQ SEQUENCE 705 AA; 79382 MW; 99DFD5ECD7902A0E CRC64;
FLALKIANVN WQFKLNKAAH HTSDYSSTEA ILRRGQAFNI TLNLQTTVQS GDNFTFIAST
GPSPAESQQT KAIFNLSEEG PSGWSATQEP SEPGCMNFTI FSPANAVIGR YKLKLQIVCG
NKVSSMLLGQ FVLLFNPWCP NDDVYMANEK ERWEYVLNDS GIIFQGLEKY IQQEAWNYGQ
FEEDILDISL AILDRSLNHR QDPAVDVSNR NNPVYVSRVI SAMVNSNDEK GVVEGKWNGK
YCSGTNPLQW SGSVTILRKW YRGRYKPVRY GQCWVFAGVM CTVLRSLGIP TRVITNFNSA
HDRNINLSID KYIDISGRTL HLTEDSVWNF HVWNESWFIR RDLGSFYDGW QVLDATPQER
SKGIYQCGPA STRAIKEGDV NLDYDSSFVF AAVNADYVTW IHYSNKRKER IYSDTRKIGK
FISTKAVGTN SRVDITANYK YPEGSLKERQ VYKKALKLLG VRSTGKRTKI TRPRRPSSVA
WRQNMTQPAQ KPSISGKLIL DASPVIGQDI LLTLALRNLI SDFKTVKVKL RASAILYTRK
PKAEILQLSR SVKLGSEEVK EISFKISYSQ YKNSLMDDRK ILVTAVCETK QGASLLVEKD
IVLQDPSLTI KVLGPTAVDK AVNVQVTFTN PLSEVVTDCV LRAEGSGLLR EQLRINVARM
APMESSTVQF EIIPYKSGIR QLQVDLVCIH FSDIKGFVML DVAPA
//
