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Database: UniProt
Entry: V8P2F3_OPHHA
LinkDB: V8P2F3_OPHHA
Original site: V8P2F3_OPHHA 
ID   V8P2F3_OPHHA            Unreviewed;       393 AA.
AC   V8P2F3;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Coagulation factor XIII A chain {ECO:0000313|EMBL:ETE68118.1};
GN   Name=F13a1 {ECO:0000313|EMBL:ETE68118.1};
GN   ORFNames=L345_06085 {ECO:0000313|EMBL:ETE68118.1};
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE68118.1, ECO:0000313|Proteomes:UP000018936};
RN   [1] {ECO:0000313|EMBL:ETE68118.1, ECO:0000313|Proteomes:UP000018936}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood {ECO:0000313|EMBL:ETE68118.1};
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA   Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT   snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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:ETE68118.1}.
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DR   EMBL; AZIM01001094; ETE68118.1; -; Genomic_DNA.
DR   AlphaFoldDB; V8P2F3; -.
DR   Proteomes; UP000018936; Unassembled WGS sequence.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR036238; Transglutaminase_C_sf.
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   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT   DOMAIN          139..240
FT                   /note="Transglutaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00927"
FT   DOMAIN          299..388
FT                   /note="Transglutaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00927"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   393 AA;  44216 MW;  D0358B2F0540BF29 CRC64;
     MSRHDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAIKH GHVCFQFDAP FVFAEVNSDV
     IYSKVMKNGS KVIQHIDKTQ IGTLILTKEM GSNKMKDITE HYKFQEGTEE ERLALETALM
     YGVKKSVAED ITSNTEVDMN VVIKDSVLGS DFNVTITFQN KTSRPYTVTA YISGNVVFYT
     GVPKTEFKND SFDVTLEPMK AETLEVLIES SEYMSELLEQ ASLHFFVTAR VNELQKILAR
     QKTVSLKIPQ LHLKREGYRQ GAQWPQKMGF WDAKEEGVIS PSLLLQAAME LMQSSATWQV
     PGEKVVGKEM TIIVEFPNPL KQNLTNVWVR LDGPGVLKPV SKLFREVPTN STLIWEDKYV
     PKQSGFRKLI SSLNCDALRH VYGELDINIQ SAE
//
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