ID A0A091W2D9_NIPNI Unreviewed; 735 AA.
AC A0A091W2D9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Coagulation factor XIII A chain {ECO:0000313|EMBL:KFR09215.1};
GN ORFNames=Y956_11888 {ECO:0000313|EMBL:KFR09215.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR09215.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFR09215.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR09215.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL411540; KFR09215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091W2D9; -.
DR STRING; 128390.A0A091W2D9; -.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR Proteomes; UP000053283; 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:SF42; COAGULATION FACTOR XIII A CHAIN; 1.
DR PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 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:UP000053283}.
FT DOMAIN 314..407
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 322
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 381
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 404
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 735 AA; 83915 MW; 82CEE23027DDD1FE CRC64;
MSETTNTNEE KKKPPLNGRR ALPPNNSNDE ENEVPEMEAF GLIPRGFNPK DYLRVVDIHM
FKEPHEINKQ QHHTDKYYSP KLIVRRGQPF QIQIDFNRPY KPETDQFWLE YLIGRYPQQN
KGTYIPILVT DVLQPGKWGA KITHKENNSI RLSIMSSATC IVGKFRLYVA VWTPFGILRT
HRNSTTDTYI LFNPWCQQDA VYLDDEKERE EYVLNDVGIV FHGNINEIKL RSWSYGQFEE
NILDACLFLM DKAELELSGR GNPIKICRVA SAVINSRDDN GVIAGSWDNT YTYGVAPSAW
TGSVDILLEY YSSKQPVRYG QCWVFAGVFN TFLRCLGIPA RLVTNYSSAH DNNGNLRLDF
FLDDEGKVDT KLTKDSVWNY HCWNEAWMTR PDLPVGFGGW QVVDGTPQET SDGMYRCGPA
SVQAIKHGHV CFQFDAPFVY AEVNSDIVYS RREKNGTQVI EKIDTTHIGQ LIVTKEVGGD
GMMEITEEYK FQEGSQEERL ALETAVMYGV EKQTTQNIAY QPQTDVDMDF QVQKAVLGSD
FKVTITFRNK SRNYYTATTY LSGNIVFYTG VTKNEFKKCL FPFLFLPSAT SFDVVIKSSE
YLSDLLDQAS FHFFVTARIN ETGKILATQK ATVLEIPTLR IKTQGETVAG KEMSVTVEFT
NPLKQTLENV TLRLEGPGVL RTMKKEFRQI PTNSTLIWEV KCIPKRPGLR KLIASLNCDA
LRHVYGELNV QIQKP
//
