ID   P91590_CIOIN            Unreviewed;       766 AA.
AC   P91590; A0A1W2VNA7;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 2.
DT   08-NOV-2023, entry version 109.
DE   SubName: Full=Transglutiminase {ECO:0000313|EMBL:CAA71263.1};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|EMBL:CAA71263.1};
RN   [1] {ECO:0000313|EMBL:CAA71263.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9187361; DOI=10.1016/S0014-5793(97)00342-6;
RA   Cariello L., Ristoratore F., Zanetti L.;
RT   "A new transglutaminase-like from the ascidian Ciona intestinalis.";
RL   FEBS Lett. 408:171-176(1997).
RN   [2] {ECO:0000313|EMBL:CAA71263.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Cariello L.;
RL   Submitted (SEP-1998) 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; Y10212; CAA71263.1; -; mRNA.
DR   RefSeq; NP_001027712.1; NM_001032540.1.
DR   AlphaFoldDB; P91590; -.
DR   GeneID; 445739; -.
DR   KEGG; cin:445739; -.
DR   CTD; 7052; -.
DR   OrthoDB; 5344745at2759; -.
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; IPR036238; Transglutaminase_C_sf.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   PANTHER; PTHR11590:SF40; HEMOCYTE PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
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.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2}.
FT   DOMAIN          340..432
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   ACT_SITE        348
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        406
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         469
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         471
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         519
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         524
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   766 AA;  87194 MW;  7F90D921D87FDD1D CRC64;
     MSRFRRRWFV IDAENAEEVN EFLDEHPRFL GEYIDRNPHL LDNYVIDNVD EETIQKWLDK
     VSGPAPTEVL QILRVNYKKE TNCVDHHTDK YIHNSLVVRR ATTFDLGLVF KNRNYRPAKD
     DIVLEFTIGS DPTIKNETKI RVPVGDSLQG SKWTCMKINE DEVTKEVTLQ VNIPPDAIIG
     RYKLTVEVAT ELKDGRQKER KVKPDIVVLF NPFKPADPVY MESSVEREEY VLNDTGRIYV
     GQWYRIGAKD WLFGQFEEGI LDIALKLLRE HTNAQKNATK SLKKRASPAY CSRLLSAMVN
     CNDDNGVLWG RWDGKYEEGV KPTTWSGSVA ILKQWNRTKM NPVKYGQCWV FSGLLTTVLR
     ALGIPARSIT NFNSAHDTEY NMTIDKFLTE DGESAEGTGD SIWNFHVWNE GFFRRPDLPK
     GYDGWQAVDA TPQEESSGVM QCGPAPIKAI KNGEIYIGSD TNFVFAEVNA DRVFWEVNDE
     GEVTKMVKND KRHVGRNIST KAVGSDERED VTLQYKFAEG SEEERVAFER AYAHGRKAPY
     HDKFVLEDEG NIKIDINPVG DVINGSDVSI SVKVTNAKGV DCDATITTVI HTMLNNEERK
     RLLKRSRGTR KIAAGKDDVE SFKFGFGDYG RHLSDENVIR VTTTVRVKET NKLYVDQYDI
     QIESPQCLEL ICADELKVRE YQPIRFKITN PLKVAMTSAV FSLQGSGISS GKSFEVPSPI
     EPGETYTSPE MEVRPYRSSR ATTILGDFDC NEIWNIKARK RVAVNF
//